Ligand source activities (1 row/activity)



Get vendors


Ligands (move mouse cursor over ligand name to see structure) Receptor Assay information Chemical information
Sel. page Common
name		 GPCRdb
ID		 #Vendors

 Reference
ligand		 Fold
selectivity		 # Tested
GPCRs		 Species

 p-value
(-log)		 Activity
Type		 Activity
Relation		 Activity
Value		 AssayType

 Assay
Description		 Source

 Mol
weight		 Rot
Bonds		 H don

 H acc

 LogP

 Smiles

 DOI
10353365 90022 1 None 13 3 Human 10.1 pEC50 = 10.1 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL218710 90022 1 None 13 3 Human 10.1 pEC50 = 10.1 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
117972056 148911 0 None - 1 Human 9.4 pEC50 = 9.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 5 0 4 5.2 Fc1ccc(C2CC(Oc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)C2)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3883435 148911 0 None - 1 Human 9.4 pEC50 = 9.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 5 0 4 5.2 Fc1ccc(C2CC(Oc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)C2)cc1 10.1016/j.bmc.2016.11.018
117971665 149004 0 None - 1 Human 9.4 pEC50 = 9.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 415 5 0 4 5.8 FC(F)(F)c1c(O[C@H]2CC[C@H](c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884532 149004 0 None - 1 Human 9.4 pEC50 = 9.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 415 5 0 4 5.8 FC(F)(F)c1c(O[C@H]2CC[C@H](c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
117971685 148991 0 None - 1 Human 9.3 pEC50 = 9.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 387 5 0 4 5.0 FC(F)(F)c1c(OC2CC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884187 148991 0 None - 1 Human 9.3 pEC50 = 9.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 387 5 0 4 5.0 FC(F)(F)c1c(OC2CC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
1395 9306 15 None -7 4 Rat 9.2 pEC50 = 9.2 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
9837317 9306 15 None -7 4 Rat 9.2 pEC50 = 9.2 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
CHEMBL121053 9306 15 None -7 4 Rat 9.2 pEC50 = 9.2 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
1395 9306 15 None 3 4 Human 9.2 pEC50 = 9.2 Functional
Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
9837317 9306 15 None 3 4 Human 9.2 pEC50 = 9.2 Functional
Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
CHEMBL121053 9306 15 None 3 4 Human 9.2 pEC50 = 9.2 Functional
Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
71131322 130184 0 None 43 2 Human 9.2 pEC50 = 9.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616857 130184 0 None 43 2 Human 9.2 pEC50 = 9.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
90098428 130183 0 None 60 2 Human 9.2 pEC50 = 9.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616856 130183 0 None 60 2 Human 9.2 pEC50 = 9.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
68109941 162901 0 None - 1 Human 9.0 pEC50 = 9.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4063313 162901 0 None - 1 Human 9.0 pEC50 = 9.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
1395 9306 15 None -7 4 Rat 8.9 pEC50 = 8.9 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
9837317 9306 15 None -7 4 Rat 8.9 pEC50 = 8.9 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
CHEMBL121053 9306 15 None -7 4 Rat 8.9 pEC50 = 8.9 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
123289788 149015 0 None - 1 Human 8.9 pEC50 = 8.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OCC2CC2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884636 149015 0 None - 1 Human 8.9 pEC50 = 8.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OCC2CC2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
117972250 149090 3 None 32 2 Human 8.9 pEC50 = 8.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885379 149090 3 None 32 2 Human 8.9 pEC50 = 8.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
134130172 148937 0 None - 1 Human 8.8 pEC50 = 8.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 6 0 4 5.0 Fc1ccc(C2CC2COc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3883634 148937 0 None - 1 Human 8.8 pEC50 = 8.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 6 0 4 5.0 Fc1ccc(C2CC2COc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1 10.1016/j.bmc.2016.11.018
117968349 148978 0 None - 1 Human 8.7 pEC50 = 8.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 429 6 0 4 6.0 FC(F)(F)c1c(OCC2(c3ccccc3)CCCCC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884094 148978 0 None - 1 Human 8.7 pEC50 = 8.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 429 6 0 4 6.0 FC(F)(F)c1c(OCC2(c3ccccc3)CCCCC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
1393 8321 64 None 2 6 Human 8.0 pEC50 = 8 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
1396 8321 64 None 2 6 Human 8.0 pEC50 = 8 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
213056 8321 64 None 2 6 Human 8.0 pEC50 = 8 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
CHEMBL8759 8321 64 None 2 6 Human 8.0 pEC50 = 8 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
117968551 149001 0 None - 1 Human 8.0 pEC50 = 8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 393 6 0 4 5.0 CC(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3884343 149001 0 None - 1 Human 8.0 pEC50 = 8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 393 6 0 4 5.0 CC(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1 10.1016/j.bmc.2016.11.018
146036859 181326 5 None - 1 Human 8.0 pEC50 = 8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 293 2 0 3 3.8 Brc1cccc2c1nnn2CC1CCCCC1 10.1021/acs.jmedchem.8b00161
CHEMBL4556144 181326 5 None - 1 Human 8.0 pEC50 = 8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 293 2 0 3 3.8 Brc1cccc2c1nnn2CC1CCCCC1 10.1021/acs.jmedchem.8b00161
68108471 89423 0 None - 1 Human 8.0 pEC50 = 8 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 436 4 0 4 5.4 Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/jm3010724
CHEMBL2179326 89423 0 None - 1 Human 8.0 pEC50 = 8 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 436 4 0 4 5.4 Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/jm3010724
156020355 184807 0 None 104 2 Human 8.0 pEC50 = 8 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4646835 184807 0 None 104 2 Human 8.0 pEC50 = 8 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
67060140 174176 0 None 26 2 Rat 8.0 pEC50 = 8.0 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
CHEMBL4295230 174176 0 None 26 2 Rat 8.0 pEC50 = 8.0 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
71135411 130175 0 None 5 2 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616848 130175 0 None 5 2 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
57459497 90676 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 442 4 0 5 5.0 COc1ccc(F)cc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206439 90676 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 442 4 0 5 5.0 COc1ccc(F)cc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2Cl)CC1 10.1021/jm300912k
44361501 126082 0 None - 1 Rat 7.0 pEC50 = 7 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 217 5 4 4 -1.2 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC(=O)O 10.1021/jm030967o
CHEMBL343994 126082 0 None - 1 Rat 7.0 pEC50 = 7 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 217 5 4 4 -1.2 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC(=O)O 10.1021/jm030967o
70683631 81363 0 None - 1 Human 7.0 pEC50 = 7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 384 6 0 4 5.4 CC(C)CCn1ccc(-c2ccc(OC3CCCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029795 81363 0 None - 1 Human 7.0 pEC50 = 7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 384 6 0 4 5.4 CC(C)CCn1ccc(-c2ccc(OC3CCCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
70689929 81383 0 None - 1 Human 7.0 pEC50 = 7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 387 6 0 5 5.2 Cc1ccc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)c(C)n1 10.1021/jm2016864
CHEMBL2029813 81383 0 None - 1 Human 7.0 pEC50 = 7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 387 6 0 5 5.2 Cc1ccc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)c(C)n1 10.1021/jm2016864
70689930 81387 0 None - 1 Human 7.0 pEC50 = 7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3cccnc3C)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029817 81387 0 None - 1 Human 7.0 pEC50 = 7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3cccnc3C)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
66785101 164824 0 None - 1 Human 7.0 pEC50 = 7 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4085882 164824 0 None - 1 Human 7.0 pEC50 = 7 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
71136186 158848 0 None - 1 Human 7.0 pEC50 = 7 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 431 3 0 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21 nan
CHEMBL3967432 158848 0 None - 1 Human 7.0 pEC50 = 7 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 431 3 0 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21 nan
151031 165072 8 None - 1 Rat 4.0 pEC50 = 4 Functional
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 NC(C(=O)O)C1CC(O)=NO1 10.1021/jm701394a
59951973 165072 8 None - 1 Rat 4.0 pEC50 = 4 Functional
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 NC(C(=O)O)C1CC(O)=NO1 10.1021/jm701394a
CHEMBL408899 165072 8 None - 1 Rat 4.0 pEC50 = 4 Functional
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 NC(C(=O)O)C1CC(O)=NO1 10.1021/jm701394a
168298834 199472 0 None - 1 Human 7.0 pEC50 = 7 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1cnn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5219313 199472 0 None - 1 Human 7.0 pEC50 = 7 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1cnn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O 10.1021/acs.jmedchem.2c00969
11951272 74004 0 None - 1 Human 6.0 pEC50 = 6 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 475 12 1 6 6.4 CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL187939 74004 0 None - 1 Human 6.0 pEC50 = 6 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 475 12 1 6 6.4 CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
59234239 121337 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 349 5 0 4 4.2 CC(C)CCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337502 121337 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 349 5 0 4 4.2 CC(C)CCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
57459640 89412 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 366 4 0 4 4.7 Clc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179314 89412 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 366 4 0 4 4.7 Clc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
11545979 172575 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL424795 172575 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
44595851 10574 4 None -3 2 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
6259 10574 4 None -3 2 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
CHEMBL4092105 10574 4 None -3 2 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
11950926 74033 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 9 1 6 5.4 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL188080 74033 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 9 1 6 5.4 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
155514221 176618 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 191 2 0 3 2.0 Fc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4439927 176618 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 191 2 0 3 2.0 Fc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
118714735 121335 0 None - 1 Human 5.0 pEC50 = 5.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 309 6 0 4 3.4 CC(C)CCn1ccc(N(C)Cc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337500 121335 0 None - 1 Human 5.0 pEC50 = 5.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 309 6 0 4 3.4 CC(C)CCn1ccc(N(C)Cc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
70681520 81381 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 357 5 0 5 4.3 Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1 10.1021/jm2016864
CHEMBL2029811 81381 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 357 5 0 5 4.3 Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1 10.1021/jm2016864
59599475 155937 0 None 1 2 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 7 2 8 3.7 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(F)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3943547 155937 0 None 1 2 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 7 2 8 3.7 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(F)c1O 10.1016/j.bmcl.2016.11.049
46225569 208141 0 None 12 2 Rat 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL604467 208141 0 None 12 2 Rat 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1021/jm101414h
59599577 151663 0 None -1 2 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3909995 151663 0 None -1 2 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
11646457 73088 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2cccnc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL184917 73088 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2cccnc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
46226934 206824 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 373 5 0 7 2.7 N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CCC3CC3)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL595587 206824 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 373 5 0 7 2.7 N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CCC3CC3)cnc12 10.1016/j.bmcl.2009.11.008
69093509 90685 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 448 5 0 5 5.2 COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/jm300912k
CHEMBL2206448 90685 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 448 5 0 5 5.2 COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/jm300912k
117972256 148976 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1ccccc1COc1ccn2c(CC3CC3)nnc2c1Cl 10.1016/j.bmc.2016.11.018
CHEMBL3884075 148976 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1ccccc1COc1ccn2c(CC3CC3)nnc2c1Cl 10.1016/j.bmc.2016.11.018
117972015 149000 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 407 6 0 4 5.2 CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3884332 149000 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 407 6 0 4 5.2 CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1 10.1016/j.bmc.2016.11.018
68107863 199151 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1 10.1021/acs.jmedchem.2c00593
CHEMBL5207431 199151 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1 10.1021/acs.jmedchem.2c00593
1393 8321 64 None 2 6 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
1396 8321 64 None 2 6 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
213056 8321 64 None 2 6 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
CHEMBL8759 8321 64 None 2 6 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
1393 8321 64 None -2 6 Rat 8.0 pEC50 = 8.0 Functional
Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
1396 8321 64 None -2 6 Rat 8.0 pEC50 = 8.0 Functional
Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
213056 8321 64 None -2 6 Rat 8.0 pEC50 = 8.0 Functional
Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
CHEMBL8759 8321 64 None -2 6 Rat 8.0 pEC50 = 8.0 Functional
Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
1393 8321 64 None 2 6 Human 8.0 pEC50 = 8.0 Functional
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
1396 8321 64 None 2 6 Human 8.0 pEC50 = 8.0 Functional
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
213056 8321 64 None 2 6 Human 8.0 pEC50 = 8.0 Functional
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
CHEMBL8759 8321 64 None 2 6 Human 8.0 pEC50 = 8.0 Functional
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
71136653 130181 0 None 51 2 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616854 130181 0 None 51 2 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
156013901 184017 0 None 114 2 Human 7.9 pEC50 = 7.9 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4635729 184017 0 None 114 2 Human 7.9 pEC50 = 7.9 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
71137034 130177 0 None 7 2 Human 7.9 pEC50 = 7.9 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616850 130177 0 None 7 2 Human 7.9 pEC50 = 7.9 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
71454787 87584 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 428 4 0 4 6.0 N#Cc1c(-c2cc(Cl)c3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152118 87584 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 428 4 0 4 6.0 N#Cc1c(-c2cc(Cl)c3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
70685763 81362 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 370 7 0 4 4.9 CC(C)CCn1ccc(-c2ccc(OCC3CC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029794 81362 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 370 7 0 4 4.9 CC(C)CCn1ccc(-c2ccc(OCC3CC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
51357934 68749 0 None - 1 Rat 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1 10.1021/jm101414h
CHEMBL1774227 68749 0 None - 1 Rat 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1 10.1021/jm101414h
9815617 121277 7 None -1 2 Rat 6.0 pEC50 = 6.0 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
CHEMBL333519 121277 7 None -1 2 Rat 6.0 pEC50 = 6.0 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
57459485 89410 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 4 0 6 3.6 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CN3CCCC3)nnc12 10.1021/jm3010724
CHEMBL2179312 89410 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 4 0 6 3.6 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CN3CCCC3)nnc12 10.1021/jm3010724
11951989 74802 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 11 1 6 5.6 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2C(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL191391 74802 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 11 1 6 5.6 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2C(C)C 10.1016/j.bmcl.2005.06.017
70685761 81356 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 296 5 0 4 3.4 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
CHEMBL2029787 81356 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 296 5 0 4 3.4 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
49822037 89414 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 412 3 0 4 5.0 FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(F)(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179316 89414 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 412 3 0 4 5.0 FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(F)(c4ccccc4)CC3)ccn12 10.1021/jm3010724
57459500 89417 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 374 3 0 4 4.7 CCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179320 89417 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 374 3 0 4 4.7 CCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
71117470 152460 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 498 5 1 6 4.7 Cc1cccc(S(=O)(=O)NC2CC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)CCC2(C)C)c1 nan
CHEMBL3916091 152460 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 498 5 1 6 4.7 Cc1cccc(S(=O)(=O)NC2CC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)CCC2(C)C)c1 nan
25173448 191041 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 5 0 3 4.0 O=C1OCCCN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL483754 191041 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 5 0 3 4.0 O=C1OCCCN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
71681826 96836 0 None -1 3 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL2381651 96836 0 None -1 3 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
44155423 15471 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 277 7 0 3 4.0 CCCCCCC1CN(c2ccc(OC)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095750 15471 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 277 7 0 3 4.0 CCCCCCC1CN(c2ccc(OC)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
24809653 81358 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 314 5 0 4 3.6 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1F 10.1021/jm2016864
CHEMBL2029790 81358 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 314 5 0 4 3.6 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1F 10.1021/jm2016864
11950744 133586 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 6 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1CCN2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL365440 133586 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 6 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1CCN2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
71117232 160670 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 398 7 1 7 2.3 Cn1cnc(C(=O)NCCCCc2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1 nan
CHEMBL3983091 160670 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 398 7 1 7 2.3 Cn1cnc(C(=O)NCCCCc2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1 nan
155523303 177614 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 337 3 0 3 4.9 Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4453680 177614 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 337 3 0 3 4.9 Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
46887460 15618 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 337 4 0 3 4.1 O=C1OC(COc2cccc(C(F)(F)F)c2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1097044 15618 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 337 4 0 3 4.1 O=C1OC(COc2cccc(C(F)(F)F)c2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
90643858 118643 0 None 25 2 Rat 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287695 118643 0 None 25 2 Rat 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
156013901 184017 0 None 114 2 Human 7.9 pEC50 = 7.9 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4635729 184017 0 None 114 2 Human 7.9 pEC50 = 7.9 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
68109335 163890 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4074664 163890 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
71136640 130180 0 None 60 2 Human 7.9 pEC50 = 7.9 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616853 130180 0 None 60 2 Human 7.9 pEC50 = 7.9 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
46215878 87583 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 388 2 0 4 5.1 Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)cc(Cl)c21 10.1021/jm201561r
CHEMBL2152117 87583 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 388 2 0 4 5.1 Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)cc(Cl)c21 10.1021/jm201561r
156012835 184213 0 None -2 2 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4638687 184213 0 None -2 2 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156016100 184466 0 None -1 2 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4641860 184466 0 None -1 2 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
46887271 15462 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 275 8 0 2 4.8 CCCCCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095701 15462 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 275 8 0 2 4.8 CCCCCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
156016100 184466 0 None -1 2 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4641860 184466 0 None -1 2 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
162669954 189448 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 353 6 0 4 4.0 COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
CHEMBL4789052 189448 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 353 6 0 4 4.0 COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
44155986 15320 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 305 7 0 4 3.8 CCCCCCC1CN(c2ccc(C(=O)OC)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094462 15320 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 305 7 0 4 3.8 CCCCCCC1CN(c2ccc(C(=O)OC)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
71117222 152863 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 441 4 0 7 2.6 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
CHEMBL3919237 152863 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 441 4 0 7 2.6 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
57459655 89408 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 359 2 0 5 4.3 CC(C)(C)c1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179310 89408 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 359 2 0 5 4.3 CC(C)(C)c1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
68107697 89422 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 4 0 4 4.7 FC(F)(F)c1c(N2CCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179325 89422 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 4 0 4 4.7 FC(F)(F)c1c(N2CCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
156012835 184213 0 None -2 2 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4638687 184213 0 None -2 2 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
58103861 89429 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 384 3 0 4 4.7 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm3010724
CHEMBL2179332 89429 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 384 3 0 4 4.7 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm3010724
90668093 116315 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3ccccc3OC)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221832 116315 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3ccccc3OC)cccc2c1=O 10.1039/C0MD00200C
53322147 64498 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 298 3 0 3 4.1 CCCn1ccc2cc(-c3ccncc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669380 64498 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 298 3 0 3 4.1 CCCn1ccc2cc(-c3ccncc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53325451 64517 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 404 6 0 4 5.7 CCCn1ccc2cc(-c3ccc(OCc4cccnc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669398 64517 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 404 6 0 4 5.7 CCCn1ccc2cc(-c3ccc(OCc4cccnc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46190878 8653 7 None - 1 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
6253 8653 7 None - 1 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
CHEMBL595759 8653 7 None - 1 Human 5.9 pEC50 = 5.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
155548817 180619 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 180619 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
90668101 116326 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 384 7 1 4 5.8 CCCn1ccc2c(NCc3cccc(Oc4ccccc4)c3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221842 116326 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 384 7 1 4 5.8 CCCn1ccc2c(NCc3cccc(Oc4ccccc4)c3)cccc2c1=O 10.1039/C0MD00200C
1310 9095 110 None -389 17 Human 4.9 pEC50 = 4.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
1369 9095 110 None -389 17 Human 4.9 pEC50 = 4.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
33032 9095 110 None -389 17 Human 4.9 pEC50 = 4.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
44272391 9095 110 None -389 17 Human 4.9 pEC50 = 4.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
88747398 9095 110 None -389 17 Human 4.9 pEC50 = 4.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
CHEMBL575060 9095 110 None -389 17 Human 4.9 pEC50 = 4.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
DB00142 9095 110 None -389 17 Human 4.9 pEC50 = 4.9 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
70694131 81376 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 371 5 0 5 4.7 Cc1cc(Oc2ccc(-c3ccn(CC4CCC4)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
CHEMBL2029806 81376 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 371 5 0 5 4.7 Cc1cc(Oc2ccc(-c3ccn(CC4CCC4)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
71137012 130178 0 None 11 2 Human 7.9 pEC50 = 7.9 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616851 130178 0 None 11 2 Human 7.9 pEC50 = 7.9 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
117971683 149084 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OCC2(c3ccc(Cl)cc3)CC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885312 149084 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OCC2(c3ccc(Cl)cc3)CC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
134131394 149092 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2cccc(-c3ccccc3)c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885396 149092 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2cccc(-c3ccccc3)c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
155536450 178958 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 406 3 0 4 5.4 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(C(F)(F)F)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4473537 178958 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 406 3 0 4 5.4 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(C(F)(F)F)cccc32)cn1 10.1021/acs.jmedchem.8b00161
25008958 68738 1 None - 1 Rat 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 404 4 0 5 4.4 COc1cc(C(F)(F)F)ccc1C1CCN(Cc2nc3ncccc3n2C)CC1 10.1021/jm101414h
CHEMBL1774112 68738 1 None - 1 Rat 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 404 4 0 5 4.4 COc1cc(C(F)(F)F)ccc1C1CCN(Cc2nc3ncccc3n2C)CC1 10.1021/jm101414h
50992248 173321 0 None 1 2 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 376 5 0 5 3.9 CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2 10.1016/j.bmcl.2018.08.022
CHEMBL4279401 173321 0 None 1 2 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 376 5 0 5 3.9 CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2 10.1016/j.bmcl.2018.08.022
71137010 130176 0 None 5 2 Human 7.9 pEC50 = 7.9 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616849 130176 0 None 5 2 Human 7.9 pEC50 = 7.9 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
162651557 186964 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 319 6 0 3 4.3 c1ccc(CCCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4749289 186964 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 319 6 0 3 4.3 c1ccc(CCCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
24815439 208714 1 None -18 2 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.ejmech.2019.111881
CHEMBL607689 208714 1 None -18 2 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.ejmech.2019.111881
46887273 15464 5 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 219 4 0 2 3.2 CCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095703 15464 5 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 219 4 0 2 3.2 CCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
6604704 108177 35 None 2 3 Human 4.9 pEC50 = 4.9 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation
ChEMBL 173 2 3 3 -0.3 N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1 10.1021/jm970207b
CHEMBL29726 108177 35 None 2 3 Human 4.9 pEC50 = 4.9 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation
ChEMBL 173 2 3 3 -0.3 N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1 10.1021/jm970207b
1310 9095 110 None -457 17 Rat 4.9 pEC50 = 4.9 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
1369 9095 110 None -457 17 Rat 4.9 pEC50 = 4.9 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
33032 9095 110 None -457 17 Rat 4.9 pEC50 = 4.9 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
44272391 9095 110 None -457 17 Rat 4.9 pEC50 = 4.9 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
88747398 9095 110 None -457 17 Rat 4.9 pEC50 = 4.9 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
CHEMBL575060 9095 110 None -457 17 Rat 4.9 pEC50 = 4.9 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
DB00142 9095 110 None -457 17 Rat 4.9 pEC50 = 4.9 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
44397878 131179 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 389 6 1 5 5.6 CCCc1c(Oc2cccc(-c3nnn[nH]3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL363945 131179 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 389 6 1 5 5.6 CCCc1c(Oc2cccc(-c3nnn[nH]3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
71116730 155841 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 424 3 1 6 2.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21 nan
CHEMBL3942904 155841 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 424 3 1 6 2.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21 nan
44155989 15319 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 305 7 0 4 3.8 CCCCCCC1CN(c2cccc(C(=O)OC)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094461 15319 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 305 7 0 4 3.8 CCCCCCC1CN(c2cccc(C(=O)OC)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
25073615 173243 0 None -4 2 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 300 3 0 5 2.4 CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1 10.1016/j.bmcl.2018.08.022
CHEMBL4278070 173243 0 None -4 2 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 300 3 0 5 2.4 CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1 10.1016/j.bmcl.2018.08.022
11951270 74100 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 9 1 6 5.3 CCCc1c(OCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL188455 74100 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 9 1 6 5.3 CCCc1c(OCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
156817945 197263 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL5179002 197263 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
162676513 190292 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 291 4 0 3 3.5 c1ccc(CCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4799794 190292 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 291 4 0 3 3.5 c1ccc(CCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
70689928 81382 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 5.0 CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029812 81382 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 5.0 CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)cc2)c(C#N)c1=O 10.1021/jm2016864
46887493 15356 1 None - 1 Human 4.9 pEC50 = 4.9 Functional
Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094762 15356 1 None - 1 Human 4.9 pEC50 = 4.9 Functional
Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
162674797 190247 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4799164 190247 0 None - 1 Human 5.9 pEC50 = 5.9 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
155562956 181956 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 365 2 0 3 4.0 Brc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4570470 181956 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 365 2 0 3 4.0 Brc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
67060162 173742 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4cc(C)c(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
CHEMBL4287326 173742 0 None - 1 Human 7.9 pEC50 = 7.9 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4cc(C)c(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
71116701 151637 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 387 4 1 4 2.4 CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O nan
CHEMBL3909811 151637 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 387 4 1 4 2.4 CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O nan
146036860 180057 6 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 253 2 0 3 2.9 CC(C)Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4525401 180057 6 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 253 2 0 3 2.9 CC(C)Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
155552571 180935 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 319 2 0 3 3.6 FC(F)(F)c1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4546739 180935 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 319 2 0 3 3.6 FC(F)(F)c1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
118714748 121348 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3cccc(F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337514 121348 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3cccc(F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
155519836 177149 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 338 3 0 4 4.3 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)nc1 10.1021/acs.jmedchem.8b00161
CHEMBL4447702 177149 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 338 3 0 4 4.3 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)nc1 10.1021/acs.jmedchem.8b00161
46227787 206472 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 390 4 1 4 5.2 N#Cc1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL593168 206472 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 390 4 1 4 5.2 N#Cc1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
25173776 191081 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 267 3 0 2 3.7 C[C@@H]1CN(Cc2ccc(-c3ccccc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484128 191081 0 None - 1 Human 6.9 pEC50 = 6.9 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 267 3 0 2 3.7 C[C@@H]1CN(Cc2ccc(-c3ccccc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
59599515 154926 0 None -10 2 Human 5.8 pEC50 = 5.8 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 9 2 6 5.0 CCCc1c(OCc2ccc(Oc3ccc(C(=O)O)cn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3935529 154926 0 None -10 2 Human 5.8 pEC50 = 5.8 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 9 2 6 5.0 CCCc1c(OCc2ccc(Oc3ccc(C(=O)O)cn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
24815882 68731 0 None - 1 Rat 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccccc3Cl)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL1774104 68731 0 None - 1 Rat 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccccc3Cl)CC2)nc2ccccc21 10.1021/jm101414h
71137008 130182 0 None 7 2 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616855 130182 0 None 7 2 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
25195461 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
8946 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
CHEMBL3337527 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
DB12059 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
68109272 165397 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4092275 165397 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
70689926 81374 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 358 6 1 5 4.6 CC(C)CCn1ccc(-c2ccc(Nc3ccncc3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029804 81374 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 358 6 1 5 4.6 CC(C)CCn1ccc(-c2ccc(Nc3ccncc3)cc2)c(C#N)c1=O 10.1021/jm2016864
70977933 178083 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 241 2 0 3 2.9 FC(F)(F)c1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4460927 178083 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 241 2 0 3 2.9 FC(F)(F)c1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
57459517 89420 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 372 3 0 4 4.3 FC(F)(F)c1c(N2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179323 89420 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 372 3 0 4 4.3 FC(F)(F)c1c(N2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
25173286 179473 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 5 0 3 4.0 CC1CN(Cc2ccc(OCC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL450207 179473 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 5 0 3 4.0 CC1CN(Cc2ccc(OCC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
155534303 178723 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4470447 178723 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
155567633 182779 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4589377 182779 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
66785780 165523 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093657 165523 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
58103890 87586 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 457 4 2 4 6.1 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)cnc4c3Cl)cc2Cl)CC1 10.1021/jm201561r
CHEMBL2152120 87586 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 457 4 2 4 6.1 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)cnc4c3Cl)cc2Cl)CC1 10.1021/jm201561r
11531870 71087 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 420 10 1 4 5.6 CC(C)CC(=O)c1ccc(OCCCCOc2ccccc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL181089 71087 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 420 10 1 4 5.6 CC(C)CC(=O)c1ccc(OCCCCOc2ccccc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
59234231 8924 4 None -1 2 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
6330 8924 4 None -1 2 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
6331 8924 4 None -1 2 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
CHEMBL3337510 8924 4 None -1 2 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
118714757 121357 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3cc(F)cc(F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337523 121357 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3cc(F)cc(F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
66785393 163673 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4072134 163673 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
9815616 121578 6 None -2 4 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.ejmech.2020.112521
CHEMBL334014 121578 6 None -2 4 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.ejmech.2020.112521
11530877 71652 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2ccccn2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182166 71652 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2ccccn2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
9815616 121578 6 None -2 4 Rat 6.8 pEC50 = 6.8 Functional
Agonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.ejmech.2020.112521
CHEMBL334014 121578 6 None -2 4 Rat 6.8 pEC50 = 6.8 Functional
Agonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.ejmech.2020.112521
156014194 183989 0 None -2 2 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635373 183989 0 None -2 2 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156018860 184693 0 None -2 2 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4645193 184693 0 None -2 2 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
7504549 178290 1 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 285 3 0 3 4.1 c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4464043 178290 1 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 285 3 0 3 4.1 c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)cc1 10.1021/acs.jmedchem.8b00161
71462632 89427 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 344 4 0 4 4.5 CCCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179330 89427 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 344 4 0 4 4.5 CCCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
168299101 199529 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)nnc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5220917 199529 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)nnc2c1=O 10.1021/acs.jmedchem.2c00969
44591744 195444 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3cccc(Cl)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL503697 195444 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3cccc(Cl)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
156020355 184807 0 None 104 2 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4646835 184807 0 None 104 2 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
53321493 64516 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 390 5 0 4 5.9 CCCn1ccc2cc(-c3ccc(Oc4ccncc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669397 64516 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 390 5 0 4 5.9 CCCn1ccc2cc(-c3ccc(Oc4ccncc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46227786 206624 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 407 5 0 4 5.6 N#Cc1c(-c2ccc(OCc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL594334 206624 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 407 5 0 4 5.6 N#Cc1c(-c2ccc(OCc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
155533313 178631 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4468977 178631 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
155548817 180619 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 180619 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
90668097 116321 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 320 7 1 3 4.5 CCCn1ccc2c(NCCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221838 116321 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 320 7 1 3 4.5 CCCn1ccc2c(NCCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
68109333 164408 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4081244 164408 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
53323491 64501 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 287 3 1 3 3.5 CCCn1ccc2cc(-c3cn[nH]c3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669383 64501 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 287 3 1 3 3.5 CCCn1ccc2cc(-c3cn[nH]c3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
24815355 68730 0 None - 1 Rat 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccc(F)cc3)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL1774103 68730 0 None - 1 Rat 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccc(F)cc3)CC2)nc2ccccc21 10.1021/jm101414h
51030965 173929 0 None 1 2 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 312 3 0 5 2.3 CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21 10.1016/j.bmcl.2018.08.022
CHEMBL4290744 173929 0 None 1 2 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 312 3 0 5 2.3 CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21 10.1016/j.bmcl.2018.08.022
60096246 162726 0 None -6 2 Human 7.8 pEC50 = 7.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1 10.1021/acs.jmedchem.7b01481
CHEMBL4061162 162726 0 None -6 2 Human 7.8 pEC50 = 7.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1 10.1021/acs.jmedchem.7b01481
117972153 149080 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 6 0 4 5.0 Fc1ccc(C2(COc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3885265 149080 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 6 0 4 5.0 Fc1ccc(C2(COc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)cc1 10.1016/j.bmc.2016.11.018
49822115 8927 21 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.2c00969
8947 8927 21 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.2c00969
CHEMBL3947764 8927 21 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.2c00969
71136746 155379 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
CHEMBL3939174 155379 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
71136655 130179 0 None 12 2 Human 7.8 pEC50 = 7.8 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616852 130179 0 None 12 2 Human 7.8 pEC50 = 7.8 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
9815617 121277 7 None -1 2 Rat 7.8 pEC50 = 7.8 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
CHEMBL333519 121277 7 None -1 2 Rat 7.8 pEC50 = 7.8 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
46215704 87585 0 None 33 2 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 447 3 1 4 6.2 O[C@H]1CC[C@H](n2ccc3cc(-c4ccn5c(CC(F)(F)F)cnc5c4Cl)ccc32)CC1 10.1021/jm201561r
CHEMBL2152119 87585 0 None 33 2 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 447 3 1 4 6.2 O[C@H]1CC[C@H](n2ccc3cc(-c4ccn5c(CC(F)(F)F)cnc5c4Cl)ccc32)CC1 10.1021/jm201561r
156020355 184807 0 None 104 2 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4646835 184807 0 None 104 2 Human 6.8 pEC50 = 6.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
156014194 183989 0 None -2 2 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635373 183989 0 None -2 2 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156018860 184693 0 None -2 2 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4645193 184693 0 None -2 2 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
10976811 116490 0 None - 1 Rat 4.8 pEC50 = 4.8 Functional
Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells
ChEMBL 214 2 3 5 -1.0 N[C@]1(C(=O)O)C[C@@H]2ON=C(C(=O)O)[C@@H]2C1 10.1021/jm0308085
CHEMBL322887 116490 0 None - 1 Rat 4.8 pEC50 = 4.8 Functional
Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells
ChEMBL 214 2 3 5 -1.0 N[C@]1(C(=O)O)C[C@@H]2ON=C(C(=O)O)[C@@H]2C1 10.1021/jm0308085
1310 9095 110 None -457 17 Rat 4.8 pEC50 = 4.8 Functional
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
1369 9095 110 None -457 17 Rat 4.8 pEC50 = 4.8 Functional
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
33032 9095 110 None -457 17 Rat 4.8 pEC50 = 4.8 Functional
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
44272391 9095 110 None -457 17 Rat 4.8 pEC50 = 4.8 Functional
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
88747398 9095 110 None -457 17 Rat 4.8 pEC50 = 4.8 Functional
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
CHEMBL575060 9095 110 None -457 17 Rat 4.8 pEC50 = 4.8 Functional
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
DB00142 9095 110 None -457 17 Rat 4.8 pEC50 = 4.8 Functional
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
11310142 9200 19 None 13 3 Human 6.8 pEC50 = 6.8 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
11614 9200 19 None 13 3 Human 6.8 pEC50 = 6.8 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
CHEMBL192051 9200 19 None 13 3 Human 6.8 pEC50 = 6.8 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
51357397 68732 0 None - 1 Rat 5.8 pEC50 = 5.8 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 330 3 0 4 3.8 Cn1c(CN2CCC(c3cccc(C#N)c3)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL1774105 68732 0 None - 1 Rat 5.8 pEC50 = 5.8 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 330 3 0 4 3.8 Cn1c(CN2CCC(c3cccc(C#N)c3)CC2)nc2ccccc21 10.1021/jm101414h
70696263 81385 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029815 81385 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
49822116 153770 13 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL3926416 153770 13 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
168299087 199521 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 320 4 1 4 3.8 CCCCn1ccn2c(-c3ccc4[nH]ccc4c3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5220552 199521 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 320 4 1 4 3.8 CCCCn1ccn2c(-c3ccc4[nH]ccc4c3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
46216056 87577 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 358 2 1 5 3.8 N#Cc1c(-c2ccc3c(c2)OCCN3)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152110 87577 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 358 2 1 5 3.8 N#Cc1c(-c2ccc3c(c2)OCCN3)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
25008437 68735 0 None - 1 Rat 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cnccc21 10.1021/jm101414h
CHEMBL1774109 68735 0 None - 1 Rat 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cnccc21 10.1021/jm101414h
117972044 149061 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1cccc(COc2ccn3c(CC4CC4)nnc3c2Cl)c1 10.1016/j.bmc.2016.11.018
CHEMBL3885097 149061 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1cccc(COc2ccn3c(CC4CC4)nnc3c2Cl)c1 10.1016/j.bmc.2016.11.018
155566740 182664 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 321 2 0 3 3.9 Clc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4586335 182664 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 321 2 0 3 3.9 Clc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
49765871 8926 45 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
6317 8926 45 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
CHEMBL2179319 8926 45 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
60096236 165201 0 None -3 2 Human 7.8 pEC50 = 7.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4090293 165201 0 None -3 2 Human 7.8 pEC50 = 7.8 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
66784246 163143 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4066051 163143 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
66785300 163251 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
CHEMBL4067421 163251 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
59599580 159495 0 None 8 2 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 471 7 2 8 4.6 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(C(F)(F)F)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3973048 159495 0 None 8 2 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 471 7 2 8 4.6 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(C(F)(F)F)c1O 10.1016/j.bmcl.2016.11.049
71116952 154092 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
CHEMBL3929070 154092 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
59497100 121358 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 342 4 0 3 4.3 O=c1c(Cl)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1 10.1021/jm500496m
CHEMBL3337524 121358 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 342 4 0 3 4.3 O=c1c(Cl)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1 10.1021/jm500496m
162659390 187971 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.1 Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl 10.1016/j.ejmech.2019.111881
CHEMBL4761080 187971 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.1 Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl 10.1016/j.ejmech.2019.111881
1402 6910 44 None - 1 Human 5.8 pEC50 = 5.8 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.09.028
9825084 6910 44 None - 1 Human 5.8 pEC50 = 5.8 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.09.028
CHEMBL108939 6910 44 None - 1 Human 5.8 pEC50 = 5.8 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.09.028
10608207 125542 5 None - 1 Rat 4.8 pEC50 = 4.8 Functional
Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 203 2 3 3 -0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F 10.1021/jm000346k
CHEMBL341888 125542 5 None - 1 Rat 4.8 pEC50 = 4.8 Functional
Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 203 2 3 3 -0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F 10.1021/jm000346k
11537726 73467 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2cccnc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL185490 73467 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2cccnc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
25004010 81372 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 399 6 1 5 4.7 CC(C)CCn1ccc(-c2ccc(NC3CCOCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029802 81372 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 399 6 1 5 4.7 CC(C)CCn1ccc(-c2ccc(NC3CCOCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
168298053 199526 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 356 3 1 3 4.8 FC(F)(F)c1c(-c2ccc3[nH]ccc3c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.2c00969
CHEMBL5220838 199526 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 356 3 1 3 4.8 FC(F)(F)c1c(-c2ccc3[nH]ccc3c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.2c00969
44155644 15622 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2ccccc2C#N)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1097054 15622 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2ccccc2C#N)C(=O)O1 10.1016/j.bmcl.2010.03.089
1310 9095 110 None -389 17 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
1369 9095 110 None -389 17 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
33032 9095 110 None -389 17 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
44272391 9095 110 None -389 17 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
88747398 9095 110 None -389 17 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
CHEMBL575060 9095 110 None -389 17 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
DB00142 9095 110 None -389 17 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
71117549 153622 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 437 4 0 6 1.8 CN1c2nc(C3=CCN(C(=O)c4ccon4)C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
CHEMBL3925103 153622 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 437 4 0 6 1.8 CN1c2nc(C3=CCN(C(=O)c4ccon4)C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
155548817 180619 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 180619 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
118714745 121345 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 347 5 0 4 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337511 121345 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 347 5 0 4 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCC2CC2)c1=O 10.1021/jm500496m
57459504 89415 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 434 4 0 4 5.4 FC(F)(F)C1(c2ccccc2)CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm3010724
CHEMBL2179317 89415 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 434 4 0 4 5.4 FC(F)(F)C1(c2ccccc2)CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm3010724
134131242 149057 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 353 4 0 4 4.3 Clc1c(OC2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885072 149057 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 353 4 0 4 4.3 Clc1c(OC2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
155519900 177179 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1cc(Cn2nnc3c(Br)cccc32)ccc1Cl 10.1021/acs.jmedchem.8b00161
CHEMBL4448031 177179 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1cc(Cn2nnc3c(Br)cccc32)ccc1Cl 10.1021/acs.jmedchem.8b00161
155565817 182400 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1cccc(Cn2nnc3c(Br)cccc32)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4580527 182400 0 None - 1 Human 7.8 pEC50 = 7.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1cccc(Cn2nnc3c(Br)cccc32)c1 10.1021/acs.jmedchem.8b00161
60096190 165292 0 None -9 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4091203 165292 0 None -9 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
10353365 90022 1 None 13 3 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL218710 90022 1 None 13 3 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
49822115 8927 21 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
8947 8927 21 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
CHEMBL3947764 8927 21 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
1393 8321 64 None -2 6 Rat 7.7 pEC50 = 7.7 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
1396 8321 64 None -2 6 Rat 7.7 pEC50 = 7.7 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
213056 8321 64 None -2 6 Rat 7.7 pEC50 = 7.7 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
CHEMBL8759 8321 64 None -2 6 Rat 7.7 pEC50 = 7.7 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
66787355 163004 0 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4064589 163004 0 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
66784572 163687 0 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4072262 163687 0 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
134130477 149102 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 313 5 0 4 3.9 Clc1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885492 149102 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 313 5 0 4 3.9 Clc1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
162644700 186202 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 373 5 0 4 3.8 O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(F)c(Cl)c1 10.1016/j.ejmech.2019.111881
CHEMBL4740255 186202 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 373 5 0 4 3.8 O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(F)c(Cl)c1 10.1016/j.ejmech.2019.111881
155527610 178027 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 366 2 0 4 3.4 Brc1ccc(Cn2nnc3c(Br)cccc32)nc1 10.1021/acs.jmedchem.8b00161
CHEMBL4460043 178027 0 None - 1 Human 6.8 pEC50 = 6.8 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 366 2 0 4 3.4 Brc1ccc(Cn2nnc3c(Br)cccc32)nc1 10.1021/acs.jmedchem.8b00161
44591797 191423 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 304 3 0 3 3.4 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)cn2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484958 191423 0 None - 1 Human 5.8 pEC50 = 5.8 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 304 3 0 3 3.4 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)cn2)C(=O)O1 10.1016/j.bmcl.2009.03.032
104766 6822 42 None -2 14 Human 4.8 pEC50 = 4.8 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970207b
1365 6822 42 None -2 14 Human 4.8 pEC50 = 4.8 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970207b
CHEMBL34453 6822 42 None -2 14 Human 4.8 pEC50 = 4.8 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970207b
1310 9095 110 None -457 17 Rat 4.7 pEC50 = 4.7 Functional
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
1369 9095 110 None -457 17 Rat 4.7 pEC50 = 4.7 Functional
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
33032 9095 110 None -457 17 Rat 4.7 pEC50 = 4.7 Functional
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
44272391 9095 110 None -457 17 Rat 4.7 pEC50 = 4.7 Functional
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
88747398 9095 110 None -457 17 Rat 4.7 pEC50 = 4.7 Functional
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
CHEMBL575060 9095 110 None -457 17 Rat 4.7 pEC50 = 4.7 Functional
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
DB00142 9095 110 None -457 17 Rat 4.7 pEC50 = 4.7 Functional
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
1310 9095 110 None -389 17 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
1369 9095 110 None -389 17 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
33032 9095 110 None -389 17 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
44272391 9095 110 None -389 17 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
88747398 9095 110 None -389 17 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
CHEMBL575060 9095 110 None -389 17 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
DB00142 9095 110 None -389 17 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
44591771 191019 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 351 4 0 3 4.6 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL483561 191019 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 351 4 0 3 4.6 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
162649571 186900 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 311 3 0 3 3.7 Clc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4748614 186900 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 311 3 0 3 3.7 Clc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
51356833 68747 0 None - 1 Rat 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 400 3 0 4 4.9 Cn1c(CN2[C@H]3CC[C@@H]2CC(c2ccc(C(F)(F)F)cc2)C3)nc2ncccc21 10.1021/jm101414h
CHEMBL1774225 68747 0 None - 1 Rat 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 400 3 0 4 4.9 Cn1c(CN2[C@H]3CC[C@@H]2CC(c2ccc(C(F)(F)F)cc2)C3)nc2ncccc21 10.1021/jm101414h
46227797 208414 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 393 4 0 4 5.8 N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL605921 208414 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 393 4 0 4 5.8 N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
25004352 81364 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 400 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(OC3CCOCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029796 81364 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 400 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(OC3CCOCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
46227797 208414 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 393 4 0 4 5.8 N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL605921 208414 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 393 4 0 4 5.8 N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
11655609 172680 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 8 4.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL424998 172680 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 8 4.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
71476419 130187 0 None 51 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616860 130187 0 None 51 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
60096204 162903 0 None -2 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4063336 162903 0 None -2 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
11220424 165740 0 None -3 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 304 4 4 4 -0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4095995 165740 0 None -3 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 304 4 4 4 -0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
71456562 87579 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 394 4 0 4 5.3 N#Cc1c(-c2ccc3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152113 87579 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 394 4 0 4 5.3 N#Cc1c(-c2ccc3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
155519573 180047 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1ccc(Cn2nnc3c(Br)cccc32)c(Cl)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4525207 180047 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1ccc(Cn2nnc3c(Br)cccc32)c(Cl)c1 10.1021/acs.jmedchem.8b00161
44155748 15276 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 263 6 1 3 3.7 CCCCCCC1CN(c2cccc(O)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094124 15276 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 263 6 1 3 3.7 CCCCCCC1CN(c2cccc(O)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
118263352 121360 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 4 0 3 4.5 CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(Cl)c1=O 10.1021/jm500496m
CHEMBL3337526 121360 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 4 0 3 4.5 CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(Cl)c1=O 10.1021/jm500496m
25009651 68736 0 None - 1 Rat 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccncc21 10.1021/jm101414h
CHEMBL1774110 68736 0 None - 1 Rat 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccncc21 10.1021/jm101414h
11559813 71782 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 374 10 1 4 5.3 Cc1c(OCCCCOc2ccccc2F)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182316 71782 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 374 10 1 4 5.3 Cc1c(OCCCCOc2ccccc2F)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
90668095 116318 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 320 6 1 3 4.4 CCCn1ccc2c(NCCc3ccc(C)cc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221835 116318 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 320 6 1 3 4.4 CCCn1ccc2c(NCCc3ccc(C)cc3)cccc2c1=O 10.1039/C0MD00200C
90668102 116327 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 376 6 1 4 4.9 CCCn1ccc2c(NCc3cccc(OC(F)(F)F)c3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221843 116327 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 376 6 1 4 4.9 CCCn1ccc2c(NCc3cccc(OC(F)(F)F)c3)cccc2c1=O 10.1039/C0MD00200C
46917716 116328 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 326 5 1 3 4.7 CCCn1ccc2c(NCc3ccccc3Cl)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221844 116328 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 326 5 1 3 4.7 CCCn1ccc2c(NCc3ccccc3Cl)cccc2c1=O 10.1039/C0MD00200C
53326710 64515 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 389 5 0 3 6.5 CCCn1ccc2cc(-c3ccc(Oc4ccccc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669396 64515 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 389 5 0 3 6.5 CCCn1ccc2cc(-c3ccc(Oc4ccccc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46190877 8652 7 None - 1 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
6252 8652 7 None - 1 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
CHEMBL605836 8652 7 None - 1 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
24815976 206538 0 None -5 2 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593745 206538 0 None -5 2 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225336 206827 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 363 3 0 6 3.5 Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595609 206827 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 363 3 0 6 3.5 Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
90668098 116322 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 292 5 1 3 4.0 CCCn1ccc2c(NCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221839 116322 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 292 5 1 3 4.0 CCCn1ccc2c(NCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
10197984 9199 44 None 1 5 Human 8.6 pEC50 = 8.6 Functional
Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
1394 9199 44 None 1 5 Human 8.6 pEC50 = 8.6 Functional
Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
CHEMBL275079 9199 44 None 1 5 Human 8.6 pEC50 = 8.6 Functional
Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
10197984 9199 44 None 1 5 Human 8.6 pEC50 = 8.6 Functional
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
1394 9199 44 None 1 5 Human 8.6 pEC50 = 8.6 Functional
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
CHEMBL275079 9199 44 None 1 5 Human 8.6 pEC50 = 8.6 Functional
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
10197984 9199 44 None 1 5 Human 8.6 pEC50 = 8.6 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
1394 9199 44 None 1 5 Human 8.6 pEC50 = 8.6 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
CHEMBL275079 9199 44 None 1 5 Human 8.6 pEC50 = 8.6 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
66786902 166240 0 None - 1 Human 8.5 pEC50 = 8.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4101354 166240 0 None - 1 Human 8.5 pEC50 = 8.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
71457756 90677 0 None 66 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206440 90677 0 None 66 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
134130276 149082 0 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2ccccc2-c2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885277 149082 0 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2ccccc2-c2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
155536501 178973 1 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 265 2 0 3 3.0 Brc1cccc2c1nnn2CC1CCC1 10.1021/acs.jmedchem.8b00161
CHEMBL4473685 178973 1 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 265 2 0 3 3.0 Brc1cccc2c1nnn2CC1CCC1 10.1021/acs.jmedchem.8b00161
68108457 155335 0 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL3938796 155335 0 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL5074658 221102 0 None - 1 Human 7.7 pEC50 = 7.7 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Br)cc1 10.1021/acs.jmedchem.1c00563
71137011 130185 0 None 58 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616858 130185 0 None 58 2 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
53240406 130174 17 None 107 4 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 130174 17 None 107 4 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
50992248 173321 0 None -1 2 Rat 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 376 5 0 5 3.9 CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2 10.1016/j.bmcl.2018.08.022
CHEMBL4279401 173321 0 None -1 2 Rat 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 376 5 0 5 3.9 CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2 10.1016/j.bmcl.2018.08.022
1392 6861 48 None 5 4 Rat 6.7 pEC50 = 6.7 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
5310984 6861 48 None 5 4 Rat 6.7 pEC50 = 6.7 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
CHEMBL40086 6861 48 None 5 4 Rat 6.7 pEC50 = 6.7 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
104766 6822 42 None 2 14 Rat 5.7 pEC50 = 5.7 Functional
Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm0308085
1365 6822 42 None 2 14 Rat 5.7 pEC50 = 5.7 Functional
Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm0308085
CHEMBL34453 6822 42 None 2 14 Rat 5.7 pEC50 = 5.7 Functional
Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm0308085
11596869 150415 0 None -8 2 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 417 7 2 8 3.9 CC(=O)c1ccc(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)c(C)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3899832 150415 0 None -8 2 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 417 7 2 8 3.9 CC(=O)c1ccc(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)c(C)c1O 10.1016/j.bmcl.2016.11.049
25173287 177153 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 6 0 3 4.4 CC1CN(Cc2ccc(OCCC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL444778 177153 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 6 0 3 4.4 CC1CN(Cc2ccc(OCCC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
24809687 81373 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 351 5 0 5 3.3 CC(C)CCn1ccc(-c2ccc(N3CCOCC3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029803 81373 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 351 5 0 5 3.3 CC(C)CCn1ccc(-c2ccc(N3CCOCC3)cc2)c(C#N)c1=O 10.1021/jm2016864
156817927 198385 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 433 5 0 5 4.2 Fc1ccccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
CHEMBL5195400 198385 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 433 5 0 5 4.2 Fc1ccccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
44363330 43247 0 None - 1 Rat 7.7 pEC50 = 7.7 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)CC(O)[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
CHEMBL144747 43247 0 None - 1 Rat 7.7 pEC50 = 7.7 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)CC(O)[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
53240406 130174 17 None 107 4 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 130174 17 None 107 4 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
11275666 96832 1 None 1 3 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL2381647 96832 1 None 1 3 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
156018305 184613 0 None 89 2 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4643961 184613 0 None 89 2 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
155539343 179608 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 366 2 0 4 3.4 Brc1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4514174 179608 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 366 2 0 4 3.4 Brc1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
104766 6822 42 None 2 14 Rat 5.7 pEC50 = 5.7 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
1365 6822 42 None 2 14 Rat 5.7 pEC50 = 5.7 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
CHEMBL34453 6822 42 None 2 14 Rat 5.7 pEC50 = 5.7 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
24815434 206475 0 None 5 2 Rat 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL593196 206475 0 None 5 2 Rat 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1021/jm101414h
156018305 184613 0 None 89 2 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4643961 184613 0 None 89 2 Human 6.7 pEC50 = 6.7 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
42610167 87576 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 420 3 0 5 4.5 N#Cc1c(-c2ccc(N3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152109 87576 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 420 3 0 5 4.5 N#Cc1c(-c2ccc(N3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
71117258 153327 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 467 6 1 8 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)CCn4cncn4)C3)nc21 nan
CHEMBL3922773 153327 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 467 6 1 8 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)CCn4cncn4)C3)nc21 nan
46887416 15315 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 299 5 0 4 3.1 COc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
CHEMBL1094416 15315 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 299 5 0 4 3.1 COc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
51357936 68751 0 None 3 2 Rat 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C 10.1021/jm101414h
CHEMBL1774231 68751 0 None 3 2 Rat 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C 10.1021/jm101414h
24815439 208714 1 None 18 2 Rat 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL607689 208714 1 None 18 2 Rat 7.7 pEC50 = 7.7 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1021/jm101414h
53240406 130174 17 None 107 4 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 130174 17 None 107 4 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
25173773 191703 0 None - 1 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2C[C@H](C)OC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
CHEMBL485336 191703 0 None - 1 Human 7.7 pEC50 = 7.7 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2C[C@H](C)OC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
71117730 150709 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21 nan
CHEMBL3902193 150709 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21 nan
66784890 162829 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4062535 162829 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
68109425 165069 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4088960 165069 0 None - 1 Human 6.7 pEC50 = 6.7 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
155560108 181688 2 None - 1 Human 5.7 pEC50 = 5.7 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 225 1 0 3 2.2 CCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4564533 181688 2 None - 1 Human 5.7 pEC50 = 5.7 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 225 1 0 3 2.2 CCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
11950745 130422 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 497 9 1 6 5.9 CC(C)(C)Cn1ccc2c(Br)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
CHEMBL361934 130422 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 497 9 1 6 5.9 CC(C)(C)Cn1ccc2c(Br)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
59599555 160327 0 None 1 2 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3ncccc3-c3nn[nH]n3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3980125 160327 0 None 1 2 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3ncccc3-c3nn[nH]n3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
11951806 73579 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 487 12 1 6 6.6 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CCCCC1 10.1016/j.bmcl.2005.06.017
CHEMBL186018 73579 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 487 12 1 6 6.6 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CCCCC1 10.1016/j.bmcl.2005.06.017
162654261 187433 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 335 6 0 4 3.9 COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4755053 187433 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 335 6 0 4 3.9 COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
9979770 73112 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 424 11 2 7 4.3 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL185054 73112 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 424 11 2 7 4.3 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
46227789 206496 1 None - 1 Human 5.6 pEC50 = 5.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 361 3 0 7 2.5 CCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
CHEMBL593399 206496 1 None - 1 Human 5.6 pEC50 = 5.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 361 3 0 7 2.5 CCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
155531064 178417 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1cc(Cl)ccc1Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4465783 178417 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1cc(Cl)ccc1Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
9834591 144378 69 None 2 3 Human 7.6 pEC50 = 7.6 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 235 2 3 5 -2.1 N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL375611 144378 69 None 2 3 Human 7.6 pEC50 = 7.6 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 235 2 3 5 -2.1 N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
46215709 87578 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 354 2 0 4 4.5 Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)ccc21 10.1021/jm201561r
CHEMBL2152112 87578 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 354 2 0 4 4.5 Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)ccc21 10.1021/jm201561r
156013901 184017 0 None 114 2 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4635729 184017 0 None 114 2 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
70685768 81388 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 391 5 0 5 4.9 Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1Cl 10.1021/jm2016864
CHEMBL2029818 81388 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 391 5 0 5 4.9 Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1Cl 10.1021/jm2016864
134130478 149103 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 364 5 0 5 4.5 Clc1c(OCc2cccc3ccncc23)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885493 149103 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 364 5 0 5 4.5 Clc1c(OCc2cccc3ccncc23)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
44300122 19901 0 None - 1 Rat 5.6 pEC50 = 5.6 Functional
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 279 4 4 5 -0.3 Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1 10.1016/s0960-894x(01)00329-8
CHEMBL1190517 19901 0 None - 1 Rat 5.6 pEC50 = 5.6 Functional
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 279 4 4 5 -0.3 Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1 10.1016/s0960-894x(01)00329-8
CHEMBL541050 19901 0 None - 1 Rat 5.6 pEC50 = 5.6 Functional
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 279 4 4 5 -0.3 Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1 10.1016/s0960-894x(01)00329-8
156013901 184017 0 None 114 2 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4635729 184017 0 None 114 2 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
42610166 208448 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 384 3 0 4 5.0 N#Cc1c(-c2ccc(N3CCCCC3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL606153 208448 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 384 3 0 4 5.0 N#Cc1c(-c2ccc(N3CCCCC3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
1310 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
1369 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
33032 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
44272391 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
88747398 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
CHEMBL575060 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
DB00142 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
68107863 199151 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1 10.1021/acs.jmedchem.2c00593
CHEMBL5207431 199151 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1 10.1021/acs.jmedchem.2c00593
25173617 195435 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 289 4 0 3 3.7 CC1CN(Cc2ccc(OC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL503572 195435 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 289 4 0 3 3.7 CC1CN(Cc2ccc(OC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
57459501 89418 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 402 5 0 4 5.5 CCCCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179321 89418 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 402 5 0 4 5.5 CCCCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
46887372 15576 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 4 0 3 4.4 CC(C)(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
CHEMBL1096713 15576 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 4 0 3 4.4 CC(C)(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
162669368 189547 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 330 5 0 4 3.7 N#Cc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4790241 189547 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 330 5 0 4 3.7 N#Cc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
44300605 20127 0 None -3 3 Rat 4.6 pEC50 = 4.6 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1192345 20127 0 None -3 3 Rat 4.6 pEC50 = 4.6 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL543568 20127 0 None -3 3 Rat 4.6 pEC50 = 4.6 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1 10.1016/s0960-894x(01)00329-8
71136654 130186 0 None 3 2 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616859 130186 0 None 3 2 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
162659966 188030 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 291 3 0 3 3.4 Cc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4761771 188030 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 291 3 0 3 3.4 Cc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
156014680 184029 0 None -2 2 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635960 184029 0 None -2 2 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
51357400 68745 0 None - 1 Rat 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 408 4 0 5 4.4 Cn1c(CN2CCC(c3ccc(OC(F)(F)F)cc3F)CC2)nc2ncccc21 10.1021/jm101414h
CHEMBL1774222 68745 0 None - 1 Rat 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 408 4 0 5 4.4 Cn1c(CN2CCC(c3ccc(OC(F)(F)F)cc3F)CC2)nc2ncccc21 10.1021/jm101414h
51357399 68744 0 None - 1 Rat 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 392 3 0 4 4.5 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3F)CC2)nc2ncccc21 10.1021/jm101414h
CHEMBL1774221 68744 0 None - 1 Rat 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 392 3 0 4 4.5 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3F)CC2)nc2ncccc21 10.1021/jm101414h
68108857 164117 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4077609 164117 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
71458417 87588 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 437 4 0 3 6.8 FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4c(ccn4CC4CC4)c3)ccn12 10.1021/jm201561r
CHEMBL2152122 87588 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 437 4 0 3 6.8 FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4c(ccn4CC4CC4)c3)ccn12 10.1021/jm201561r
44155645 15468 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2cccc(C#N)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095745 15468 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2cccc(C#N)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
51030965 173929 0 None -1 2 Rat 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 312 3 0 5 2.3 CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21 10.1016/j.bmcl.2018.08.022
CHEMBL4290744 173929 0 None -1 2 Rat 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 312 3 0 5 2.3 CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21 10.1016/j.bmcl.2018.08.022
CHEMBL5083384 221636 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccccc1 10.1021/acs.jmedchem.1c00563
CHEMBL5090853 222061 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccccc1F 10.1021/acs.jmedchem.1c00563
156014680 184029 0 None -2 2 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635960 184029 0 None -2 2 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
59497075 121359 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 376 4 0 3 4.7 O=c1c(C(F)(F)F)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1 10.1021/jm500496m
CHEMBL3337525 121359 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 376 4 0 3 4.7 O=c1c(C(F)(F)F)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1 10.1021/jm500496m
46917791 64519 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 472 6 0 4 6.7 CCCn1ccc2cc(-c3ccc(OCc4ccc(C(F)(F)F)nc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669400 64519 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 472 6 0 4 6.7 CCCn1ccc2cc(-c3ccc(OCc4ccc(C(F)(F)F)nc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
90668094 116316 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221833 116316 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
69344751 116317 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221834 116317 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
58966955 116320 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 337 7 0 4 4.0 CCCn1ccc2c(OCCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221837 116320 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 337 7 0 4 4.0 CCCn1ccc2c(OCCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
90668103 116329 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 340 6 0 3 4.6 CCCn1ccc2c(N(Cl)CCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221845 116329 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 340 6 0 3 4.6 CCCn1ccc2c(N(Cl)CCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
49801371 165520 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093620 165520 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
53326074 64502 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 328 5 0 4 4.0 CCCn1ccc2cc(OCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669384 64502 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 328 5 0 4 4.0 CCCn1ccc2cc(OCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46225334 206825 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 358 3 0 4 3.7 Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595607 206825 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 358 3 0 4 3.7 Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225583 206953 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL596527 206953 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
24815883 208241 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL604993 208241 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
53325603 64496 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assayAgonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assay
ChEMBL 306 3 0 4 2.9 CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669377 64496 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assayAgonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assay
ChEMBL 306 3 0 4 2.9 CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
21393580 15465 0 None - 1 Human 4.6 pEC50 = 4.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 253 3 0 2 3.3 O=C1OC(Cc2ccccc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1095704 15465 0 None - 1 Human 4.6 pEC50 = 4.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 253 3 0 2 3.3 O=C1OC(Cc2ccccc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
60096211 96834 0 None -1 4 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL2381649 96834 0 None -1 4 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
1310 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
1369 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
33032 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
44272391 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
88747398 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
CHEMBL575060 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
DB00142 9095 110 None -389 17 Human 5.6 pEC50 = 5.6 Functional
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
69093106 90681 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)ccc(F)c1F 10.1021/jm300912k
CHEMBL2206444 90681 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)ccc(F)c1F 10.1021/jm300912k
44591748 191820 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 311 5 0 3 4.1 CCOc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL485528 191820 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 311 5 0 3 4.1 CCOc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1 10.1016/j.bmcl.2009.03.032
60096183 166063 0 None -3 2 Human 7.6 pEC50 = 7.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL4099470 166063 0 None -3 2 Human 7.6 pEC50 = 7.6 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
24809650 81360 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 326 6 0 5 3.5 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1OC 10.1021/jm2016864
CHEMBL2029792 81360 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 326 6 0 5 3.5 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1OC 10.1021/jm2016864
162665716 189148 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 323 5 0 4 4.0 c1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4784990 189148 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 323 5 0 4 4.0 c1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
1310 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
1369 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
33032 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
44272391 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
88747398 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
CHEMBL575060 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
DB00142 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
1310 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
1369 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
33032 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
44272391 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
88747398 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
CHEMBL575060 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
DB00142 9095 110 None -389 17 Human 4.6 pEC50 = 4.6 Functional
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
25173365 191584 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 5 0 3 3.6 CC1CN(Cc2ccc(OCc3ccccc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL485175 191584 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 5 0 3 3.6 CC1CN(Cc2ccc(OCc3ccccc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
70685767 81384 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 371 5 0 5 4.6 Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)c(C)n1 10.1021/jm2016864
CHEMBL2029814 81384 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 371 5 0 5 4.6 Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)c(C)n1 10.1021/jm2016864
CHEMBL5073573 221079 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc([N+](=O)[O-])c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
9815616 121578 6 None -2 4 Rat 5.6 pEC50 = 5.6 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
CHEMBL334014 121578 6 None -2 4 Rat 5.6 pEC50 = 5.6 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
71136188 152533 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 384 3 1 6 1.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21 nan
CHEMBL3916627 152533 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 384 3 1 6 1.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21 nan
155515810 176793 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(F)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4442487 176793 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(F)cccc32)cn1 10.1021/acs.jmedchem.8b00161
3954 7451 60 None 6 2 Human 7.6 pEC50 = 7.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1016/j.bmcl.2009.11.008
9868580 7451 60 None 6 2 Human 7.6 pEC50 = 7.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1016/j.bmcl.2009.11.008
CHEMBL593013 7451 60 None 6 2 Human 7.6 pEC50 = 7.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1016/j.bmcl.2009.11.008
49765871 8926 45 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
6317 8926 45 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
CHEMBL2179319 8926 45 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
162677102 190305 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 401 5 0 4 4.8 Brc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4799882 190305 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 401 5 0 4 4.8 Brc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
155511507 176373 1 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 239 2 0 3 2.6 CCCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4436220 176373 1 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 239 2 0 3 2.6 CCCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
44156621 15508 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 7 0 4 3.4 CCCCCCC1CN(c2cccc(S(C)(=O)=O)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1096080 15508 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 7 0 4 3.4 CCCCCCC1CN(c2cccc(S(C)(=O)=O)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
134131309 148952 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay
ChEMBL 359 2 0 3 6.1 Clc1cccc(Cl)c1-c1ccn2c(C3CCCCCC3)nnc2c1 10.1016/j.bmc.2016.11.018
CHEMBL3883923 148952 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay
ChEMBL 359 2 0 3 6.1 Clc1cccc(Cl)c1-c1ccn2c(C3CCCCCC3)nnc2c1 10.1016/j.bmc.2016.11.018
67060140 174176 0 None -26 2 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
CHEMBL4295230 174176 0 None -26 2 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
162661604 188282 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 307 4 0 4 3.1 COc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4764905 188282 0 None - 1 Human 5.6 pEC50 = 5.6 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 307 4 0 4 3.1 COc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
44591746 191694 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1cccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)c1 10.1016/j.bmcl.2009.03.032
CHEMBL485330 191694 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1cccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)c1 10.1016/j.bmcl.2009.03.032
70685766 81380 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 4.9 Cc1ncccc1Oc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
CHEMBL2029810 81380 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 4.9 Cc1ncccc1Oc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
60096231 164434 15 None -48 4 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assay
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
CHEMBL4081453 164434 15 None -48 4 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assay
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
44591715 198254 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3ccccc3Cl)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL519341 198254 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3ccccc3Cl)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
117967312 149088 3 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay
ChEMBL 347 5 0 4 4.3 FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885353 149088 3 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay
ChEMBL 347 5 0 4 4.3 FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
117967312 149088 3 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.3 FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885353 149088 3 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.3 FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
155551721 182208 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 337 3 0 3 4.9 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4576215 182208 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 337 3 0 3 4.9 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
51357935 68750 0 None - 1 Rat 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 372 3 0 4 4.4 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(Cl)cc1F 10.1021/jm101414h
CHEMBL1774229 68750 0 None - 1 Rat 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 372 3 0 4 4.4 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(Cl)cc1F 10.1021/jm101414h
168299593 199511 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 385 7 0 5 4.7 CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5220316 199511 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 385 7 0 5 4.7 CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
71116726 152054 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 438 3 0 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21 nan
CHEMBL3912982 152054 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 438 3 0 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21 nan
137652500 163968 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075697 163968 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
71128768 151358 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 441 4 0 7 2.7 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
CHEMBL3907644 151358 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 441 4 0 7 2.7 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
44591714 191080 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3cccc(F)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484127 191080 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3cccc(F)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL5069547 220998 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(F)cc1 10.1021/acs.jmedchem.1c00563
118714743 121344 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 335 4 0 4 3.8 CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337509 121344 0 None - 1 Human 6.6 pEC50 = 6.6 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 335 4 0 4 3.8 CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
25010196 68737 0 None - 1 Rat 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cccnc21 10.1021/jm101414h
CHEMBL1774111 68737 0 None - 1 Rat 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cccnc21 10.1021/jm101414h
134131502 148930 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 363 5 0 4 5.1 Clc1c(OCc2ccc3ccccc3c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3883585 148930 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 363 5 0 4 5.1 Clc1c(OCc2ccc3ccccc3c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
155525998 177814 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 371 3 0 3 5.3 Fc1cc(C(F)(F)F)ccc1-c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4456816 177814 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 371 3 0 3 5.3 Fc1cc(C(F)(F)F)ccc1-c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
9815616 121578 6 None -2 4 Rat 7.5 pEC50 = 7.5 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
CHEMBL334014 121578 6 None -2 4 Rat 7.5 pEC50 = 7.5 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
66785010 162642 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4060306 162642 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
66787433 163242 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4067298 163242 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
49801369 165528 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4093792 165528 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
25073303 173812 0 None 11 2 Rat 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 348 4 0 5 3.4 Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
CHEMBL4288731 173812 0 None 11 2 Rat 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 348 4 0 5 3.4 Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
156018381 184701 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4645305 184701 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
70689923 81361 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 336 7 0 4 4.2 CC(C)CCn1ccc(-c2ccc(OCC3CC3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029793 81361 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 336 7 0 4 4.2 CC(C)CCn1ccc(-c2ccc(OCC3CC3)cc2)c(C#N)c1=O 10.1021/jm2016864
155524603 177705 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 322 2 0 4 3.3 Clc1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4455228 177705 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 322 2 0 4 3.3 Clc1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL5091768 222104 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(-c4ccc(Cl)cc4)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
11690196 149544 0 None 4 2 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 416 7 2 7 4.5 CC(=O)c1ccc(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)cc2)c(C)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3892611 149544 0 None 4 2 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 416 7 2 7 4.5 CC(=O)c1ccc(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)cc2)c(C)c1O 10.1016/j.bmcl.2016.11.049
156018381 184701 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4645305 184701 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
118714734 121334 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 296 6 0 4 3.3 CC(C)CCn1ccc(OCc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337499 121334 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 296 6 0 4 3.3 CC(C)CCn1ccc(OCc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
57459483 89428 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 345 4 0 5 3.9 CCCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179331 89428 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 345 4 0 5 3.9 CCCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
51357937 68753 0 None 2 2 Human 8.5 pEC50 = 8.5 Functional
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774233 68753 0 None 2 2 Human 8.5 pEC50 = 8.5 Functional
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
60096201 165347 0 None -5 2 Human 8.4 pEC50 = 8.4 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4091735 165347 0 None -5 2 Human 8.4 pEC50 = 8.4 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
10198133 213287 12 None 1 4 Human 8.4 pEC50 = 8.4 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL8839 213287 12 None 1 4 Human 8.4 pEC50 = 8.4 Functional
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
10198133 213287 12 None 1 4 Human 8.4 pEC50 = 8.4 Functional
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
CHEMBL8839 213287 12 None 1 4 Human 8.4 pEC50 = 8.4 Functional
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
42629118 191038 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 319 3 0 2 4.5 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL483750 191038 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 319 3 0 2 4.5 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
70696264 81389 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 407 6 0 5 5.6 CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029819 81389 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 407 6 0 5 5.6 CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
162662455 188801 3 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 419 7 0 5 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4780781 188801 3 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 419 7 0 5 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1 10.1016/j.ejmech.2019.111881
146036862 182417 6 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 279 2 0 3 3.4 Brc1cccc2c1nnn2CC1CCCC1 10.1021/acs.jmedchem.8b00161
CHEMBL4580916 182417 6 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 279 2 0 3 3.4 Brc1cccc2c1nnn2CC1CCCC1 10.1021/acs.jmedchem.8b00161
162662455 188801 3 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 419 7 0 5 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1 10.1021/acs.jmedchem.1c00563
CHEMBL4780781 188801 3 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 419 7 0 5 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1 10.1021/acs.jmedchem.1c00563
CHEMBL5085978 221785 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)cc1 10.1021/acs.jmedchem.1c00563
66785087 164919 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4087196 164919 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
11362035 6831 1 None - 1 Human 7.5 pEC50 = 7.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2009.11.008
6328 6831 1 None - 1 Human 7.5 pEC50 = 7.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2009.11.008
6329 6831 1 None - 1 Human 7.5 pEC50 = 7.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2009.11.008
CHEMBL105296 6831 1 None - 1 Human 7.5 pEC50 = 7.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2009.11.008
156010124 183810 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4632373 183810 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
1377 8122 26 None 1 8 Rat 6.5 pEC50 = 6.5 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm030967o
5310979 8122 26 None 1 8 Rat 6.5 pEC50 = 6.5 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm030967o
CHEMBL284193 8122 26 None 1 8 Rat 6.5 pEC50 = 6.5 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm030967o
1368 9070 37 None -1 11 Rat 6.5 pEC50 = 6.5 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm030967o
5310956 9070 37 None -1 11 Rat 6.5 pEC50 = 6.5 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm030967o
CHEMBL280563 9070 37 None -1 11 Rat 6.5 pEC50 = 6.5 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm030967o
44361316 41746 2 None - 1 Rat 6.5 pEC50 = 6.5 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 217 5 4 4 -1.2 N[C@H](C(=O)O)[C@H]1[C@H](CC(=O)O)[C@@H]1C(=O)O 10.1021/jm030967o
CHEMBL143267 41746 2 None - 1 Rat 6.5 pEC50 = 6.5 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 217 5 4 4 -1.2 N[C@H](C(=O)O)[C@H]1[C@H](CC(=O)O)[C@@H]1C(=O)O 10.1021/jm030967o
1392 6861 48 None 5 4 Rat 6.5 pEC50 = 6.5 Functional
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
5310984 6861 48 None 5 4 Rat 6.5 pEC50 = 6.5 Functional
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
CHEMBL40086 6861 48 None 5 4 Rat 6.5 pEC50 = 6.5 Functional
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
521212 74108 59 None - 1 Human 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 209 2 0 3 2.5 c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL1884989 74108 59 None - 1 Human 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 209 2 0 3 2.5 c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
156010124 183810 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4632373 183810 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
44591812 199332 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 324 5 0 3 3.8 C[C@@H]1CN(Cc2ccc(-c3ccc(CN(C)C)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL521175 199332 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 324 5 0 3 3.8 C[C@@H]1CN(Cc2ccc(-c3ccc(CN(C)C)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
59599459 156208 0 None 1 2 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3ncccc3-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3945882 156208 0 None 1 2 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3ncccc3-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
118714740 121341 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 5 0 6 2.5 CC(C)CCn1ccc(N2CCN(c3ccccn3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337506 121341 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 5 0 6 2.5 CC(C)CCn1ccc(N2CCN(c3ccccn3)CC2)c(C#N)c1=O 10.1021/jm500496m
57459482 90675 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 433 4 0 6 4.2 COc1c(F)cccc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2C#N)CC1 10.1021/jm300912k
CHEMBL2206438 90675 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 433 4 0 6 4.2 COc1c(F)cccc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2C#N)CC1 10.1021/jm300912k
118714756 121356 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3c(F)cccc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337522 121356 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3c(F)cccc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
44178197 68755 0 None 1 2 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774235 68755 0 None 1 2 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL5078863 221370 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
25073615 173243 0 None 4 2 Rat 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 300 3 0 5 2.4 CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1 10.1016/j.bmcl.2018.08.022
CHEMBL4278070 173243 0 None 4 2 Rat 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 300 3 0 5 2.4 CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1 10.1016/j.bmcl.2018.08.022
25002940 7890 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 10.1021/jm2016864
6320 7890 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 10.1021/jm2016864
CHEMBL2029821 7890 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 10.1021/jm2016864
53326709 64513 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 405 6 0 5 5.1 CCCn1ccc2cc(-c3ccc(OCc4cccnc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669394 64513 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 405 6 0 5 5.1 CCCn1ccc2cc(-c3ccc(OCc4cccnc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53324151 64514 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 327 4 0 3 4.7 CCCn1ccc2cc(-c3ccc(OC)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669395 64514 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 327 4 0 3 4.7 CCCn1ccc2cc(-c3ccc(OC)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
90668099 116324 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 322 6 1 4 4.0 CCCn1ccc2c(NCc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221840 116324 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 322 6 1 4 4.0 CCCn1ccc2c(NCc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
156017237 184540 0 None 1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4642761 184540 0 None 1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
53317704 64503 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 327 5 1 4 4.1 CCCn1ccc2cc(NCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669385 64503 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 327 5 1 4 4.1 CCCn1ccc2cc(NCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46225582 208394 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL605831 208394 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
118714738 121339 0 None - 1 Human 4.5 pEC50 = 4.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 273 4 0 4 2.8 CC(C)CCn1ccc(N2CCCCC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337504 121339 0 None - 1 Human 4.5 pEC50 = 4.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 273 4 0 4 2.8 CC(C)CCn1ccc(N2CCCCC2)c(C#N)c1=O 10.1021/jm500496m
70683629 81357 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 296 5 0 4 3.4 COc1cccc(-c2ccn(CCC(C)C)c(=O)c2C#N)c1 10.1021/jm2016864
CHEMBL2029788 81357 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 296 5 0 4 3.4 COc1cccc(-c2ccn(CCC(C)C)c(=O)c2C#N)c1 10.1021/jm2016864
11951099 74253 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 479 8 1 5 7.1 CCCc1c(OCc2cccc(-c3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL189264 74253 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 479 8 1 5 7.1 CCCc1c(OCc2cccc(-c3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
59599568 152828 0 None -1 2 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3918914 152828 0 None -1 2 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
44591772 198246 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 369 4 0 3 4.7 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL519332 198246 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 369 4 0 3 4.7 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
117972047 148949 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 327 6 0 4 4.0 Clc1c(OCCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3883827 148949 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 327 6 0 4 4.0 Clc1c(OCCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
46215876 87582 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 374 2 1 3 5.1 N#Cc1c(-c2cc(Cl)c3[nH]ccc3c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152116 87582 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 374 2 1 3 5.1 N#Cc1c(-c2cc(Cl)c3[nH]ccc3c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
162670769 189747 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 341 5 0 4 4.2 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4793069 189747 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 341 5 0 4 4.2 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
156016100 184466 0 None -1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4641860 184466 0 None -1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156017237 184540 0 None 1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4642761 184540 0 None 1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
71136746 155379 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
CHEMBL3939174 155379 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
156015654 184300 0 None -1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4639821 184300 0 None -1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156016100 184466 0 None -1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4641860 184466 0 None -1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
11631795 71573 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2ccccn2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL181953 71573 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2ccccn2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
155531978 178511 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 363 3 0 5 4.2 N#Cc1cccc2c1nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1 10.1021/acs.jmedchem.8b00161
CHEMBL4467158 178511 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 363 3 0 5 4.2 N#Cc1cccc2c1nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1 10.1021/acs.jmedchem.8b00161
51357934 68749 0 None - 1 Rat 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1 10.1021/jm101414h
CHEMBL1774227 68749 0 None - 1 Rat 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1 10.1021/jm101414h
66784529 163872 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4074421 163872 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
71451227 87581 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 438 3 1 5 5.4 N#Cc1c(-c2ccc3c(ccn3[C@H]3CC[C@H](O)CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152115 87581 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 438 3 1 5 5.4 N#Cc1c(-c2ccc3c(ccn3[C@H]3CC[C@H](O)CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
25073303 173812 0 None -11 2 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 348 4 0 5 3.4 Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
CHEMBL4288731 173812 0 None -11 2 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 348 4 0 5 3.4 Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
156015654 184300 0 None -1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4639821 184300 0 None -1 2 Human 6.5 pEC50 = 6.5 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
44155754 15284 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 262 6 1 3 3.6 CCCCCCC1CN(c2cccc(N)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094146 15284 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 262 6 1 3 3.6 CCCCCCC1CN(c2cccc(N)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44300258 20423 0 None - 1 Rat 4.5 pEC50 = 4.5 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1194540 20423 0 None - 1 Rat 4.5 pEC50 = 4.5 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL552836 20423 0 None - 1 Rat 4.5 pEC50 = 4.5 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1 10.1016/s0960-894x(01)00329-8
51357396 68729 0 None - 1 Rat 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3cccc(F)c3)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL1774102 68729 0 None - 1 Rat 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3cccc(F)c3)CC2)nc2ccccc21 10.1021/jm101414h
118714737 121338 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 349 5 0 4 4.2 CC(C)CCn1ccc(N2CCCC(c3ccccc3)C2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337503 121338 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 349 5 0 4 4.2 CC(C)CCn1ccc(N2CCCC(c3ccccc3)C2)c(C#N)c1=O 10.1021/jm500496m
71117091 156128 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 412 4 1 6 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(NC(=O)C4CCCO4)CC3)nc21 nan
CHEMBL3945222 156128 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 412 4 1 6 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(NC(=O)C4CCCO4)CC3)nc21 nan
127030385 145941 0 None - 1 Rat 4.5 pEC50 = 4.5 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 217 5 4 4 -1.0 N[C@@H](C[C@]1(C(=O)O)C[C@@H]1C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL3787264 145941 0 None - 1 Rat 4.5 pEC50 = 4.5 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 217 5 4 4 -1.0 N[C@@H](C[C@]1(C(=O)O)C[C@@H]1C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
137635882 162673 0 None 1 2 Human 5.5 pEC50 = 5.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4060567 162673 0 None 1 2 Human 5.5 pEC50 = 5.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
9815617 121277 7 None -1 2 Rat 7.5 pEC50 = 7.5 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
CHEMBL333519 121277 7 None -1 2 Rat 7.5 pEC50 = 7.5 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
1393 8321 64 None 2 6 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
1396 8321 64 None 2 6 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
213056 8321 64 None 2 6 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
CHEMBL8759 8321 64 None 2 6 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
11187949 72377 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL183319 72377 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
162649047 186570 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 341 5 0 3 4.2 Fc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
CHEMBL4744761 186570 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 341 5 0 3 4.2 Fc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
44591796 191422 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 304 3 0 3 3.4 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484957 191422 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 304 3 0 3 3.4 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
24905705 190801 1 None - 1 Rat 4.5 pEC50 = 4.5 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL482081 190801 1 None - 1 Rat 4.5 pEC50 = 4.5 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
46887319 15765 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 283 4 0 3 3.4 Cc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL1098388 15765 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 283 4 0 3 3.4 Cc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
25003298 81379 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.7 CCCCn1ccc(-c2ccc(Oc3cccnc3C)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029809 81379 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.7 CCCCn1ccc(-c2ccc(Oc3cccnc3C)cc2)c(C#N)c1=O 10.1021/jm2016864
10047169 9998 1 None - 1 Human 6.5 pEC50 = 6.5 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.09.028
1403 9998 1 None - 1 Human 6.5 pEC50 = 6.5 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.09.028
CHEMBL182371 9998 1 None - 1 Human 6.5 pEC50 = 6.5 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.09.028
10047169 9998 1 None - 1 Human 6.5 pEC50 = 6.5 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2005.06.017
1403 9998 1 None - 1 Human 6.5 pEC50 = 6.5 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2005.06.017
CHEMBL182371 9998 1 None - 1 Human 6.5 pEC50 = 6.5 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2005.06.017
44591713 191079 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3ccccc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484126 191079 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3ccccc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
118714753 121353 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 363 5 0 5 3.5 COc1ccccc1C1CCN(c2ccn(CC3CC3)c(=O)c2C#N)CC1 10.1021/jm500496m
CHEMBL3337519 121353 0 None - 1 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 363 5 0 5 3.5 COc1ccccc1C1CCN(c2ccn(CC3CC3)c(=O)c2C#N)CC1 10.1021/jm500496m
44178197 68755 0 None -1 2 Rat 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774235 68755 0 None -1 2 Rat 7.5 pEC50 = 7.5 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
51354020 68756 0 None 23 2 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 422 4 0 5 4.6 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/acs.jmedchem.1c00563
CHEMBL1774236 68756 0 None 23 2 Human 7.5 pEC50 = 7.5 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 422 4 0 5 4.6 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/acs.jmedchem.1c00563
1393 8321 64 None -2 6 Rat 7.5 pEC50 = 7.5 Functional
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
1396 8321 64 None -2 6 Rat 7.5 pEC50 = 7.5 Functional
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
213056 8321 64 None -2 6 Rat 7.5 pEC50 = 7.5 Functional
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
CHEMBL8759 8321 64 None -2 6 Rat 7.5 pEC50 = 7.5 Functional
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
71457756 90677 0 None 66 2 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL2206440 90677 0 None 66 2 Human 7.5 pEC50 = 7.5 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
46887371 15575 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 4 0 3 4.4 CC(C)(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL1096712 15575 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 4 0 3 4.4 CC(C)(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
162661233 188291 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.3 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
CHEMBL4765006 188291 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.3 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
CHEMBL5076606 221231 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
136950 15466 26 None - 1 Human 5.5 pEC50 = 5.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 269 4 0 3 3.1 O=C1OC(COc2ccccc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1095705 15466 26 None - 1 Human 5.5 pEC50 = 5.5 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 269 4 0 3 3.1 O=C1OC(COc2ccccc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
59066632 213349 89 None 1 2 Human 4.5 pEC50 = 4.5 Functional
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9602569
92136 213349 89 None 1 2 Human 4.5 pEC50 = 4.5 Functional
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9602569
CHEMBL88804 213349 89 None 1 2 Human 4.5 pEC50 = 4.5 Functional
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9602569
44300135 20056 0 None - 1 Rat 4.5 pEC50 = 4.5 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 279 4 4 5 -0.3 Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1016/s0960-894x(01)00329-8
CHEMBL1191723 20056 0 None - 1 Rat 4.5 pEC50 = 4.5 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 279 4 4 5 -0.3 Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1016/s0960-894x(01)00329-8
CHEMBL542862 20056 0 None - 1 Rat 4.5 pEC50 = 4.5 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 279 4 4 5 -0.3 Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1016/s0960-894x(01)00329-8
11951271 74285 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 447 10 1 6 5.7 CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL189516 74285 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 447 10 1 6 5.7 CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
118714746 121346 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 389 5 0 4 4.4 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCCC(F)(F)F)c1=O 10.1021/jm500496m
CHEMBL3337512 121346 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 389 5 0 4 4.4 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCCC(F)(F)F)c1=O 10.1021/jm500496m
71117198 157077 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 358 3 1 4 1.7 CN1c2nc(C3CCCNC3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
CHEMBL3952803 157077 0 None - 1 Human 6.5 pEC50 = 6.5 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 358 3 1 4 1.7 CN1c2nc(C3CCCNC3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
11950746 73867 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 419 9 1 6 5.1 CC(C)(C)Cn1ccc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
CHEMBL187342 73867 0 None - 1 Human 5.5 pEC50 = 5.5 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 419 9 1 6 5.1 CC(C)(C)Cn1ccc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
627502 15354 1 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2ccc(Cl)cc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1094733 15354 1 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2ccc(Cl)cc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
46887370 15574 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 311 5 0 3 4.2 CC(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
CHEMBL1096711 15574 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 311 5 0 3 4.2 CC(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
46887322 15768 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 297 5 0 3 3.7 CCc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL1098391 15768 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 297 5 0 3 3.7 CCc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
59391336 121333 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 294 6 0 3 3.6 CC(C)CCn1ccc(CCc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337498 121333 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 294 6 0 3 3.6 CC(C)CCn1ccc(CCc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
10176836 42648 0 None - 1 Rat 4.4 pEC50 = 4.4 Functional
Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 221 2 3 3 -0.2 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2CC1(F)F 10.1021/jm000346k
CHEMBL144201 42648 0 None - 1 Rat 4.4 pEC50 = 4.4 Functional
Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 221 2 3 3 -0.2 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2CC1(F)F 10.1021/jm000346k
70685762 81359 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 330 5 0 4 4.1 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1Cl 10.1021/jm2016864
CHEMBL2029791 81359 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 330 5 0 4 4.1 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1Cl 10.1021/jm2016864
69093439 90680 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206443 90680 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
71457756 90677 0 None 66 2 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL2206440 90677 0 None 66 2 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
155560423 181854 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 387 3 0 3 5.8 FC(F)(F)c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4568356 181854 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 387 3 0 3 5.8 FC(F)(F)c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
44300820 20150 0 None -1 2 Rat 4.4 pEC50 = 4.4 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 265 4 3 5 -0.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1192558 20150 0 None -1 2 Rat 4.4 pEC50 = 4.4 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 265 4 3 5 -0.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL543811 20150 0 None -1 2 Rat 4.4 pEC50 = 4.4 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 265 4 3 5 -0.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1 10.1016/s0960-894x(01)00329-8
68108457 155335 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL3938796 155335 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
25002941 81392 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 391 6 0 5 5.1 CCCCn1ccc(-c2ccc(Oc3cc(C)nc(C)c3)c(F)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029823 81392 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 391 6 0 5 5.1 CCCCn1ccc(-c2ccc(Oc3cc(C)nc(C)c3)c(F)c2)c(C#N)c1=O 10.1021/jm2016864
66786069 163240 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4067290 163240 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
44591794 191420 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 370 4 0 4 4.1 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484956 191420 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 370 4 0 4 4.1 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
44155534 15456 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 261 6 0 2 4.3 CCCCCCC1CN(c2ccc(C)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095638 15456 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 261 6 0 2 4.3 CCCCCCC1CN(c2ccc(C)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44591647 191586 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 5 0 4 4.1 O=C1OC2(CCOCC2)CN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL485176 191586 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 5 0 4 4.1 O=C1OC2(CCOCC2)CN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
11531272 71976 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 392 10 1 4 5.4 Cc1c(OCCCCOc2cccc(F)c2F)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182511 71976 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 392 10 1 4 5.4 Cc1c(OCCCCOc2cccc(F)c2F)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
11710164 73110 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL185046 73110 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
57459481 89413 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 340 3 0 4 4.3 CCc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179315 89413 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 340 3 0 4 4.3 CCc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
23770349 15682 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2ccccc2Cl)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1097656 15682 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2ccccc2Cl)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
57459635 89419 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 418 4 0 4 5.2 FC(F)(F)c1c(N2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179322 89419 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 418 4 0 4 5.2 FC(F)(F)c1c(N2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
59599552 155082 0 None 12 2 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 437 7 2 8 4.2 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(Cl)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3936830 155082 0 None 12 2 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 437 7 2 8 4.2 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(Cl)c1O 10.1016/j.bmcl.2016.11.049
71135411 130175 0 None 5 2 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616848 130175 0 None 5 2 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
25002939 81391 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 377 6 0 5 4.8 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2F)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029822 81391 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 377 6 0 5 4.8 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2F)c(C#N)c1=O 10.1021/jm2016864
CHEMBL5083201 221630 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Cl)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
71136199 149465 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 423 3 0 7 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
CHEMBL3892060 149465 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 423 3 0 7 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
11310142 9200 19 None 13 3 Human 6.4 pEC50 = 6.4 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
11614 9200 19 None 13 3 Human 6.4 pEC50 = 6.4 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
CHEMBL192051 9200 19 None 13 3 Human 6.4 pEC50 = 6.4 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
25002587 81377 4 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.7 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029807 81377 4 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.7 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2)c(C#N)c1=O 10.1021/jm2016864
53320818 64510 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 346 4 0 4 4.3 CCCn1ccc2cc(-c3cnc(OC)c(F)c3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669391 64510 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 346 4 0 4 4.3 CCCn1ccc2cc(-c3cnc(OC)c(F)c3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53325452 64518 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 438 6 0 4 6.4 CCCn1ccc2cc(-c3ccc(OCc4ccc(Cl)nc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669399 64518 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 438 6 0 4 6.4 CCCn1ccc2cc(-c3ccc(OCc4ccc(Cl)nc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
90668096 116319 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 350 7 0 4 4.1 CCCn1ccc2c(N(C)CCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221836 116319 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 350 7 0 4 4.1 CCCn1ccc2c(N(C)CCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
53324803 64500 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 299 3 0 4 3.5 CCCn1ccc2cc(-c3cncnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669382 64500 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 299 3 0 4 3.5 CCCn1ccc2cc(-c3cncnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
24815439 208714 1 None -18 2 Human 5.4 pEC50 = 5.4 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL607689 208714 1 None -18 2 Human 5.4 pEC50 = 5.4 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225581 208766 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL608103 208766 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
44361401 38115 0 None 1 5 Rat 8.4 pEC50 = 8.4 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
CHEMBL140197 38115 0 None 1 5 Rat 8.4 pEC50 = 8.4 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
117972155 149033 0 None - 1 Human 8.4 pEC50 = 8.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@@H]2C[C@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884833 149033 0 None - 1 Human 8.4 pEC50 = 8.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@@H]2C[C@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
71457757 90686 0 None - 1 Human 8.4 pEC50 = 8.4 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 466 5 0 5 5.4 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/jm300912k
CHEMBL2206449 90686 0 None - 1 Human 8.4 pEC50 = 8.4 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 466 5 0 5 5.4 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/jm300912k
71137012 130178 0 None 11 2 Human 8.4 pEC50 = 8.4 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616851 130178 0 None 11 2 Human 8.4 pEC50 = 8.4 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
162654912 187431 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 387 6 0 4 4.1 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)c(Cl)c1 10.1016/j.ejmech.2019.111881
CHEMBL4755035 187431 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 387 6 0 4 4.1 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)c(Cl)c1 10.1016/j.ejmech.2019.111881
162674461 190110 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 403 6 0 4 4.4 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(C(F)(F)F)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4797417 190110 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 403 6 0 4 4.4 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(C(F)(F)F)cc1 10.1016/j.ejmech.2019.111881
CHEMBL5083122 221621 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1Cc1ccc(Cl)cc1 10.1021/acs.jmedchem.1c00563
66785551 163932 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075258 163932 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
66784675 163953 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4075537 163953 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
162642952 188516 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 373 5 0 3 5.2 Clc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(Cl)c1 10.1016/j.ejmech.2019.111881
CHEMBL4777206 188516 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 373 5 0 3 5.2 Clc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(Cl)c1 10.1016/j.ejmech.2019.111881
155554782 181377 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 203 3 0 4 1.9 COc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4557213 181377 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 203 3 0 4 1.9 COc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
57459524 89421 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 358 3 0 4 4.2 FC(F)(F)c1c(N2Cc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179324 89421 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 358 3 0 4 4.2 FC(F)(F)c1c(N2Cc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
10474978 20231 0 None 1 2 Rat 5.4 pEC50 = 5.4 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1 10.1016/s0960-894x(01)00329-8
CHEMBL1193146 20231 0 None 1 2 Rat 5.4 pEC50 = 5.4 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1 10.1016/s0960-894x(01)00329-8
CHEMBL544508 20231 0 None 1 2 Rat 5.4 pEC50 = 5.4 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1 10.1016/s0960-894x(01)00329-8
59599576 149317 0 None -5 2 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 9 2 6 5.0 CCCc1c(OCc2cccc(Oc3cc(C(=O)O)ccn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3890848 149317 0 None -5 2 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 9 2 6 5.0 CCCc1c(OCc2cccc(Oc3cc(C(=O)O)ccn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
44591745 199123 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL520677 199123 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1 10.1016/j.bmcl.2009.03.032
68109677 163972 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4075762 163972 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66786493 164039 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4076639 164039 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
46887415 15314 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 299 5 0 4 3.1 COc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL1094415 15314 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 299 5 0 4 3.1 COc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
70685764 81365 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 358 6 0 4 5.2 CC(C)CCn1ccc(-c2ccc(Oc3ccccc3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029797 81365 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 358 6 0 4 5.2 CC(C)CCn1ccc(-c2ccc(Oc3ccccc3)cc2)c(C#N)c1=O 10.1021/jm2016864
137659992 166015 0 None -8 2 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4098939 166015 0 None -8 2 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
162645511 186377 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 305 5 0 3 3.9 c1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4742196 186377 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 305 5 0 3 3.9 c1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
44392708 72854 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 423 11 1 7 4.7 Cc1c(OCCCCOc2ccc(-n3cncn3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL183807 72854 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 423 11 1 7 4.7 Cc1c(OCCCCOc2ccc(-n3cncn3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
25008615 68734 0 None 1 2 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21 10.1021/jm101414h
CHEMBL1774108 68734 0 None 1 2 Human 7.4 pEC50 = 7.4 Functional
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21 10.1021/jm101414h
71116772 154447 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 456 4 1 8 3.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21 nan
CHEMBL3931730 154447 0 None - 1 Human 7.4 pEC50 = 7.4 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 456 4 1 8 3.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21 nan
44591793 191131 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 269 3 0 4 2.5 C[C@@H]1CN(Cc2ccc(-c3cncnc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484403 191131 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 269 3 0 4 2.5 C[C@@H]1CN(Cc2ccc(-c3cncnc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
71137008 130182 0 None 7 2 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616855 130182 0 None 7 2 Human 7.4 pEC50 = 7.4 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
156019582 184790 0 None 2 2 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4646555 184790 0 None 2 2 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
3954 7451 60 None -6 2 Rat 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm5000563
9868580 7451 60 None -6 2 Rat 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm5000563
CHEMBL593013 7451 60 None -6 2 Rat 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm5000563
44155643 15621 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 281 6 0 2 4.6 CCCCCCC1CN(c2ccc(Cl)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1097053 15621 0 None - 1 Human 5.4 pEC50 = 5.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 281 6 0 2 4.6 CCCCCCC1CN(c2ccc(Cl)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
156019582 184790 0 None 2 2 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4646555 184790 0 None 2 2 Human 6.4 pEC50 = 6.4 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
46227795 206742 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 357 2 0 3 5.3 CC(C)(C)c1ccc(-c2ccn3c(CC(F)(F)F)cnc3c2C#N)cc1 10.1016/j.bmcl.2009.11.008
CHEMBL595043 206742 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 357 2 0 3 5.3 CC(C)(C)c1ccc(-c2ccn3c(CC(F)(F)F)cnc3c2C#N)cc1 10.1016/j.bmcl.2009.11.008
46227792 206871 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 415 3 0 7 3.0 Cc1cc(C)nc(N2CCN(c3ccn4c(CC(F)(F)F)cnc4c3C#N)CC2)n1 10.1016/j.bmcl.2009.11.008
CHEMBL595967 206871 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 415 3 0 7 3.0 Cc1cc(C)nc(N2CCN(c3ccn4c(CC(F)(F)F)cnc4c3C#N)CC2)n1 10.1016/j.bmcl.2009.11.008
70689927 81375 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 4.9 Cc1cc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
CHEMBL2029805 81375 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 4.9 Cc1cc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
10822010 43160 1 None - 1 Rat 5.4 pEC50 = 5.4 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F 10.1021/jm000346k
CHEMBL144678 43160 1 None - 1 Rat 5.4 pEC50 = 5.4 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F 10.1021/jm000346k
1377 8122 26 None 1 8 Rat 7.4 pEC50 = 7.4 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm901523t
5310979 8122 26 None 1 8 Rat 7.4 pEC50 = 7.4 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm901523t
CHEMBL284193 8122 26 None 1 8 Rat 7.4 pEC50 = 7.4 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm901523t
11344646 133554 1 None 2 3 Human 7.4 pEC50 = 7.4 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm040222y
CHEMBL365368 133554 1 None 2 3 Human 7.4 pEC50 = 7.4 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm040222y
46887493 15356 1 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094762 15356 1 None - 1 Human 6.4 pEC50 = 6.4 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
11951449 73496 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 495 9 1 6 7.2 CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL185659 73496 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 495 9 1 6 7.2 CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
51356571 68746 0 None - 1 Rat 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.8 C[C@@H]1C[C@H](c2ccc(C(F)(F)F)cc2)CCN1Cc1nc2ncccc2n1C 10.1021/jm101414h
CHEMBL1774224 68746 0 None - 1 Rat 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.8 C[C@@H]1C[C@H](c2ccc(C(F)(F)F)cc2)CCN1Cc1nc2ncccc2n1C 10.1021/jm101414h
11494153 72855 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 356 10 1 4 5.2 Cc1c(OCCCCOc2ccccc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL183808 72855 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 356 10 1 4 5.2 Cc1c(OCCCCOc2ccccc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
118714752 121352 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 401 4 0 4 4.5 N#Cc1c(N2CCC(c3cccc(C(F)(F)F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337518 121352 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 401 4 0 4 4.5 N#Cc1c(N2CCC(c3cccc(C(F)(F)F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
71136640 130180 0 None 60 2 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616853 130180 0 None 60 2 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
53240406 130174 17 None 107 4 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 130174 17 None 107 4 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
70689925 81371 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 295 5 1 4 3.5 CNc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
CHEMBL2029801 81371 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 295 5 1 4 3.5 CNc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
118714741 121342 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 364 6 0 5 3.1 CC(C)CCn1ccc(N2CCN(Cc3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337507 121342 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 364 6 0 5 3.1 CC(C)CCn1ccc(N2CCN(Cc3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
57459480 89409 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 347 4 0 6 3.1 COCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179311 89409 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 347 4 0 6 3.1 COCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
60096231 164434 15 None -48 4 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
CHEMBL4081453 164434 15 None -48 4 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
59599565 152093 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3913281 152093 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
44300587 19805 0 None 12 2 Rat 5.3 pEC50 = 5.3 Functional
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1189911 19805 0 None 12 2 Rat 5.3 pEC50 = 5.3 Functional
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL539761 19805 0 None 12 2 Rat 5.3 pEC50 = 5.3 Functional
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1 10.1016/s0960-894x(01)00329-8
162647052 186408 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1cccc(CCN2CCn3c(nc4ccccc43)C2)c1 10.1016/j.ejmech.2019.111881
CHEMBL4742843 186408 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1cccc(CCN2CCn3c(nc4ccccc43)C2)c1 10.1016/j.ejmech.2019.111881
156014680 184029 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635960 184029 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
70692086 81367 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3cccnc3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029799 81367 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3cccnc3)cc2)c(C#N)c1=O 10.1021/jm2016864
44591774 198872 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 268 3 0 3 3.1 C[C@@H]1CN(Cc2ccc(-c3ccncc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL520300 198872 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 268 3 0 3 3.1 C[C@@H]1CN(Cc2ccc(-c3ccncc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
54583299 68727 0 None - 1 Rat 5.3 pEC50 = 5.3 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 390 4 0 6 3.7 Cc1cc(C2CCN(Cc3nc4ccccc4n3C)CC2)nc(N2CCCC2)n1 10.1021/jm101414h
CHEMBL1774100 68727 0 None - 1 Rat 5.3 pEC50 = 5.3 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 390 4 0 6 3.7 Cc1cc(C2CCN(Cc3nc4ccccc4n3C)CC2)nc(N2CCCC2)n1 10.1021/jm101414h
118714751 121351 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 367 4 0 4 4.2 N#Cc1c(N2CCC(c3ccc(Cl)cc3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337517 121351 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 367 4 0 4 4.2 N#Cc1c(N2CCC(c3ccc(Cl)cc3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
25008615 68734 0 None -1 2 Rat 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21 10.1021/jm101414h
CHEMBL1774108 68734 0 None -1 2 Rat 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21 10.1021/jm101414h
53240406 130174 17 None 107 4 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 130174 17 None 107 4 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
71119170 155551 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 468 4 1 5 1.9 CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
CHEMBL3940610 155551 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 468 4 1 5 1.9 CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
1392 6861 48 None 5 4 Rat 6.3 pEC50 = 6.3 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(01)00329-8
5310984 6861 48 None 5 4 Rat 6.3 pEC50 = 6.3 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(01)00329-8
CHEMBL40086 6861 48 None 5 4 Rat 6.3 pEC50 = 6.3 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(01)00329-8
156014680 184029 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635960 184029 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
10330132 108159 1 None 10 2 Rat 5.3 pEC50 = 5.3 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 189 2 4 5 -2.2 NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1016/s0960-894x(99)00266-8
CHEMBL297150 108159 1 None 10 2 Rat 5.3 pEC50 = 5.3 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 189 2 4 5 -2.2 NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1016/s0960-894x(99)00266-8
1374 8862 35 None -19 4 Human 4.3 pEC50 = 4.3 Functional
Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor
ChEMBL 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 10.1021/jm060950g
5311455 8862 35 None -19 4 Human 4.3 pEC50 = 4.3 Functional
Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor
ChEMBL 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 10.1021/jm060950g
CHEMBL39372 8862 35 None -19 4 Human 4.3 pEC50 = 4.3 Functional
Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor
ChEMBL 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 10.1021/jm060950g
168299034 199460 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1ncn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5219080 199460 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1ncn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O 10.1021/acs.jmedchem.2c00969
118714750 121350 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 367 4 0 4 4.2 N#Cc1c(N2CCC(c3ccccc3Cl)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337516 121350 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 367 4 0 4 4.2 N#Cc1c(N2CCC(c3ccccc3Cl)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
168295099 199829 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 378 6 0 5 4.0 CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5219090 199829 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 378 6 0 5 4.0 CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5223017 199829 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 378 6 0 5 4.0 CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
46830123 7859 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
6321 7859 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
CHEMBL1094763 7859 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
46197780 12354 0 None -25 4 Rat 4.3 pEC50 = 4.3 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 273 7 4 4 -0.2 N[C@@H](CCP(=O)(O)CC(Cl)C(=O)O)C(=O)O 10.1021/jm901523t
CHEMBL1076865 12354 0 None -25 4 Rat 4.3 pEC50 = 4.3 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 273 7 4 4 -0.2 N[C@@H](CCP(=O)(O)CC(Cl)C(=O)O)C(=O)O 10.1021/jm901523t
44591684 191115 0 None - 1 Human 8.3 pEC50 = 8.3 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
CHEMBL484340 191115 0 None - 1 Human 8.3 pEC50 = 8.3 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
44361401 38115 0 None 1 5 Rat 8.3 pEC50 = 8.3 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
CHEMBL140197 38115 0 None 1 5 Rat 8.3 pEC50 = 8.3 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
1393 8321 64 None 2 6 Human 8.3 pEC50 = 8.3 Functional
Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm970719q
1396 8321 64 None 2 6 Human 8.3 pEC50 = 8.3 Functional
Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm970719q
213056 8321 64 None 2 6 Human 8.3 pEC50 = 8.3 Functional
Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm970719q
CHEMBL8759 8321 64 None 2 6 Human 8.3 pEC50 = 8.3 Functional
Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm970719q
1393 8321 64 None 2 6 Human 8.3 pEC50 = 8.3 Functional
Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/s0960-894x(98)00146-2
1396 8321 64 None 2 6 Human 8.3 pEC50 = 8.3 Functional
Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/s0960-894x(98)00146-2
213056 8321 64 None 2 6 Human 8.3 pEC50 = 8.3 Functional
Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/s0960-894x(98)00146-2
CHEMBL8759 8321 64 None 2 6 Human 8.3 pEC50 = 8.3 Functional
Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/s0960-894x(98)00146-2
71476419 130187 0 None 51 2 Human 8.3 pEC50 = 8.3 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616860 130187 0 None 51 2 Human 8.3 pEC50 = 8.3 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
71457756 90677 0 None 66 2 Human 8.3 pEC50 = 8.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL2206440 90677 0 None 66 2 Human 8.3 pEC50 = 8.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
71457756 90677 0 None 66 2 Human 8.3 pEC50 = 8.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL2206440 90677 0 None 66 2 Human 8.3 pEC50 = 8.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
117968589 149046 0 None - 1 Human 8.3 pEC50 = 8.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 423 6 0 4 5.7 CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(Cl)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3884936 149046 0 None - 1 Human 8.3 pEC50 = 8.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 423 6 0 4 5.7 CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(Cl)cc1 10.1016/j.bmc.2016.11.018
53240406 130174 17 None 107 4 Human 8.3 pEC50 = 8.3 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 130174 17 None 107 4 Human 8.3 pEC50 = 8.3 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
68109580 165304 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4091370 165304 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
162650622 186829 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 431 6 0 4 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1Br 10.1016/j.ejmech.2019.111881
CHEMBL4747716 186829 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 431 6 0 4 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1Br 10.1016/j.ejmech.2019.111881
162662472 188832 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 371 6 0 4 3.6 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1F 10.1016/j.ejmech.2019.111881
CHEMBL4781224 188832 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 371 6 0 4 3.6 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1F 10.1016/j.ejmech.2019.111881
155513095 176483 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 329 2 0 3 3.4 Brc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4437986 176483 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 329 2 0 3 3.4 Brc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
155540333 179275 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 338 3 0 4 4.3 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4483344 179275 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 338 3 0 4 4.3 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL5074997 221130 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1CC1CCC1 10.1021/acs.jmedchem.1c00563
CHEMBL5091657 222098 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Br)cc1F 10.1021/acs.jmedchem.1c00563
10807972 42591 1 None -3 4 Rat 7.3 pEC50 = 7.3 Functional
Antagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm000346k
CHEMBL144151 42591 1 None -3 4 Rat 7.3 pEC50 = 7.3 Functional
Antagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm000346k
104766 6822 42 None 2 14 Rat 5.3 pEC50 = 5.3 Functional
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
1365 6822 42 None 2 14 Rat 5.3 pEC50 = 5.3 Functional
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
CHEMBL34453 6822 42 None 2 14 Rat 5.3 pEC50 = 5.3 Functional
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
46215708 87580 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 424 3 0 5 5.3 N#Cc1c(-c2ccc3c(ccn3C3CCOCC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152114 87580 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 424 3 0 5 5.3 N#Cc1c(-c2ccc3c(ccn3C3CCOCC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
71450118 89425 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 330 3 0 4 4.2 CCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179328 89425 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 330 3 0 4 4.2 CCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
53320175 64511 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 390 5 0 4 5.9 CCCn1ccc2cc(-c3ccc(Oc4ccccc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669392 64511 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 390 5 0 4 5.9 CCCn1ccc2cc(-c3ccc(Oc4ccccc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
90668092 116314 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 306 6 1 3 4.1 CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221831 116314 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 306 6 1 3 4.1 CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
90668100 116325 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 322 6 1 4 4.0 CCCn1ccc2c(NCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221841 116325 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 322 6 1 4 4.0 CCCn1ccc2c(NCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
90668105 116331 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 356 6 0 4 4.6 CCCn1ccc2c(N(Cl)Cc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221847 116331 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 356 6 0 4 4.6 CCCn1ccc2c(N(Cl)Cc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
53325603 64496 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 306 3 0 4 2.9 CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669377 64496 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 306 3 0 4 2.9 CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53316861 64497 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 320 3 1 4 3.0 CCCn1ccc2cc(N3CCC(O)CC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669378 64497 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 320 3 1 4 3.0 CCCn1ccc2cc(N3CCC(O)CC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53323493 64506 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 341 4 0 4 4.2 CCCn1ccc2cc(-c3ccc(N(C)C)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669388 64506 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 341 4 0 4 4.2 CCCn1ccc2cc(-c3ccc(N(C)C)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
24849462 206537 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593744 206537 0 None - 1 Human 5.3 pEC50 = 5.3 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
90668104 116330 0 None - 1 Human 4.3 pEC50 = 4.3 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 326 5 0 3 4.6 CCCn1ccc2c(N(Cl)Cc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221846 116330 0 None - 1 Human 4.3 pEC50 = 4.3 Functional
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 326 5 0 3 4.6 CCCn1ccc2c(N(Cl)Cc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
60096194 163367 0 None -1 2 Human 6.3 pEC50 = 6.3 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 290 5 4 4 0.3 N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4068679 163367 0 None -1 2 Human 6.3 pEC50 = 6.3 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 290 5 4 4 0.3 N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
156014194 183989 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635373 183989 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156018860 184693 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4645193 184693 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
71117065 156054 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 539 3 1 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCN(C(=O)OC(C)(C)C)C5)CC4C3)nc21 nan
CHEMBL3944557 156054 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 539 3 1 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCN(C(=O)OC(C)(C)C)C5)CC4C3)nc21 nan
156014194 183989 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635373 183989 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156018860 184693 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4645193 184693 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
57459542 89424 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 401 4 0 5 4.5 FC(F)(F)c1c(N2CCC(c3cccnc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179327 89424 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 401 4 0 5 4.5 FC(F)(F)c1c(N2CCC(c3cccnc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
28407322 189616 9 None - 1 Human 5.3 pEC50 = 5.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 277 3 0 3 3.1 c1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4791292 189616 9 None - 1 Human 5.3 pEC50 = 5.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 277 3 0 3 3.1 c1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
3756397 15086 2 None -7 4 Rat 4.3 pEC50 = 4.3 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 239 7 4 4 -0.5 NC(CCP(=O)(O)CCC(=O)O)C(=O)O 10.1021/jm901523t
4041087 15086 2 None -7 4 Rat 4.3 pEC50 = 4.3 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 239 7 4 4 -0.5 NC(CCP(=O)(O)CCC(=O)O)C(=O)O 10.1021/jm901523t
CHEMBL1092727 15086 2 None -7 4 Rat 4.3 pEC50 = 4.3 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 239 7 4 4 -0.5 NC(CCP(=O)(O)CCC(=O)O)C(=O)O 10.1021/jm901523t
44591747 191695 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL485331 191695 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1 10.1016/j.bmcl.2009.03.032
71137034 130177 0 None 7 2 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616850 130177 0 None 7 2 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
156012835 184213 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4638687 184213 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156012835 184213 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4638687 184213 0 None -2 2 Human 6.3 pEC50 = 6.3 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
71137010 130176 0 None 5 2 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616849 130176 0 None 5 2 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
162646719 186388 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 357 5 0 3 4.7 Fc1cc(Cl)ccc1CCCCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
CHEMBL4742364 186388 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 357 5 0 3 4.7 Fc1cc(Cl)ccc1CCCCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
162662970 188711 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 343 5 0 4 3.6 Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1F 10.1016/j.ejmech.2019.111881
CHEMBL4779768 188711 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 343 5 0 4 3.6 Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1F 10.1016/j.ejmech.2019.111881
CHEMBL5090065 222019 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)nc1 10.1021/acs.jmedchem.1c00563
156015654 184300 0 None -1 2 Human 6.3 pEC50 = 6.3 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4639821 184300 0 None -1 2 Human 6.3 pEC50 = 6.3 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
118714744 121330 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 347 4 0 4 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CC2CCC2)c1=O 10.1021/jm500496m
CHEMBL3337456 121330 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 347 4 0 4 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CC2CCC2)c1=O 10.1021/jm500496m
66788653 89411 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 394 3 0 4 4.9 FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179313 89411 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 394 3 0 4 4.9 FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
156015654 184300 0 None -1 2 Human 6.3 pEC50 = 6.3 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4639821 184300 0 None -1 2 Human 6.3 pEC50 = 6.3 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
70681519 81370 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3ccncc3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029800 81370 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3ccncc3)cc2)c(C#N)c1=O 10.1021/jm2016864
162669063 189515 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 357 5 0 4 4.7 Clc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4789937 189515 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 357 5 0 4 4.7 Clc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
44392629 71542 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 456 10 1 4 5.9 CC(C)CC(=O)c1ccc(OCCCCOc2cccc(F)c2F)c(Br)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL181921 71542 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 456 10 1 4 5.9 CC(C)CC(=O)c1ccc(OCCCCOc2cccc(F)c2F)c(Br)c1O 10.1016/j.bmcl.2004.09.028
11271167 73574 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 461 11 1 6 6.1 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL185994 73574 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 461 11 1 6 6.1 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
11950927 130207 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 475 11 1 6 6.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cc(C)n2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL361724 130207 0 None - 1 Human 6.3 pEC50 = 6.3 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 475 11 1 6 6.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cc(C)n2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
57459477 89430 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 385 3 0 5 4.1 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12 10.1021/jm3010724
CHEMBL2179333 89430 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 385 3 0 5 4.1 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12 10.1021/jm3010724
71117141 154227 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 435 4 0 8 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21 nan
CHEMBL3930164 154227 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 435 4 0 8 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21 nan
57459477 89430 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 385 3 0 5 4.1 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12 10.1021/jm300912k
CHEMBL2179333 89430 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 385 3 0 5 4.1 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12 10.1021/jm300912k
49801368 166437 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4103808 166437 0 None - 1 Human 7.3 pEC50 = 7.3 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
59599616 153042 1 None -1 2 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)nc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3920609 153042 1 None -1 2 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)nc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
25125217 7343 25 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
7678 7343 25 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
CHEMBL3937907 7343 25 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
DB16073 7343 25 None - 1 Human 6.3 pEC50 = 6.3 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
44428730 151484 1 None - 1 Rat 4.3 pEC50 = 4.3 Functional
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 185 3 3 5 -0.2 CCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
CHEMBL390863 151484 1 None - 1 Rat 4.3 pEC50 = 4.3 Functional
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 185 3 3 5 -0.2 CCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
137652320 164053 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4076786 164053 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
24779944 14640 0 None -36 3 Rat 4.2 pEC50 = 4.2 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 225 6 4 4 -0.9 N[C@@H](CCP(=O)(O)CC(=O)O)C(=O)O 10.1021/jm901523t
CHEMBL1089852 14640 0 None -36 3 Rat 4.2 pEC50 = 4.2 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 225 6 4 4 -0.9 N[C@@H](CCP(=O)(O)CC(=O)O)C(=O)O 10.1021/jm901523t
44428730 151484 1 None - 1 Rat 4.2 pEC50 = 4.2 Functional
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 185 3 3 5 -0.2 CCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
CHEMBL390863 151484 1 None - 1 Rat 4.2 pEC50 = 4.2 Functional
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 185 3 3 5 -0.2 CCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
11546303 72008 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 10 1 5 5.0 CC(C)CC(=O)c1ccc(OCCCCOc2cccnc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182668 72008 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 10 1 5 5.0 CC(C)CC(=O)c1ccc(OCCCCOc2cccnc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
44392671 72043 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 7 1 5 6.4 Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182822 72043 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 7 1 5 6.4 Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2004.09.028
46887369 15647 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 311 5 0 3 4.2 CC(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL1097380 15647 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 311 5 0 3 4.2 CC(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL5081320 221521 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(-c4ccc(F)cc4)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
44155863 15318 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 262 6 1 3 3.6 CCCCCCC1CN(c2ccc(N)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094460 15318 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 262 6 1 3 3.6 CCCCCCC1CN(c2ccc(N)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
25173209 195802 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 289 5 0 3 3.6 O=C1OCCN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL509096 195802 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 289 5 0 3 3.6 O=C1OCCN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
44155315 15427 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095385 15427 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44155642 15620 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 281 6 0 2 4.6 CCCCCCC1CN(c2cccc(Cl)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1097052 15620 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 281 6 0 2 4.6 CCCCCCC1CN(c2cccc(Cl)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
46887367 15645 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 297 5 0 3 3.7 CCc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
CHEMBL1097378 15645 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 297 5 0 3 3.7 CCc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
71117030 152631 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 423 5 1 7 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(C(=O)NCc4ncco4)CC3)nc21 nan
CHEMBL3917329 152631 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 423 5 1 7 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(C(=O)NCc4ncco4)CC3)nc21 nan
44591795 199219 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 320 3 0 3 3.9 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL520837 199219 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 320 3 0 3 3.9 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
11952168 74117 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 461 14 1 6 6.2 CCCCCn1ccc2c(CCC)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
CHEMBL188538 74117 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 461 14 1 6 6.2 CCCCCn1ccc2c(CCC)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
57459494 90679 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206442 90679 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
155566352 182713 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 416 3 0 4 5.1 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4587631 182713 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 416 3 0 4 5.1 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
11626955 158590 0 None 18 2 Human 8.2 pEC50 = 8.2 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 471 7 2 8 4.6 CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(C(F)(F)F)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3965244 158590 0 None 18 2 Human 8.2 pEC50 = 8.2 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 471 7 2 8 4.6 CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(C(F)(F)F)c1O 10.1016/j.bmcl.2016.11.049
117971699 149063 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 397 6 0 4 4.9 FC(F)(F)c1c(OCC(F)(F)c2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885115 149063 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 397 6 0 4 4.9 FC(F)(F)c1c(OCC(F)(F)c2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
71131322 130184 0 None 43 2 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616857 130184 0 None 43 2 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
60096228 163566 0 None -2 2 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4070866 163566 0 None -2 2 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
71137011 130185 0 None 58 2 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616858 130185 0 None 58 2 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
134130002 148945 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2ccc(-c3ccccc3)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3883801 148945 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2ccc(-c3ccccc3)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
69093928 90684 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206447 90684 0 None - 1 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
60096250 165700 0 None -1 2 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4095567 165700 0 None -1 2 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
117972041 148987 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1ccc(COc2ccn3c(CC4CC4)nnc3c2Cl)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3884170 148987 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1ccc(COc2ccn3c(CC4CC4)nnc3c2Cl)cc1 10.1016/j.bmc.2016.11.018
155559961 181674 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 285 2 0 3 3.3 Clc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4564190 181674 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 285 2 0 3 3.3 Clc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
155567522 182750 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 253 3 0 3 3.0 CCCCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4588508 182750 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 253 3 0 3 3.0 CCCCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL5086642 221820 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CCC1 10.1021/acs.jmedchem.1c00563
CHEMBL5088821 221958 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)cc1F 10.1021/acs.jmedchem.1c00563
CHEMBL5093895 222231 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CC2CCC1C2 10.1021/acs.jmedchem.1c00563
155522079 177480 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 304 3 0 4 3.7 Fc1ccccc1-c1ccc(Cn2nnc3ccccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4451873 177480 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 304 3 0 4 3.7 Fc1ccccc1-c1ccc(Cn2nnc3ccccc32)cn1 10.1021/acs.jmedchem.8b00161
57459487 90674 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 402 4 0 4 5.0 Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c(F)c1 10.1021/jm300912k
CHEMBL2206437 90674 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 402 4 0 4 5.0 Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c(F)c1 10.1021/jm300912k
1310 9095 110 None -457 17 Rat 6.2 pEC50 = 6.2 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
1369 9095 110 None -457 17 Rat 6.2 pEC50 = 6.2 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
33032 9095 110 None -457 17 Rat 6.2 pEC50 = 6.2 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
44272391 9095 110 None -457 17 Rat 6.2 pEC50 = 6.2 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
88747398 9095 110 None -457 17 Rat 6.2 pEC50 = 6.2 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
CHEMBL575060 9095 110 None -457 17 Rat 6.2 pEC50 = 6.2 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
DB00142 9095 110 None -457 17 Rat 6.2 pEC50 = 6.2 Functional
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
10376615 87344 0 None - 1 Rat 6.2 pEC50 = 6.2 Functional
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 232 4 4 5 -2.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL214917 87344 0 None - 1 Rat 6.2 pEC50 = 6.2 Functional
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 232 4 4 5 -2.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL544505 87344 0 None - 1 Rat 6.2 pEC50 = 6.2 Functional
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 232 4 4 5 -2.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL5074682 221105 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(-c4cccc(F)c4)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
10473248 20958 0 None 4 3 Rat 5.2 pEC50 = 5.2 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1198741 20958 0 None 4 3 Rat 5.2 pEC50 = 5.2 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL540015 20958 0 None 4 3 Rat 5.2 pEC50 = 5.2 Functional
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1 10.1016/s0960-894x(01)00329-8
42610165 87574 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 435 4 0 5 5.2 N#Cc1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152107 87574 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 435 4 0 5 5.2 N#Cc1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL5079928 221433 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3ccccc3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
155559438 181638 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 198 2 0 4 1.7 N#Cc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4563304 181638 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 198 2 0 4 1.7 N#Cc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
66785027 165117 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4089416 165117 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL5076356 221210 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(-c4ccccc4)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
53316862 64499 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 298 3 0 3 4.1 CCCn1ccc2cc(-c3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669381 64499 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 298 3 0 3 4.1 CCCn1ccc2cc(-c3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53323492 64505 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 356 7 0 4 4.5 CCCn1ccc2cc(OCCCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669387 64505 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 356 7 0 4 4.5 CCCn1ccc2cc(OCCCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53325450 64512 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 418 7 0 4 5.7 CCCn1ccc2cc(-c3ccc(OCCc4ccccc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669393 64512 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 418 7 0 4 5.7 CCCn1ccc2cc(-c3ccc(OCCc4ccccc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46225584 206454 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 408 3 0 4 5.0 Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593056 206454 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 408 3 0 4 5.0 Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46226929 209392 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 366 5 0 7 2.3 CCCCn1ccc(N2CCN(c3nc(C)cc(C)n3)CC2)c(C#N)c1=O 10.1016/j.bmcl.2009.11.008
CHEMBL612133 209392 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 366 5 0 7 2.3 CCCCn1ccc(N2CCN(c3nc(C)cc(C)n3)CC2)c(C#N)c1=O 10.1016/j.bmcl.2009.11.008
68109379 164004 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4076286 164004 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
24815434 206475 0 None -5 2 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593196 206475 0 None -5 2 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225337 206756 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 375 3 0 5 3.3 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595151 206756 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 375 3 0 5 3.3 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225335 206826 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595608 206826 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
24849789 206913 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 324 3 0 4 3.0 Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL596270 206913 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 324 3 0 4 3.0 Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225569 208141 0 None -12 2 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL604467 208141 0 None -12 2 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
44591813 191438 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 324 5 0 3 3.8 C[C@@H]1CN(Cc2ccc(-c3ccccc3CN(C)C)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484972 191438 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 324 5 0 3 3.8 C[C@@H]1CN(Cc2ccc(-c3ccccc3CN(C)C)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
11950742 73881 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 462 11 1 7 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ncn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL187398 73881 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 462 11 1 7 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ncn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
70685769 81390 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 405 5 0 5 5.3 Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2Cl)c(C)n1 10.1021/jm2016864
CHEMBL2029820 81390 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 405 5 0 5 5.3 Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2Cl)c(C)n1 10.1021/jm2016864
155552204 180921 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1ccccc1Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4546388 180921 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1ccccc1Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
71136691 150399 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 394 3 0 5 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21 nan
CHEMBL3899706 150399 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 394 3 0 5 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21 nan
68109605 165169 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4089955 165169 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
9815616 121578 6 None -2 4 Rat 7.2 pEC50 = 7.2 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
CHEMBL334014 121578 6 None -2 4 Rat 7.2 pEC50 = 7.2 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
44155538 15280 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2cccc(F)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094134 15280 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2cccc(F)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44155316 15470 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 277 7 0 3 4.0 CCCCCCC1CN(c2cccc(OC)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095749 15470 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 277 7 0 3 4.0 CCCCCCC1CN(c2cccc(OC)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44155420 15531 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 261 6 0 2 4.3 CCCCCCC1CN(c2cccc(C)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1096423 15531 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 261 6 0 2 4.3 CCCCCCC1CN(c2cccc(C)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
46227790 206870 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 375 4 0 7 2.9 CCCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
CHEMBL595966 206870 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 375 4 0 7 2.9 CCCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
70689924 81366 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3ccccn3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029798 81366 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3ccccn3)cc2)c(C#N)c1=O 10.1021/jm2016864
162665242 188887 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 391 5 0 4 5.3 Clc1cccc(SCCCN2CCn3c(nc4ccccc43)C2)c1Cl 10.1016/j.ejmech.2019.111881
CHEMBL4781971 188887 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 391 5 0 4 5.3 Clc1cccc(SCCCN2CCn3c(nc4ccccc43)C2)c1Cl 10.1016/j.ejmech.2019.111881
11951987 75007 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 12 1 6 5.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CCC 10.1016/j.bmcl.2005.06.017
CHEMBL191579 75007 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 12 1 6 5.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CCC 10.1016/j.bmcl.2005.06.017
46887320 15766 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 283 4 0 3 3.4 Cc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
CHEMBL1098389 15766 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 283 4 0 3 3.4 Cc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
118714739 121340 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 350 5 0 5 3.1 CC(C)CCn1ccc(N2CCN(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337505 121340 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 350 5 0 5 3.1 CC(C)CCn1ccc(N2CCN(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
46197778 14990 0 None -6 5 Rat 5.2 pEC50 = 5.2 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 237 6 4 4 -0.3 N[C@@H](CCP(=O)(O)/C=C/C(=O)O)C(=O)O 10.1021/jm901523t
CHEMBL1092243 14990 0 None -6 5 Rat 5.2 pEC50 = 5.2 Functional
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 237 6 4 4 -0.3 N[C@@H](CCP(=O)(O)/C=C/C(=O)O)C(=O)O 10.1021/jm901523t
11626305 73428 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 437 10 1 5 5.7 CC(C)CC(=O)c1ccc(OCCCCSc2ccncc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL185290 73428 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 437 10 1 5 5.7 CC(C)CC(=O)c1ccc(OCCCCSc2ccncc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
44428731 149925 0 None - 1 Rat 4.2 pEC50 = 4.2 Functional
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 199 4 3 5 0.2 CCCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
CHEMBL389585 149925 0 None - 1 Rat 4.2 pEC50 = 4.2 Functional
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 199 4 3 5 0.2 CCCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
11575058 72375 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2ccccc2Sc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL183304 72375 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2ccccc2Sc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
118714755 121355 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3ccc(F)cc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337521 121355 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3ccc(F)cc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
155550797 181899 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1ccc2c(c1)nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1 10.1021/acs.jmedchem.8b00161
CHEMBL4569581 181899 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1ccc2c(c1)nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1 10.1021/acs.jmedchem.8b00161
59599538 151823 0 None -1 2 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3911282 151823 0 None -1 2 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
71136653 130181 0 None 51 2 Human 7.2 pEC50 = 7.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616854 130181 0 None 51 2 Human 7.2 pEC50 = 7.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
57459475 89426 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 331 3 0 5 3.5 CCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179329 89426 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 331 3 0 5 3.5 CCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
1393 8321 64 None 2 6 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
1396 8321 64 None 2 6 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
213056 8321 64 None 2 6 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
CHEMBL8759 8321 64 None 2 6 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
1393 8321 64 None 2 6 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
1396 8321 64 None 2 6 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
213056 8321 64 None 2 6 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
CHEMBL8759 8321 64 None 2 6 Human 8.2 pEC50 = 8.2 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
156817932 198853 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 465 4 0 5 4.1 O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1 10.1021/acs.jmedchem.2c00593
CHEMBL5202739 198853 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 465 4 0 5 4.1 O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1 10.1021/acs.jmedchem.2c00593
60096224 163324 0 None -43 2 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4068189 163324 0 None -43 2 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
71461395 90682 1 None - 1 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206445 90682 1 None - 1 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
23725156 68733 0 None - 1 Rat 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 357 3 0 3 4.7 Cn1c(CN2CCC(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL1774107 68733 0 None - 1 Rat 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 357 3 0 3 4.7 Cn1c(CN2CCC(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1021/jm101414h
49801370 163814 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4073628 163814 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
90098428 130183 0 None 60 2 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616856 130183 0 None 60 2 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
25173616 191273 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC1CN(Cc2ccc(OC(C)C3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484731 191273 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC1CN(Cc2ccc(OC(C)C3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
156010124 183810 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4632373 183810 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
156010124 183810 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4632373 183810 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
44591773 191039 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 3 0 2 4.0 C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL483751 191039 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 3 0 2 4.0 C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
162662443 188790 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 369 6 0 4 4.0 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(Cl)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4780663 188790 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 369 6 0 4 4.0 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(Cl)cc1 10.1016/j.ejmech.2019.111881
162675793 190194 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 375 5 0 4 4.6 Clc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl 10.1016/j.ejmech.2019.111881
CHEMBL4798495 190194 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 375 5 0 4 4.6 Clc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl 10.1016/j.ejmech.2019.111881
155546950 180438 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 320 3 0 4 4.2 Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cn2)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4534604 180438 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 320 3 0 4 4.2 Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cn2)cc1 10.1021/acs.jmedchem.8b00161
155565811 182399 1 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 269 2 0 3 2.7 Fc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4580525 182399 1 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 269 2 0 3 2.7 Fc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
146036861 182828 6 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 251 2 0 3 2.6 Brc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4590535 182828 6 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 251 2 0 3 2.6 Brc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
155549028 180576 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 321 3 0 3 4.4 Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(F)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4538026 180576 0 None - 1 Human 7.2 pEC50 = 7.2 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 321 3 0 3 4.4 Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(F)c1 10.1021/acs.jmedchem.8b00161
71460259 87575 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 434 4 1 5 5.2 N#Cc1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152108 87575 0 None - 1 Human 6.2 pEC50 = 6.2 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 434 4 1 5 5.2 N#Cc1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
44155535 15279 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2ccccc2F)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094133 15279 0 None - 1 Human 5.2 pEC50 = 5.2 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2ccccc2F)C(=O)O1 10.1016/j.bmcl.2010.03.089
134130007 148969 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 391 6 0 6 4.4 Clc1c(OCc2cccc(-c3cncnc3)c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884042 148969 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 391 6 0 6 4.4 Clc1c(OCc2cccc(-c3cncnc3)c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
44428731 149925 0 None - 1 Rat 4.1 pEC50 = 4.1 Functional
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 199 4 3 5 0.2 CCCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
CHEMBL389585 149925 0 None - 1 Rat 4.1 pEC50 = 4.1 Functional
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 199 4 3 5 0.2 CCCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
68107827 199263 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
CHEMBL5208947 199263 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
155535327 178794 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 281 3 0 4 2.6 COc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4471540 178794 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 281 3 0 4 2.6 COc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
71136654 130186 0 None 3 2 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616859 130186 0 None 3 2 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
57459636 89407 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 357 4 0 5 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179309 89407 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 357 4 0 5 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
66786816 165135 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4089612 165135 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
162675603 190075 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 389 6 0 4 4.8 FC(F)(F)Oc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4796990 190075 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 389 6 0 4 4.8 FC(F)(F)Oc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
54580322 68748 0 None - 1 Rat 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 402 3 0 4 5.0 Cn1c(CN2CC[C@@H](c3ccc(C(F)(F)F)cc3)C(C)(C)C2)nc2ncccc21 10.1021/jm101414h
CHEMBL1774226 68748 0 None - 1 Rat 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 402 3 0 4 5.0 Cn1c(CN2CC[C@@H](c3ccc(C(F)(F)F)cc3)C(C)(C)C2)nc2ncccc21 10.1021/jm101414h
25173691 195787 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2CCCOC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
CHEMBL508821 195787 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2CCCOC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
162643509 188448 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1ccccc1CCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
CHEMBL4776355 188448 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1ccccc1CCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
11951986 131097 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 445 12 1 6 5.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CC1 10.1016/j.bmcl.2005.06.017
CHEMBL363531 131097 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 445 12 1 6 5.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CC1 10.1016/j.bmcl.2005.06.017
44591792 200149 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 268 3 0 3 3.1 C[C@@H]1CN(Cc2ccc(-c3cccnc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL525075 200149 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 268 3 0 3 3.1 C[C@@H]1CN(Cc2ccc(-c3cccnc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
168298153 199518 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 421 6 0 4 5.8 FC(F)(F)c1c(-c2ccc(OCC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.2c00969
CHEMBL5220484 199518 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 421 6 0 4 5.8 FC(F)(F)c1c(-c2ccc(OCC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.2c00969
25173778 191692 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3ccc(Cl)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL485329 191692 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3ccc(Cl)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
51357936 68751 0 None -3 2 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C 10.1021/jm101414h
CHEMBL1774231 68751 0 None -3 2 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C 10.1021/jm101414h
44155747 15469 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2ccc(C#N)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095746 15469 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2ccc(C#N)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
11951991 140700 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 447 12 1 6 5.7 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL371578 140700 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 447 12 1 6 5.7 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)C 10.1016/j.bmcl.2005.06.017
66786131 163945 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075417 163945 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
11510036 73002 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 9 1 5 6.2 Cc1c(OCc2ccc(CSc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL184531 73002 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 9 1 5 6.2 Cc1c(OCc2ccc(CSc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
11952169 74304 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 459 10 1 6 5.8 CCCc1c(OC/C=C/COc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL189623 74304 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 459 10 1 6 5.8 CCCc1c(OC/C=C/COc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
24815976 206538 0 None 5 2 Rat 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL593745 206538 0 None 5 2 Rat 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1021/jm101414h
46887418 15771 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 337 4 0 3 4.1 O=C1OC(COc2ccc(C(F)(F)F)cc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1098406 15771 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 337 4 0 3 4.1 O=C1OC(COc2ccc(C(F)(F)F)cc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
22368592 15524 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 263 6 1 3 3.7 CCCCCCC1CN(c2ccc(O)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1096318 15524 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 263 6 1 3 3.7 CCCCCCC1CN(c2ccc(O)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
51354014 68752 0 None - 1 Rat 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@H]1CCN(Cc2nc3ncccc3n2C)C[C@H]1C 10.1021/jm101414h
CHEMBL1774232 68752 0 None - 1 Rat 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@H]1CCN(Cc2nc3ncccc3n2C)C[C@H]1C 10.1021/jm101414h
11952347 74208 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 7 5.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c(CC(C)(C)C)noc12 10.1016/j.bmcl.2005.06.017
CHEMBL188977 74208 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 7 5.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c(CC(C)(C)C)noc12 10.1016/j.bmcl.2005.06.017
155518831 177138 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 353 3 0 3 5.5 Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4447550 177138 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 353 3 0 3 5.5 Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
CHEMBL5093066 222184 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None Cn1c(CN2CCN(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ncccc21 10.1021/acs.jmedchem.1c00563
156019582 184790 0 None 2 2 Human 7.1 pEC50 = 7.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4646555 184790 0 None 2 2 Human 7.1 pEC50 = 7.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
59234231 8924 4 None -1 2 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6330 8924 4 None -1 2 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6331 8924 4 None -1 2 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
CHEMBL3337510 8924 4 None -1 2 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
156019582 184790 0 None 2 2 Human 7.1 pEC50 = 7.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4646555 184790 0 None 2 2 Human 7.1 pEC50 = 7.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
67060124 173556 0 None - 1 Rat 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 388 4 0 5 3.8 O=c1ccn2c(n1)O[C@H](COc1ccc(-c3cccc(C(F)(F)F)c3)cc1)C2 10.1016/j.bmcl.2018.08.022
CHEMBL4283963 173556 0 None - 1 Rat 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 388 4 0 5 3.8 O=c1ccn2c(n1)O[C@H](COc1ccc(-c3cccc(C(F)(F)F)c3)cc1)C2 10.1016/j.bmcl.2018.08.022
46887272 15463 3 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 233 5 0 2 3.6 CCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095702 15463 3 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 233 5 0 2 3.6 CCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44155540 15499 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2ccc(F)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095970 15499 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2ccc(F)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
53322148 64504 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 342 6 0 4 4.1 CCCn1ccc2cc(OCCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669386 64504 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 342 6 0 4 4.1 CCCn1ccc2cc(OCCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53326075 64507 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 383 4 0 5 4.0 CCCn1ccc2cc(-c3ccc(N4CCOCC4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669389 64507 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 383 4 0 5 4.0 CCCn1ccc2cc(-c3ccc(N4CCOCC4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53322149 64509 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 328 4 0 4 4.1 CCCn1ccc2cc(-c3ccc(OC)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669390 64509 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 328 4 0 4 4.1 CCCn1ccc2cc(-c3ccc(OC)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53324152 64520 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 264 3 0 3 3.5 CCCn1ccc2cc(-c3cccnc3)ccc2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669402 64520 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 264 3 0 3 3.5 CCCn1ccc2cc(-c3cccnc3)ccc2c1=O 10.1016/j.bmcl.2010.12.048
10176324 121605 1 None 4 4 Rat 8.1 pEC50 = 8.1 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 173 3 3 3 -0.6 C[C@H]1[C@H](C(=O)O)[C@H]1[C@H](N)C(=O)O 10.1021/jm030967o
CHEMBL334160 121605 1 None 4 4 Rat 8.1 pEC50 = 8.1 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 173 3 3 3 -0.6 C[C@H]1[C@H](C(=O)O)[C@H]1[C@H](N)C(=O)O 10.1021/jm030967o
57459488 90678 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206441 90678 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
68107827 199263 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
CHEMBL5208947 199263 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
60096178 163660 0 None -10 2 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4071962 163660 0 None -10 2 Human 8.1 pEC50 = 8.1 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
156018381 184701 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4645305 184701 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
70209638 164388 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4080973 164388 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
156018381 184701 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4645305 184701 0 None - 1 Human 8.1 pEC50 = 8.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
146036869 182516 7 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 287 2 0 3 3.2 Brc1cccc2c1nnn2Cc1ccccc1 10.1021/acs.jmedchem.8b00161
CHEMBL4583006 182516 7 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 287 2 0 3 3.2 Brc1cccc2c1nnn2Cc1ccccc1 10.1021/acs.jmedchem.8b00161
162657401 187885 3 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 355 3 0 3 3.9 Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4760211 187885 3 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 355 3 0 3 3.9 Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
162657401 187885 3 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 355 3 0 3 3.9 Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1021/acs.jmedchem.1c00563
CHEMBL4760211 187885 3 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 355 3 0 3 3.9 Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1021/acs.jmedchem.1c00563
118714747 121347 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3ccccc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337513 121347 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3ccccc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
51354020 68756 0 None -23 2 Rat 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774236 68756 0 None -23 2 Rat 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
11495483 73441 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 9 1 5 6.2 Cc1c(OCc2cccc(CSc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL185392 73441 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 9 1 5 6.2 Cc1c(OCc2cccc(CSc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
49822116 153770 13 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL3926416 153770 13 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
46830123 7859 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
6321 7859 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
CHEMBL1094763 7859 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
44450470 102861 1 None -1 2 Rat 4.1 pEC50 = 4.1 Functional
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 N[C@H](C(=O)O)[C@H]1CC(O)=NO1 10.1021/jm701394a
CHEMBL260122 102861 1 None -1 2 Rat 4.1 pEC50 = 4.1 Functional
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 N[C@H](C(=O)O)[C@H]1CC(O)=NO1 10.1021/jm701394a
70685765 81378 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 357 5 0 5 4.3 Cc1cc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
CHEMBL2029808 81378 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 357 5 0 5 4.3 Cc1cc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
156817932 198853 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 465 4 0 5 4.1 O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1 10.1021/acs.jmedchem.2c00593
CHEMBL5202739 198853 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 465 4 0 5 4.1 O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1 10.1021/acs.jmedchem.2c00593
25173697 179465 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL450076 179465 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
46887417 15716 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2cccc(Cl)c2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1097984 15716 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2cccc(Cl)c2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
44450470 102861 1 None -1 2 Rat 4.1 pEC50 = 4.1 Functional
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 N[C@H](C(=O)O)[C@H]1CC(O)=NO1 10.1021/jm701394a
CHEMBL260122 102861 1 None -1 2 Rat 4.1 pEC50 = 4.1 Functional
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 N[C@H](C(=O)O)[C@H]1CC(O)=NO1 10.1021/jm701394a
58081135 87587 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 383 2 1 2 5.9 FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4[nH]ccc4c3)ccn12 10.1021/jm201561r
CHEMBL2152121 87587 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 383 2 1 2 5.9 FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4[nH]ccc4c3)ccn12 10.1021/jm201561r
1310 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
1369 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
33032 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
44272391 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
88747398 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
CHEMBL575060 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
DB00142 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
46226952 206630 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 387 3 0 7 2.4 N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL594386 206630 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 387 3 0 7 2.4 N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
66612837 81355 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 266 4 0 3 3.4 CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029786 81355 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 266 4 0 3 3.4 CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O 10.1021/jm2016864
66612837 81355 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 266 4 0 3 3.4 CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL2029786 81355 0 None - 1 Human 5.1 pEC50 = 5.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 266 4 0 3 3.4 CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O 10.1021/jm500496m
155553087 180883 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1ccc2nnn(Cc3ccc(-c4ccc(Cl)cc4F)nc3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4545027 180883 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1ccc2nnn(Cc3ccc(-c4ccc(Cl)cc4F)nc3)c2c1 10.1021/acs.jmedchem.8b00161
51356569 68728 2 None 10 3 Rat 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 335 4 0 4 4.0 COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1 10.1021/jm101414h
CHEMBL1774101 68728 2 None 10 3 Rat 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 335 4 0 4 4.0 COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1 10.1021/jm101414h
168299005 199533 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1cnc2c(-c3ccc(OCC4CC4)c(Cl)c3)cnn2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5221091 199533 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1cnc2c(-c3ccc(OCC4CC4)c(Cl)c3)cnn2c1=O 10.1021/acs.jmedchem.2c00969
66785182 163957 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4075593 163957 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
59599545 153937 0 None 3 2 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 437 7 2 8 4.2 CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(Cl)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3927834 153937 0 None 3 2 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 437 7 2 8 4.2 CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(Cl)c1O 10.1016/j.bmcl.2016.11.049
71136655 130179 0 None 12 2 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616852 130179 0 None 12 2 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
51356569 68728 2 None -10 3 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 335 4 0 4 4.0 COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1 10.1016/j.ejmech.2019.111881
CHEMBL1774101 68728 2 None -10 3 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 335 4 0 4 4.0 COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1 10.1016/j.ejmech.2019.111881
118714736 121336 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 321 4 0 4 3.3 CC(C)CCn1ccc(N2CCc3ccccc3C2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337501 121336 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 321 4 0 4 3.3 CC(C)CCn1ccc(N2CCc3ccccc3C2)c(C#N)c1=O 10.1021/jm500496m
11951447 74258 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 495 9 1 6 7.2 CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cc3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL189290 74258 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 495 9 1 6 7.2 CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cc3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
44591712 191091 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 318 5 0 4 3.8 CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cn1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
CHEMBL484178 191091 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 318 5 0 4 3.8 CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cn1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
118714749 121349 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3ccc(F)cc3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337515 121349 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3ccc(F)cc3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
44392645 72018 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2cccc(Sc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182715 72018 0 None - 1 Human 6.1 pEC50 = 6.1 Functional
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2cccc(Sc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
54584258 68726 0 None - 1 Rat 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 456 5 0 6 3.3 COc1ccccc1N1CCN(Cc2c(Br)c(=O)n(-c3ccccc3)n2C)CC1 10.1021/jm101414h
CHEMBL1774099 68726 0 None - 1 Rat 6.1 pEC50 = 6.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 456 5 0 6 3.3 COc1ccccc1N1CCN(Cc2c(Br)c(=O)n(-c3ccccc3)n2C)CC1 10.1021/jm101414h
137634033 163420 0 None -1 2 Human 6.1 pEC50 = 6.1 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4069251 163420 0 None -1 2 Human 6.1 pEC50 = 6.1 Functional
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
51357937 68753 0 None -2 2 Rat 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774233 68753 0 None -2 2 Rat 8.1 pEC50 = 8.1 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
156018305 184613 0 None 89 2 Human 8.1 pEC50 = 8.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4643961 184613 0 None 89 2 Human 8.1 pEC50 = 8.1 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
156018305 184613 0 None 89 2 Human 8.0 pEC50 = 8.0 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4643961 184613 0 None 89 2 Human 8.0 pEC50 = 8.0 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
69093344 90683 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206446 90683 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
66786493 166458 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4104081 166458 0 None - 1 Human 8.0 pEC50 = 8.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
156020355 184807 0 None 104 2 Human 8.0 pEC50 = 8 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4646835 184807 0 None 104 2 Human 8.0 pEC50 = 8 Functional
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
6604805 209467 2 None - 1 Rat 7.1 pEC50 = 7.1 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 195 3 3 3 -0.6 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)C1(F)F 10.1021/jm030967o
CHEMBL61605 209467 2 None - 1 Rat 7.1 pEC50 = 7.1 Functional
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 195 3 3 3 -0.6 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)C1(F)F 10.1021/jm030967o
162659759 188090 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.3 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1F 10.1016/j.ejmech.2019.111881
CHEMBL4762556 188090 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.3 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1F 10.1016/j.ejmech.2019.111881
162662067 188188 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 349 6 0 4 3.7 Cc1ccccc1OCCCCN1CCn2c(nc3ccccc32)C1=O 10.1016/j.ejmech.2019.111881
CHEMBL4763686 188188 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 349 6 0 4 3.7 Cc1ccccc1OCCCCN1CCn2c(nc3ccccc32)C1=O 10.1016/j.ejmech.2019.111881
162662384 188831 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 389 5 0 4 4.3 O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(Cl)c(Cl)c1 10.1016/j.ejmech.2019.111881
CHEMBL4781222 188831 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 389 5 0 4 4.3 O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(Cl)c(Cl)c1 10.1016/j.ejmech.2019.111881
155518472 177084 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 207 2 0 3 2.5 Clc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4446625 177084 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 207 2 0 3 2.5 Clc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
156017237 184540 0 None 1 2 Human 6.1 pEC50 = 6.1 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4642761 184540 0 None 1 2 Human 6.1 pEC50 = 6.1 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156017237 184540 0 None 1 2 Human 6.0 pEC50 = 6.0 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4642761 184540 0 None 1 2 Human 6.0 pEC50 = 6.0 Functional
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156817945 197263 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL5179002 197263 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
3954 7451 60 None 6 2 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
9868580 7451 60 None 6 2 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
CHEMBL593013 7451 60 None 6 2 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
66784262 165010 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4088239 165010 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
70694132 81386 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2Cl)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029816 81386 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2Cl)c(C#N)c1=O 10.1021/jm2016864
11655609 172680 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree CEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree C
ChEMBL 463 11 1 8 4.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL424998 172680 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree CEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree C
ChEMBL 463 11 1 8 4.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
1395 9306 15 None -7 4 Rat 7.0 pEC50 = 7.0 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
9837317 9306 15 None -7 4 Rat 7.0 pEC50 = 7.0 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
CHEMBL121053 9306 15 None -7 4 Rat 7.0 pEC50 = 7.0 Functional
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
57459512 89416 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 367 4 0 5 3.7 Clc1c(N2CCN(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179318 89416 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 367 4 0 5 3.7 Clc1c(N2CCN(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
118714742 121343 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 335 5 0 4 3.9 CCCCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337508 121343 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 335 5 0 4 3.9 CCCCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
71117214 157886 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 446 4 0 8 2.1 Cn1cnc(S(=O)(=O)N2CCCC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)C2)c1 nan
CHEMBL3959189 157886 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 446 4 0 8 2.1 Cn1cnc(S(=O)(=O)N2CCCC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)C2)c1 nan
44591770 199097 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 311 5 0 3 4.1 CCOc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL520639 199097 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 311 5 0 3 4.1 CCOc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1 10.1016/j.bmcl.2009.03.032
68109333 166171 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4100691 166171 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
162649465 186844 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 391 5 0 3 5.0 Fc1cc(C(F)(F)F)ccc1CCCCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
CHEMBL4747874 186844 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 391 5 0 3 5.0 Fc1cc(C(F)(F)F)ccc1CCCCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
46226930 208696 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 345 4 0 5 3.5 CCCc1cnc2c(C#N)c(N3CCN(c4ccccc4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
CHEMBL607518 208696 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 345 4 0 5 3.5 CCCc1cnc2c(C#N)c(N3CCN(c4ccccc4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
118714754 121354 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 363 5 0 5 3.5 COc1ccc(C2CCN(c3ccn(CC4CC4)c(=O)c3C#N)CC2)cc1 10.1021/jm500496m
CHEMBL3337520 121354 0 None - 1 Human 7.0 pEC50 = 7.0 Functional
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 363 5 0 5 3.5 COc1ccc(C2CCN(c3ccn(CC4CC4)c(=O)c3C#N)CC2)cc1 10.1021/jm500496m
11950553 74069 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 462 11 1 7 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL188286 74069 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 462 11 1 7 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
71117402 157210 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 532 5 1 6 5.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4ccc(OC(F)(F)F)cc4)C3)nc21 nan
CHEMBL3953950 157210 0 None - 1 Human 6.0 pEC50 = 6.0 Functional
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 532 5 1 6 5.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4ccc(OC(F)(F)F)cc4)C3)nc21 nan
51354017 68754 0 None - 1 Rat 6.0 pEC50 = 6 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774234 68754 0 None - 1 Rat 6.0 pEC50 = 6 Functional
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
131636309 166824 0 None - 1 Human 9.0 pIC50 = 9.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 445 4 0 5 5.6 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
CHEMBL4108184 166824 0 None - 1 Human 9.0 pIC50 = 9.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 445 4 0 5 5.6 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
131636462 166948 0 None - 1 Human 8.8 pIC50 = 8.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 5 0 5 4.8 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C nan
CHEMBL4109246 166948 0 None - 1 Human 8.8 pIC50 = 8.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 5 0 5 4.8 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C nan
131636310 167325 0 None - 1 Human 8.8 pIC50 = 8.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 4 0 5 5.3 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
CHEMBL4112479 167325 0 None - 1 Human 8.8 pIC50 = 8.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 4 0 5 5.3 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
131636389 166885 0 None - 1 Human 8.7 pIC50 = 8.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 441 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4108743 166885 0 None - 1 Human 8.7 pIC50 = 8.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 441 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636463 167089 0 None - 1 Human 8.7 pIC50 = 8.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4110543 167089 0 None - 1 Human 8.7 pIC50 = 8.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
78319942 166959 0 None - 1 Human 8.7 pIC50 = 8.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4109319 166959 0 None - 1 Human 8.7 pIC50 = 8.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636453 167349 0 None - 1 Human 8.7 pIC50 = 8.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112624 167349 0 None - 1 Human 8.7 pIC50 = 8.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
11484819 63080 0 None -2 2 Human 8.0 pIC50 = 8 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629863 63080 0 None -2 2 Human 8.0 pIC50 = 8 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
44450479 103038 0 None - 1 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 398 3 1 4 4.9 CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL261050 103038 0 None - 1 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 398 3 1 4 4.9 CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
9909080 162061 0 None - 1 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 402 2 1 4 4.7 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL402886 162061 0 None - 1 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 402 2 1 4 4.7 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
22317744 63061 0 None - 1 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 1 4 5.5 COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629844 63061 0 None - 1 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 1 4 5.5 COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
22317767 63064 0 None - 1 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629847 63064 0 None - 1 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11235624 63079 0 None -1 3 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629862 63079 0 None -1 3 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
22317431 63187 0 None - 1 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631864 63187 0 None - 1 Rat 8.0 pIC50 = 8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
78324632 167032 0 None - 1 Human 8.0 pIC50 = 8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 3 0 5 4.9 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
CHEMBL4110016 167032 0 None - 1 Human 8.0 pIC50 = 8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 3 0 5 4.9 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
78320556 167436 0 None - 1 Human 8.0 pIC50 = 8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 4.8 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl nan
CHEMBL4113304 167436 0 None - 1 Human 8.0 pIC50 = 8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 4.8 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl nan
131636370 166657 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 3 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4106787 166657 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 3 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636447 167522 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113943 167522 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636434 158152 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 5 0 5 4.8 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1CC nan
CHEMBL3961419 158152 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 5 0 5 4.8 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1CC nan
131636342 149671 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)ccn1 nan
CHEMBL3893630 149671 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)ccn1 nan
76318479 112880 0 None - 1 Human 7.0 pIC50 = 7 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 446 6 1 5 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCCF)c(C(F)(F)F)cc2N1 10.1039/C3MD00110E
CHEMBL3133886 112880 0 None - 1 Human 7.0 pIC50 = 7 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 446 6 1 5 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCCF)c(C(F)(F)F)cc2N1 10.1039/C3MD00110E
131636402 167203 0 None - 1 Human 7.0 pIC50 = 7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 4 1 6 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
CHEMBL4111387 167203 0 None - 1 Human 7.0 pIC50 = 7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 4 1 6 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
10778385 85514 0 None -1 2 Human 6.0 pIC50 = 6 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 269 6 3 4 1.2 NC(CCc1ccsc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112581 85514 0 None -1 2 Human 6.0 pIC50 = 6 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 269 6 3 4 1.2 NC(CCc1ccsc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
10826383 85517 0 None -1 2 Human 6.0 pIC50 = 6 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 277 7 3 3 1.5 NC(CCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112584 85517 0 None -1 2 Human 6.0 pIC50 = 6 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 277 7 3 3 1.5 NC(CCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
44348769 23553 0 None -3 2 Human 6.0 pIC50 = 6 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 279 6 4 4 0.8 N[C@@](CCc1cccc(O)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL124483 23553 0 None -3 2 Human 6.0 pIC50 = 6 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 279 6 4 4 0.8 N[C@@](CCc1cccc(O)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
49858118 7894 0 None 10 2 Human 6.0 pIC50 = 6 Functional
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
6224 7894 0 None 10 2 Human 6.0 pIC50 = 6 Functional
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
CHEMBL1630807 7894 0 None 10 2 Human 6.0 pIC50 = 6 Functional
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
11269030 63078 0 None -1 3 Rat 7.0 pIC50 = 7 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629861 63078 0 None -1 3 Rat 7.0 pIC50 = 7 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
155550334 181076 0 None - 1 Rat 7.0 pIC50 = 7.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 449 5 1 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4550009 181076 0 None - 1 Rat 7.0 pIC50 = 7.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 449 5 1 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155550334 181076 0 None - 1 Rat 7.0 pIC50 = 7.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 449 5 1 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4550009 181076 0 None - 1 Rat 7.0 pIC50 = 7.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 449 5 1 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
131636325 167467 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 6 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCC4(C)COC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113523 167467 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 6 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCC4(C)COC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
155559601 181634 0 None - 1 Rat 6.0 pIC50 = 6.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 405 4 1 4 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4563183 181634 0 None - 1 Rat 6.0 pIC50 = 6.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 405 4 1 4 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1 10.1021/acs.jmedchem.8b01266
155566989 182656 0 None - 1 Rat 6.0 pIC50 = 6.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4586203 182656 0 None - 1 Rat 6.0 pIC50 = 6.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1 10.1021/acs.jmedchem.8b01266
155559601 181634 0 None - 1 Rat 6.0 pIC50 = 6.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 405 4 1 4 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4563183 181634 0 None - 1 Rat 6.0 pIC50 = 6.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 405 4 1 4 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1 10.1021/acs.jmedchem.8b01266
155566989 182656 0 None - 1 Rat 6.0 pIC50 = 6.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4586203 182656 0 None - 1 Rat 6.0 pIC50 = 6.0 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1 10.1021/acs.jmedchem.8b01266
131636415 166664 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 463 7 1 7 3.9 COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
CHEMBL4106864 166664 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 463 7 1 7 3.9 COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
9845873 167578 0 None - 1 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL411440 167578 0 None - 1 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
9845873 167578 0 None - 1 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL411440 167578 0 None - 1 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
22224657 102947 0 None 2 2 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260636 102947 0 None 2 2 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
9952648 103083 0 None 1 2 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL261288 103083 0 None 1 2 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
11474913 63181 0 None - 1 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631858 63181 0 None - 1 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
9845873 167578 0 None - 1 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL411440 167578 0 None - 1 Rat 8.0 pIC50 = 8.0 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
90354590 152459 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 443 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(OCc4ccccc4)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3916087 152459 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 443 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(OCc4ccccc4)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
90354676 167178 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
CHEMBL4111258 167178 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
131636304 167390 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 411 4 0 5 5.2 CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3cc(C)nc(C)c3)c2CCO1 nan
CHEMBL4112952 167390 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 411 4 0 5 5.2 CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3cc(C)nc(C)c3)c2CCO1 nan
131636458 167290 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OCCF)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112214 167290 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OCCF)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
10515174 85506 0 None 1 2 Human 6.0 pIC50 = 6.0 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 255 5 3 3 1.5 NC(CC1CCCCC1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112574 85506 0 None 1 2 Human 6.0 pIC50 = 6.0 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 255 5 3 3 1.5 NC(CC1CCCCC1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
44272296 72966 1 None - 1 Rat 5.0 pIC50 = 5.0 Functional
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 245 4 4 3 0.4 C[C@H](Nc1ccc(P(=O)(O)O)cc1)C(=O)O 10.1016/S0960-894X(97)00177-7
CHEMBL18439 72966 1 None - 1 Rat 5.0 pIC50 = 5.0 Functional
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 245 4 4 3 0.4 C[C@H](Nc1ccc(P(=O)(O)O)cc1)C(=O)O 10.1016/S0960-894X(97)00177-7
90643971 118778 0 None -1 2 Rat 6.0 pIC50 = 6.0 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 386 2 0 5 4.6 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(Cl)cc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288667 118778 0 None -1 2 Rat 6.0 pIC50 = 6.0 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 386 2 0 5 4.6 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(Cl)cc3)cc12 10.1016/j.bmcl.2014.04.051
134138062 154278 0 None -1 2 Human 6.0 pIC50 = 6.0 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 374 5 4 5 0.9 N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
CHEMBL3930511 154278 0 None -1 2 Human 6.0 pIC50 = 6.0 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 374 5 4 5 0.9 N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
162658781 190470 0 None 1 2 Human 6.9 pIC50 = 6.9 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4759209 190470 0 None 1 2 Human 6.9 pIC50 = 6.9 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803105 190470 0 None 1 2 Human 6.9 pIC50 = 6.9 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
18548766 102638 0 None - 1 Rat 6.9 pIC50 = 6.9 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 405 2 1 5 4.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259053 102638 0 None - 1 Rat 6.9 pIC50 = 6.9 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 405 2 1 5 4.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
131636289 167508 0 None - 1 Human 6.9 pIC50 = 6.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 3 0 5 4.0 COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1F nan
CHEMBL4113819 167508 0 None - 1 Human 6.9 pIC50 = 6.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 3 0 5 4.0 COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1F nan
22224854 102159 0 None - 1 Rat 7.9 pIC50 = 7.9 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL256812 102159 0 None - 1 Rat 7.9 pIC50 = 7.9 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
131636351 157276 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 0 6 4.4 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)F nan
CHEMBL3954434 157276 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 0 6 4.4 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)F nan
90354488 167715 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 3 0 5 4.5 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C nan
CHEMBL4115442 167715 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 3 0 5 4.5 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C nan
131636294 166802 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4108019 166802 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
67705089 159034 0 None 1 2 Human 7.9 pIC50 = 7.9 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 458 7 4 7 1.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
CHEMBL3969063 159034 0 None 1 2 Human 7.9 pIC50 = 7.9 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 458 7 4 7 1.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
90367533 166862 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.7 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4108547 166862 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.7 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
131636379 167523 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 3 0 5 5.2 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113948 167523 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 3 0 5 5.2 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
137635882 162673 0 None 1 2 Human 4.9 pIC50 = 4.9 Functional
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4060567 162673 0 None 1 2 Human 4.9 pIC50 = 4.9 Functional
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
162644419 190401 0 None 186 2 Human 7.9 pIC50 = 7.9 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4778355 190401 0 None 186 2 Human 7.9 pIC50 = 7.9 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4802356 190401 0 None 186 2 Human 7.9 pIC50 = 7.9 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
22448689 104331 0 None - 1 Rat 7.9 pIC50 = 7.9 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 457 4 1 6 4.6 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL270616 104331 0 None - 1 Rat 7.9 pIC50 = 7.9 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 457 4 1 6 4.6 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
11281280 63182 0 None 1 3 Rat 7.9 pIC50 = 7.9 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631859 63182 0 None 1 3 Rat 7.9 pIC50 = 7.9 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
90354550 166721 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4107291 166721 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636419 154886 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)cc(CF)n1 nan
CHEMBL3935209 154886 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)cc(CF)n1 nan
131636316 166671 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.7 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4106929 166671 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.7 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
78324633 167360 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 4.9 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
CHEMBL4112706 167360 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 4.9 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
131636296 167633 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 3 0 5 5.7 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4114910 167633 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 3 0 5 5.7 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354846 166787 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 4 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
CHEMBL4107888 166787 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 4 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
131636366 167019 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 2 0 4 5.3 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4109916 167019 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 2 0 4 5.3 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636405 166908 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108937 166908 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354352 151503 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3908808 151503 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
76318478 112877 0 None - 1 Human 6.9 pIC50 = 6.9 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 504 3 1 4 5.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(I)c3)cc2N1 10.1039/C3MD00110E
CHEMBL3133883 112877 0 None - 1 Human 6.9 pIC50 = 6.9 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 504 3 1 4 5.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(I)c3)cc2N1 10.1039/C3MD00110E
44328753 214533 0 None -45 6 Rat 5.9 pIC50 = 5.9 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 409 8 3 4 4.2 CCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL95868 214533 0 None -45 6 Rat 5.9 pIC50 = 5.9 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 409 8 3 4 4.2 CCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
76336598 112878 0 None - 1 Human 6.9 pIC50 = 6.9 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 504 3 1 4 5.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(I)cc3)cc2N1 10.1039/C3MD00110E
CHEMBL3133884 112878 0 None - 1 Human 6.9 pIC50 = 6.9 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 504 3 1 4 5.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(I)cc3)cc2N1 10.1039/C3MD00110E
44329033 214759 0 None -34 5 Rat 5.9 pIC50 = 5.9 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 409 7 3 4 4.1 CC(C)C[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL97200 214759 0 None -34 5 Rat 5.9 pIC50 = 5.9 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 409 7 3 4 4.1 CC(C)C[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
90643959 118770 0 None -1 2 Rat 5.9 pIC50 = 5.9 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 460 4 1 7 3.2 COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccc(S(N)(=O)=O)c5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
CHEMBL3288646 118770 0 None -1 2 Rat 5.9 pIC50 = 5.9 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 460 4 1 7 3.2 COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccc(S(N)(=O)=O)c5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
11158623 10124 11 None -7 4 Human 7.9 pIC50 = 7.9 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
6226 10124 11 None -7 4 Human 7.9 pIC50 = 7.9 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
CHEMBL1629855 10124 11 None -7 4 Human 7.9 pIC50 = 7.9 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
10115228 102948 0 None - 1 Rat 7.9 pIC50 = 7.9 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 456 5 1 6 4.8 CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL260642 102948 0 None - 1 Rat 7.9 pIC50 = 7.9 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 456 5 1 6 4.8 CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
53324715 63193 0 None - 1 Rat 7.9 pIC50 = 7.9 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 453 3 2 4 5.8 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631870 63193 0 None - 1 Rat 7.9 pIC50 = 7.9 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 453 3 2 4 5.8 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636423 166813 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 471 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1 nan
CHEMBL4108112 166813 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 471 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1 nan
122580887 167285 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112158 167285 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636280 166645 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4106725 166645 0 None - 1 Human 7.9 pIC50 = 7.9 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)ccn1 nan
131636375 167695 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.6 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4115306 167695 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.6 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
10710505 85513 0 None -1 2 Human 5.9 pIC50 = 5.9 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 316 6 3 4 1.6 Cn1cc(CCC(N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c2ccccc21 10.1021/jm970497w
CHEMBL2112580 85513 0 None -1 2 Human 5.9 pIC50 = 5.9 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 316 6 3 4 1.6 Cn1cc(CCC(N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c2ccccc21 10.1021/jm970497w
155526616 177914 0 None - 1 Rat 5.9 pIC50 = 5.9 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 5 1 5 3.0 CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1 10.1021/acs.jmedchem.8b01266
CHEMBL4458387 177914 0 None - 1 Rat 5.9 pIC50 = 5.9 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 5 1 5 3.0 CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1 10.1021/acs.jmedchem.8b01266
155530126 178247 0 None - 1 Rat 5.9 pIC50 = 5.9 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 401 5 1 6 3.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4463498 178247 0 None - 1 Rat 5.9 pIC50 = 5.9 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 401 5 1 6 3.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
155526616 177914 0 None - 1 Rat 5.9 pIC50 = 5.9 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 5 1 5 3.0 CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1 10.1021/acs.jmedchem.8b01266
CHEMBL4458387 177914 0 None - 1 Rat 5.9 pIC50 = 5.9 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 5 1 5 3.0 CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1 10.1021/acs.jmedchem.8b01266
155530126 178247 0 None - 1 Rat 5.9 pIC50 = 5.9 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 401 5 1 6 3.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4463498 178247 0 None - 1 Rat 5.9 pIC50 = 5.9 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 401 5 1 6 3.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
162654849 190449 0 None -1 2 Human 5.8 pIC50 = 5.8 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4755204 190449 0 None -1 2 Human 5.8 pIC50 = 5.8 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802906 190449 0 None -1 2 Human 5.8 pIC50 = 5.8 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
155550549 181887 0 None - 1 Rat 6.8 pIC50 = 6.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4569114 181887 0 None - 1 Rat 6.8 pIC50 = 6.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
155550549 181887 0 None - 1 Rat 6.8 pIC50 = 6.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4569114 181887 0 None - 1 Rat 6.8 pIC50 = 6.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
134139744 152737 0 None -1 2 Human 6.8 pIC50 = 6.8 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3918170 152737 0 None -1 2 Human 6.8 pIC50 = 6.8 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
11442010 63083 0 None -5 3 Human 7.8 pIC50 = 7.8 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629866 63083 0 None -5 3 Human 7.8 pIC50 = 7.8 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
18548908 103039 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 404 2 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261051 103039 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 404 2 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
9891158 162365 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 476 6 1 6 4.8 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL404463 162365 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 476 6 1 6 4.8 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
22317918 63074 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 3 2 4 5.3 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629858 63074 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 3 2 4 5.3 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1 10.1016/j.bmcl.2010.09.125
131636418 167366 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 4 5.7 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4112763 167366 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 4 5.7 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636410 167607 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 5 0 5 5.8 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F nan
CHEMBL4114609 167607 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 5 0 5 5.8 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F nan
131636388 167138 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 439 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4110884 167138 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 439 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636353 167705 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 2 0 4 5.9 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4115388 167705 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 2 0 4 5.9 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636385 167571 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 6 0 6 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
CHEMBL4114364 167571 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 6 0 6 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
49858117 7875 4 None 5 2 Human 5.8 pIC50 = 5.8 Functional
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
6223 7875 4 None 5 2 Human 5.8 pIC50 = 5.8 Functional
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
CHEMBL1630806 7875 4 None 5 2 Human 5.8 pIC50 = 5.8 Functional
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
155566841 182639 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 382 5 1 6 3.5 Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1 10.1021/acs.jmedchem.8b01266
CHEMBL4585786 182639 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 382 5 1 6 3.5 Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1 10.1021/acs.jmedchem.8b01266
155566841 182639 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 382 5 1 6 3.5 Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1 10.1021/acs.jmedchem.8b01266
CHEMBL4585786 182639 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 382 5 1 6 3.5 Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1 10.1021/acs.jmedchem.8b01266
71681826 96836 0 None -1 3 Human 4.8 pIC50 = 4.8 Functional
Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL2381651 96836 0 None -1 3 Human 4.8 pIC50 = 4.8 Functional
Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
90643958 118769 0 None -6 2 Rat 5.8 pIC50 = 5.8 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 370 2 0 5 4.1 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(F)c3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288644 118769 0 None -6 2 Rat 5.8 pIC50 = 5.8 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 370 2 0 5 4.1 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(F)c3)cc12 10.1016/j.bmcl.2014.04.051
22224970 162271 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL404080 162271 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1 10.1016/j.bmcl.2007.12.005
22317715 63071 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629854 63071 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
53326017 63195 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 1 4 5.5 COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631872 63195 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 1 4 5.5 COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
131636403 166674 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4106954 166674 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636317 167354 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 5 0 5 5.0 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
CHEMBL4112663 167354 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 5 0 5 5.0 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
69669747 190432 11 None -2 4 Human 7.8 pIC50 = 7.8 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4751065 190432 11 None -2 4 Human 7.8 pIC50 = 7.8 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802733 190432 11 None -2 4 Human 7.8 pIC50 = 7.8 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
90354858 166643 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F nan
CHEMBL4106716 166643 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F nan
67705326 160027 0 None 2 2 Human 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 457 7 4 6 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2ncc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
CHEMBL3977508 160027 0 None 2 2 Human 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 457 7 4 6 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2ncc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
131636349 152010 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3912677 152010 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
131636444 166656 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 4 0 5 4.6 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4106785 166656 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 4 0 5 4.6 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
131636315 167308 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4112341 167308 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
22317185 63065 0 None - 1 Rat 6.8 pIC50 = 6.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 410 2 2 4 5.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629848 63065 0 None - 1 Rat 6.8 pIC50 = 6.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 410 2 2 4 5.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
44345358 120127 0 None 1 2 Human 5.8 pIC50 = 5.8 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 215 5 3 3 0.5 CC(C)C[C@](N)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL331753 120127 0 None 1 2 Human 5.8 pIC50 = 5.8 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 215 5 3 3 0.5 CC(C)C[C@](N)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970497w
10456810 114656 0 None -13 5 Rat 5.8 pIC50 = 5.8 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 457 8 3 4 4.7 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1[C@H](CCc2ccccc2)[C@@H]1C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL319279 114656 0 None -13 5 Rat 5.8 pIC50 = 5.8 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 457 8 3 4 4.7 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1[C@H](CCc2ccccc2)[C@@H]1C(=O)O 10.1016/s0960-894x(98)00510-1
134132133 151567 0 None -1 2 Human 6.8 pIC50 = 6.8 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3909237 151567 0 None -1 2 Human 6.8 pIC50 = 6.8 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
44450391 175614 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 414 3 1 4 5.3 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL437835 175614 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 414 3 1 4 5.3 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
9820321 161787 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
CHEMBL401446 161787 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
135544097 162444 0 None 269 2 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 437 2 2 6 4.0 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL404886 162444 0 None 269 2 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 437 2 2 6 4.0 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
9820321 161787 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
CHEMBL401446 161787 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
67633340 190500 0 None 1 2 Human 7.8 pIC50 = 7.8 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4780402 190500 0 None 1 2 Human 7.8 pIC50 = 7.8 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4803381 190500 0 None 1 2 Human 7.8 pIC50 = 7.8 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
131636443 166625 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 6 0 5 5.5 CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1 nan
CHEMBL4106566 166625 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 6 0 5 5.5 CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1 nan
131636400 166780 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1C nan
CHEMBL4107829 166780 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1C nan
131636337 159454 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3972702 159454 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
131636401 167174 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 1 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
CHEMBL4111225 167174 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 1 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
11503055 9179 3 None -31 2 Human 4.8 pIC50 = 4.8 Functional
Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1021/jm400439t
9694 9179 3 None -31 2 Human 4.8 pIC50 = 4.8 Functional
Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1021/jm400439t
CHEMBL2204436 9179 3 None -31 2 Human 4.8 pIC50 = 4.8 Functional
Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1021/jm400439t
155538435 179146 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 447 5 1 5 5.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4476138 179146 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 447 5 1 5 5.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155539352 179614 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 369 4 1 4 4.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4514334 179614 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 369 4 1 4 4.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
155562175 182603 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4584801 182603 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1 10.1021/acs.jmedchem.8b01266
155539352 179614 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 369 4 1 4 4.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4514334 179614 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 369 4 1 4 4.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
155562175 182603 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4584801 182603 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1 10.1021/acs.jmedchem.8b01266
155538435 179146 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 447 5 1 5 5.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4476138 179146 0 None - 1 Rat 5.8 pIC50 = 5.8 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 447 5 1 5 5.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
11298568 76150 1 None 5 2 Human 5.8 pIC50 = 5.8 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O 10.1021/jm040222y
CHEMBL192977 76150 1 None 5 2 Human 5.8 pIC50 = 5.8 Functional
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O 10.1021/jm040222y
90643974 118780 0 None -3 2 Rat 5.8 pIC50 = 5.8 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 352 2 0 5 3.9 Cn1c(=O)c2ccc(-c3ccncc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288675 118780 0 None -3 2 Rat 5.8 pIC50 = 5.8 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 352 2 0 5 3.9 Cn1c(=O)c2ccc(-c3ccncc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
90643963 118772 0 None -3 2 Rat 5.8 pIC50 = 5.8 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 366 2 0 5 4.2 Cc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
CHEMBL3288653 118772 0 None -3 2 Rat 5.8 pIC50 = 5.8 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 366 2 0 5 4.2 Cc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
22224670 103042 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 415 3 1 5 4.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261081 103042 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 415 3 1 5 4.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
53316736 63058 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 3 1 3 6.1 CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629715 63058 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 3 1 3 6.1 CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
22317847 63184 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 420 2 1 4 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631861 63184 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 420 2 1 4 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
11212447 63191 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 2 4 5.0 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631868 63191 0 None - 1 Rat 7.8 pIC50 = 7.8 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 2 4 5.0 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636450 167417 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 1 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113175 167417 0 None - 1 Human 7.8 pIC50 = 7.8 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 1 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636373 166637 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4106692 166637 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636397 166762 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.0 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1OC(F)(F)F nan
CHEMBL4107640 166762 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.0 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1OC(F)(F)F nan
131636360 157027 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3952383 157027 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
131636427 167460 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 453 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4113474 167460 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 453 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
67707808 155421 0 None 1 2 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 432 6 4 6 1.3 COC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
CHEMBL3939492 155421 0 None 1 2 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 432 6 4 6 1.3 COC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
131636372 166989 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 0 6 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
CHEMBL4109618 166989 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 0 6 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
131636299 167049 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
CHEMBL4110209 167049 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
10492773 23557 0 None -2 2 Human 6.8 pIC50 = 6.8 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 277 6 3 3 1.4 Cc1cccc(CC[C@](N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
CHEMBL124501 23557 0 None -2 2 Human 6.8 pIC50 = 6.8 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 277 6 3 3 1.4 Cc1cccc(CC[C@](N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
44348993 121363 0 None 1 2 Human 6.8 pIC50 = 6.8 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 297 6 3 3 1.8 N[C@@](CCc1cccc(Cl)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL333771 121363 0 None 1 2 Human 6.8 pIC50 = 6.8 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 297 6 3 3 1.8 N[C@@](CCc1cccc(Cl)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
44348706 123660 0 None 1 2 Human 6.8 pIC50 = 6.8 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 281 6 3 3 1.3 N[C@@](CCc1ccc(F)cc1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL338282 123660 0 None 1 2 Human 6.8 pIC50 = 6.8 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 281 6 3 3 1.3 N[C@@](CCc1ccc(F)cc1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
10828532 85540 0 None -22 2 Human 5.8 pIC50 = 5.8 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 307 7 4 4 0.8 NC(CCc1cccc(C(=O)O)c1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL2112634 85540 0 None -22 2 Human 5.8 pIC50 = 5.8 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 307 7 4 4 0.8 NC(CCc1cccc(C(=O)O)c1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
10359073 161753 1 None -1 2 Human 4.8 pIC50 = 4.8 Functional
Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00091-2
CHEMBL40123 161753 1 None -1 2 Human 4.8 pIC50 = 4.8 Functional
Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00091-2
18613455 102825 0 None - 1 Rat 6.7 pIC50 = 6.7 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 414 3 1 6 3.8 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL259924 102825 0 None - 1 Rat 6.7 pIC50 = 6.7 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 414 3 1 6 3.8 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
44329031 115051 0 None -15 7 Rat 5.7 pIC50 = 5.7 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 437 10 3 4 5.0 CCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL319732 115051 0 None -15 7 Rat 5.7 pIC50 = 5.7 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 437 10 3 4 5.0 CCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
18548739 167144 0 None - 1 Rat 7.7 pIC50 = 7.7 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL411095 167144 0 None - 1 Rat 7.7 pIC50 = 7.7 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
18548739 167144 0 None - 1 Rat 7.7 pIC50 = 7.7 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL411095 167144 0 None - 1 Rat 7.7 pIC50 = 7.7 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636333 160967 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3985799 160967 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
131636339 166915 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 383 3 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
CHEMBL4108997 166915 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 383 3 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
131636378 167267 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.8 COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
CHEMBL4111987 167267 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.8 COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
131636395 167281 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4112129 167281 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636373 166637 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4106692 166637 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636407 166882 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 3 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4108700 166882 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 3 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636408 167539 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.2 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4114047 167539 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.2 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636329 151415 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.1 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1C nan
CHEMBL3908089 151415 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.1 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1C nan
131636284 167283 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4112146 167283 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
90354963 167425 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 427 4 0 5 5.3 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F nan
CHEMBL4113235 167425 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 427 4 0 5 5.3 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F nan
131636406 167155 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4111067 167155 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
90355009 167028 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4109993 167028 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1 nan
86695984 156544 0 None 1 2 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 472 7 3 8 1.9 Cn1ncnc1S[C@@H]1[C@@H](OCc2ccc(Cl)c(Cl)c2)[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1016/j.bmcl.2016.10.067
CHEMBL3948272 156544 0 None 1 2 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 472 7 3 8 1.9 Cn1ncnc1S[C@@H]1[C@@H](OCc2ccc(Cl)c(Cl)c2)[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1016/j.bmcl.2016.10.067
53316798 63179 0 None - 1 Rat 6.7 pIC50 = 6.7 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 384 2 1 4 4.6 Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
CHEMBL1631856 63179 0 None - 1 Rat 6.7 pIC50 = 6.7 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 384 2 1 4 4.6 Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
44348846 123790 0 None -1 2 Human 6.7 pIC50 = 6.7 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 341 7 3 5 0.5 CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
CHEMBL2111822 123790 0 None -1 2 Human 6.7 pIC50 = 6.7 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 341 7 3 5 0.5 CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
CHEMBL338911 123790 0 None -1 2 Human 6.7 pIC50 = 6.7 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 341 7 3 5 0.5 CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
90643954 118767 0 None -2 2 Rat 5.7 pIC50 = 5.7 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 430 3 1 6 3.2 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288636 118767 0 None -2 2 Rat 5.7 pIC50 = 5.7 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 430 3 1 6 3.2 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
155523578 177687 0 None - 1 Rat 5.7 pIC50 = 5.7 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4454867 177687 0 None - 1 Rat 5.7 pIC50 = 5.7 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
155523578 177687 0 None - 1 Rat 5.7 pIC50 = 5.7 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4454867 177687 0 None - 1 Rat 5.7 pIC50 = 5.7 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
11304010 63081 0 None 2 3 Rat 8.7 pIC50 = 8.7 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629864 63081 0 None 2 3 Rat 8.7 pIC50 = 8.7 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
122580902 166784 0 None - 1 Human 8.7 pIC50 = 8.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4107872 166784 0 None - 1 Human 8.7 pIC50 = 8.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636451 166789 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4107913 166789 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636422 166821 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 467 5 0 5 5.3 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
CHEMBL4108163 166821 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 467 5 0 5 5.3 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
131636461 166903 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108918 166903 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
78320558 167226 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4111659 167226 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1 nan
90354985 167458 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 425 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113466 167458 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 425 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
78319944 167510 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.0 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F nan
CHEMBL4113834 167510 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.0 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F nan
78320252 167304 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 411 4 0 5 5.2 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
CHEMBL4112321 167304 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 411 4 0 5 5.2 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
90354835 167343 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112598 167343 0 None - 1 Human 8.6 pIC50 = 8.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636455 167183 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4111276 167183 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636460 167258 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.9 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C nan
CHEMBL4111924 167258 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.9 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C nan
1397 9307 15 None 1 8 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
9886034 9307 15 None 1 8 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
CHEMBL186453 9307 15 None 1 8 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
22317728 63063 0 None - 1 Rat 7.7 pIC50 = 7.7 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629846 63063 0 None - 1 Rat 7.7 pIC50 = 7.7 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
71566598 149468 15 None 1 3 Human 7.7 pIC50 = 7.7 Functional
Negative allosteric modulation of human mGluR2 by GTPgammaS binding assayNegative allosteric modulation of human mGluR2 by GTPgammaS binding assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3892073 149468 15 None 1 3 Human 7.7 pIC50 = 7.7 Functional
Negative allosteric modulation of human mGluR2 by GTPgammaS binding assayNegative allosteric modulation of human mGluR2 by GTPgammaS binding assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
67637138 190397 0 None 2 2 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4776989 190397 0 None 2 2 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802329 190397 0 None 2 2 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
131636365 166774 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4107737 166774 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636282 167358 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112692 167358 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636409 167240 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 467 6 0 5 5.7 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C(F)F)n1 nan
CHEMBL4111753 167240 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 467 6 0 5 5.7 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C(F)F)n1 nan
131636331 151678 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3910129 151678 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
131636297 166761 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4107635 166761 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
122580890 167255 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4111874 167255 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
10807972 42591 1 None -12 4 Human 6.7 pIC50 = 6.7 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL144151 42591 1 None -12 4 Human 6.7 pIC50 = 6.7 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
1378 9195 54 None -9 14 Rat 6.7 pIC50 = 6.7 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(98)00510-1
1399 9195 54 None -9 14 Rat 6.7 pIC50 = 6.7 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(98)00510-1
9819927 9195 54 None -9 14 Rat 6.7 pIC50 = 6.7 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(98)00510-1
CHEMBL432038 9195 54 None -9 14 Rat 6.7 pIC50 = 6.7 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(98)00510-1
10358265 108903 0 None -2 2 Human 4.7 pIC50 = 4.7 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 314 4 3 4 1.3 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc3ccccc23)C1 10.1016/s0960-894x(98)00352-7
CHEMBL302411 108903 0 None -2 2 Human 4.7 pIC50 = 4.7 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 314 4 3 4 1.3 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc3ccccc23)C1 10.1016/s0960-894x(98)00352-7
162663798 190498 0 None 1 2 Human 5.7 pIC50 = 5.7 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4779554 190498 0 None 1 2 Human 5.7 pIC50 = 5.7 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4803378 190498 0 None 1 2 Human 5.7 pIC50 = 5.7 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
1378 9195 54 None -2 14 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmcl.2012.01.039
1399 9195 54 None -2 14 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmcl.2012.01.039
9819927 9195 54 None -2 14 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmcl.2012.01.039
CHEMBL432038 9195 54 None -2 14 Human 7.7 pIC50 = 7.7 Functional
Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmcl.2012.01.039
131636435 155169 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 5 0 5 4.5 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1CC nan
CHEMBL3937514 155169 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 5 0 5 4.5 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1CC nan
131636361 167453 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113439 167453 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636283 167563 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 3 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4114284 167563 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 3 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
131636454 166744 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4107497 166744 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636290 167278 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112105 167278 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
122580905 166845 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108383 166845 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636285 167726 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.2 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4115529 167726 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.2 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
134154496 159289 0 None -1 2 Human 6.7 pIC50 = 6.7 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 341 5 4 5 0.3 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3971347 159289 0 None -1 2 Human 6.7 pIC50 = 6.7 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 341 5 4 5 0.3 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
134141510 153846 0 None -2 2 Human 6.7 pIC50 = 6.7 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 339 5 4 5 0.1 Cc1cc(CO[C@@H]2[C@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1016/j.bmcl.2016.10.067
CHEMBL3927108 153846 0 None -2 2 Human 6.7 pIC50 = 6.7 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 339 5 4 5 0.1 Cc1cc(CO[C@@H]2[C@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1016/j.bmcl.2016.10.067
44329029 170300 0 None 2 6 Rat 5.7 pIC50 = 5.7 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 479 13 3 4 6.2 CCCCCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL420262 170300 0 None 2 6 Rat 5.7 pIC50 = 5.7 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 479 13 3 4 6.2 CCCCCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
9952648 103083 0 None 1 2 Rat 7.7 pIC50 = 7.7 Functional
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261288 103083 0 None 1 2 Rat 7.7 pIC50 = 7.7 Functional
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
118906265 152726 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.7 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)(F)F nan
CHEMBL3918111 152726 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.7 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)(F)F nan
131636314 166820 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4108162 166820 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
131636448 167319 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(C)c(OCC(C)C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112439 167319 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(C)c(OCC(C)C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636346 159279 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F nan
CHEMBL3971278 159279 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F nan
131636369 167596 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 4 5.8 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4114534 167596 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 4 5.8 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636276 152685 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 383 3 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl nan
CHEMBL3917816 152685 0 None - 1 Human 7.7 pIC50 = 7.7 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 383 3 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl nan
90367528 150859 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl nan
CHEMBL3903357 150859 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl nan
44348911 23338 0 None 1 2 Human 6.7 pIC50 = 6.7 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 331 6 3 3 2.1 N[C@@](CCc1cccc(C(F)(F)F)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL123847 23338 0 None 1 2 Human 6.7 pIC50 = 6.7 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 331 6 3 3 2.1 N[C@@](CCc1cccc(C(F)(F)F)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
10688450 23376 0 None -1 2 Human 6.7 pIC50 = 6.7 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 339 7 3 3 2.7 N[C@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL124078 23376 0 None -1 2 Human 6.7 pIC50 = 6.7 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 339 7 3 3 2.7 N[C@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
155547618 180365 0 None - 1 Rat 6.7 pIC50 = 6.7 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 441 5 1 6 3.4 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4533083 180365 0 None - 1 Rat 6.7 pIC50 = 6.7 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 441 5 1 6 3.4 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155547618 180365 0 None - 1 Rat 6.7 pIC50 = 6.7 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 441 5 1 6 3.4 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4533083 180365 0 None - 1 Rat 6.7 pIC50 = 6.7 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 441 5 1 6 3.4 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1 10.1021/acs.jmedchem.8b01266
134129940 149224 0 None -1 2 Human 6.7 pIC50 = 6.7 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 359 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3890112 149224 0 None -1 2 Human 6.7 pIC50 = 6.7 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 359 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
162652146 186992 0 None 1 2 Human 5.6 pIC50 = 5.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 289 5 4 5 -0.2 CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4749728 186992 0 None 1 2 Human 5.6 pIC50 = 5.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 289 5 4 5 -0.2 CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O 10.1021/acs.jmedchem.6b01119
1378 9195 54 None -2 14 Human 7.6 pIC50 = 7.6 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm970498o
1399 9195 54 None -2 14 Human 7.6 pIC50 = 7.6 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm970498o
9819927 9195 54 None -2 14 Human 7.6 pIC50 = 7.6 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm970498o
CHEMBL432038 9195 54 None -2 14 Human 7.6 pIC50 = 7.6 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm970498o
22224852 102639 0 None -2 2 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259054 102639 0 None -2 2 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
9845873 167578 0 None - 1 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL411440 167578 0 None - 1 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
9845873 167578 0 None - 1 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL411440 167578 0 None - 1 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
131636382 167186 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.8 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F nan
CHEMBL4111287 167186 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.8 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F nan
131636396 167020 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 3 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4109918 167020 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 3 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636301 167215 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4111566 167215 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
10852666 85516 0 None 1 2 Human 6.6 pIC50 = 6.6 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 313 6 3 3 2.3 NC(CCc1cccc2ccccc12)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112583 85516 0 None 1 2 Human 6.6 pIC50 = 6.6 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 313 6 3 3 2.3 NC(CCc1cccc2ccccc12)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
10567792 85519 0 None 3 2 Human 6.6 pIC50 = 6.6 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 321 6 3 3 2.5 NC(CCC12CC3CC(CC(C3)C1)C2)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112586 85519 0 None 3 2 Human 6.6 pIC50 = 6.6 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 321 6 3 3 2.5 NC(CCC12CC3CC(CC(C3)C1)C2)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
90355016 167481 0 None - 1 Human 6.6 pIC50 = 6.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 1 6 3.7 COc1cc(-c2nc(-c3ccnc(CO)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
CHEMBL4113592 167481 0 None - 1 Human 6.6 pIC50 = 6.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 1 6 3.7 COc1cc(-c2nc(-c3ccnc(CO)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
86298614 118781 0 None -3 2 Rat 6.6 pIC50 = 6.6 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 353 2 0 6 3.3 Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288676 118781 0 None -3 2 Rat 6.6 pIC50 = 6.6 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 353 2 0 6 3.3 Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
86298614 118781 0 None -3 2 Rat 6.6 pIC50 = 6.6 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 353 2 0 6 3.3 Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288676 118781 0 None -3 2 Rat 6.6 pIC50 = 6.6 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 353 2 0 6 3.3 Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
11211597 63082 0 None -1 3 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629865 63082 0 None -1 3 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
131636336 155443 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 378 2 0 5 4.3 Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3939714 155443 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 378 2 0 5 4.3 Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCOCC3)cc(C)n1 nan
131636311 159427 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 4 0 5 4.3 COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2CCOCC3)ccc1Cl nan
CHEMBL3972441 159427 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 4 0 5 4.3 COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2CCOCC3)ccc1Cl nan
131636326 167338 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4112588 167338 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636323 154840 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3934756 154840 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCOCC3)cc(C)n1 nan
131636298 166907 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 4 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4108936 166907 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 4 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)ccn1 nan
122580894 167472 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 4 5.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113546 167472 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 4 5.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
155538978 179561 0 None - 1 Rat 5.6 pIC50 = 5.6 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 383 5 1 6 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4513332 179561 0 None - 1 Rat 5.6 pIC50 = 5.6 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 383 5 1 6 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1 10.1021/acs.jmedchem.8b01266
155538978 179561 0 None - 1 Rat 5.6 pIC50 = 5.6 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 383 5 1 6 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4513332 179561 0 None - 1 Rat 5.6 pIC50 = 5.6 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 383 5 1 6 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1 10.1021/acs.jmedchem.8b01266
155514808 176677 0 None - 1 Rat 5.6 pIC50 = 5.6 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4440771 176677 0 None - 1 Rat 5.6 pIC50 = 5.6 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
155514808 176677 0 None - 1 Rat 5.6 pIC50 = 5.6 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4440771 176677 0 None - 1 Rat 5.6 pIC50 = 5.6 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
11269030 63078 0 None -1 3 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629861 63078 0 None -1 3 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
131636328 155524 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 2 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3940380 155524 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 2 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
131636354 167129 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 392 2 0 5 4.7 Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4110789 167129 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 392 2 0 5 4.7 Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
67705376 152117 0 None -1 2 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 416 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
CHEMBL3913414 152117 0 None -1 2 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 416 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
69669820 190419 0 None -2 2 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
CHEMBL4746125 190419 0 None -2 2 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
CHEMBL4802570 190419 0 None -2 2 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
131636374 166879 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4108665 166879 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
90354688 167318 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCCF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112422 167318 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCCF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
1378 9195 54 None -2 14 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
1399 9195 54 None -2 14 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
9819927 9195 54 None -2 14 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
CHEMBL432038 9195 54 None -2 14 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
131636393 166851 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 4.9 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4108446 166851 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 4.9 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636442 167730 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 6 0 5 5.2 CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1 nan
CHEMBL4115553 167730 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 6 0 5 5.2 CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1 nan
18613373 102949 0 None - 1 Rat 6.6 pIC50 = 6.6 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 442 5 2 6 4.8 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL260643 102949 0 None - 1 Rat 6.6 pIC50 = 6.6 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 442 5 2 6 4.8 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
22224657 102947 0 None 2 2 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260636 102947 0 None 2 2 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
9952648 103083 0 None 1 2 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL261288 103083 0 None 1 2 Rat 7.6 pIC50 = 7.6 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
131636338 154760 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.1 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3934173 154760 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.1 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCOCC3)cc(C)n1 nan
131636432 157069 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3952745 157069 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCOCC3)cc(C)n1 nan
69669646 190458 0 None 2 2 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
CHEMBL4757159 190458 0 None 2 2 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
CHEMBL4802990 190458 0 None 2 2 Human 7.6 pIC50 = 7.6 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
131636367 153415 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 459 5 0 6 5.2 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3923457 153415 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 459 5 0 6 5.2 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
131636357 167484 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 2 0 4 5.3 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113614 167484 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 2 0 4 5.3 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354626 166642 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 4 0 5 4.7 COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
CHEMBL4106714 166642 0 None - 1 Human 7.6 pIC50 = 7.6 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 4 0 5 4.7 COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
131636286 166675 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 6 4.6 COc1cc(-c2nc(-c3ccc(Cl)c(OC)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4106958 166675 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 6 4.6 COc1cc(-c2nc(-c3ccc(Cl)c(OC)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636319 160841 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3984622 160841 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
134144441 157173 0 None -1 2 Human 6.6 pIC50 = 6.6 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 341 5 4 5 0.3 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3953570 157173 0 None -1 2 Human 6.6 pIC50 = 6.6 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 341 5 4 5 0.3 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
44329042 175862 0 None -38 5 Rat 5.5 pIC50 = 5.5 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 381 6 3 4 3.5 CC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL439775 175862 0 None -38 5 Rat 5.5 pIC50 = 5.5 Functional
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 381 6 3 4 3.5 CC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
155555318 181097 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 6 1 7 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4550517 181097 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 6 1 7 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
155555318 181097 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 6 1 7 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4550517 181097 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 6 1 7 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
131636300 166912 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 4 0 5 4.1 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
CHEMBL4108984 166912 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 4 0 5 4.1 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
131636399 167495 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
CHEMBL4113737 167495 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
131636312 167083 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 4 0 5 4.9 C[C@@H]1Cn2c(-c3ccc(OC(F)(F)F)cc3)nc(-c3ccnc(CF)c3)c2CCO1 nan
CHEMBL4110503 167083 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 4 0 5 4.9 C[C@@H]1Cn2c(-c3ccc(OC(F)(F)F)cc3)nc(-c3ccnc(CF)c3)c2CCO1 nan
22224852 102639 0 None -2 2 Rat 6.5 pIC50 = 6.5 Functional
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259054 102639 0 None -2 2 Rat 6.5 pIC50 = 6.5 Functional
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
11158623 10124 11 None 1 4 Rat 8.5 pIC50 = 8.5 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
6226 10124 11 None 1 4 Rat 8.5 pIC50 = 8.5 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
CHEMBL1629855 10124 11 None 1 4 Rat 8.5 pIC50 = 8.5 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
11484819 63080 0 None 2 2 Rat 8.5 pIC50 = 8.5 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629863 63080 0 None 2 2 Rat 8.5 pIC50 = 8.5 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
11406781 63199 0 None - 1 Rat 8.5 pIC50 = 8.5 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631876 63199 0 None - 1 Rat 8.5 pIC50 = 8.5 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636376 167435 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4113300 167435 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
78319946 167711 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4115420 167711 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636324 166891 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108816 166891 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
78320250 167241 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 0 6 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
CHEMBL4111755 167241 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 0 6 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
78320247 167237 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4111744 167237 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
78324635 167245 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4111773 167245 0 None - 1 Human 8.5 pIC50 = 8.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636416 167674 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 460 4 0 6 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4115199 167674 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 460 4 0 6 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636417 166796 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 446 4 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4107975 166796 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 446 4 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636305 166864 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3ccnc(C)c3)c2CCO1 nan
CHEMBL4108564 166864 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3ccnc(C)c3)c2CCO1 nan
78319945 167121 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 6 4.7 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F nan
CHEMBL4110721 167121 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 6 4.7 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F nan
78319941 167721 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.2 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
CHEMBL4115490 167721 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.2 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
131636446 167321 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.9 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4112442 167321 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.9 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
22317318 63198 0 None - 1 Rat 7.5 pIC50 = 7.5 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631875 63198 0 None - 1 Rat 7.5 pIC50 = 7.5 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636456 166647 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 1 6 4.0 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4106741 166647 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 1 6 4.0 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636412 166964 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 6 1 6 3.9 Cc1cc(-c2nc(-c3ccc(OCF)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1 nan
CHEMBL4109387 166964 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 6 1 6 3.9 Cc1cc(-c2nc(-c3ccc(OCF)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1 nan
131636306 158041 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C(F)F)OCC3)ccc1Cl nan
CHEMBL3960280 158041 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C(F)F)OCC3)ccc1Cl nan
15392101 107215 0 None - 1 Rat 4.5 pIC50 = 4.5 Functional
Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding
ChEMBL 517 7 0 7 5.8 COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1 10.1016/j.bmcl.2007.10.026
CHEMBL290509 107215 0 None - 1 Rat 4.5 pIC50 = 4.5 Functional
Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding
ChEMBL 517 7 0 7 5.8 COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1 10.1016/j.bmcl.2007.10.026
4694355 105515 36 None - 1 Rat 4.5 pIC50 = 4.5 Functional
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 257 2 4 3 -0.3 NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21 10.1016/S0960-894X(97)00177-7
CHEMBL277961 105515 36 None - 1 Rat 4.5 pIC50 = 4.5 Functional
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 257 2 4 3 -0.3 NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21 10.1016/S0960-894X(97)00177-7
134144056 157416 0 None -1 2 Human 6.5 pIC50 = 6.5 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 307 5 4 5 -0.3 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3955458 157416 0 None -1 2 Human 6.5 pIC50 = 6.5 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 307 5 4 5 -0.3 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
131636303 167584 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4114464 167584 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636293 166918 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3cccc(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4109021 166918 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3cccc(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636343 151649 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.5 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3909878 151649 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.5 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
90354563 156461 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 427 3 0 5 4.6 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Br nan
CHEMBL3947609 156461 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 427 3 0 5 4.6 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Br nan
44348859 23336 0 None -15 2 Human 5.5 pIC50 = 5.5 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 278 6 4 4 0.7 Nc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
CHEMBL123842 23336 0 None -15 2 Human 5.5 pIC50 = 5.5 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 278 6 4 4 0.7 Nc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
21309795 157602 0 None -3 2 Human 6.5 pIC50 = 6.5 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 327 4 3 3 1.8 N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
CHEMBL3956934 157602 0 None -3 2 Human 6.5 pIC50 = 6.5 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 327 4 3 3 1.8 N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
90643961 118771 0 None -2 2 Rat 5.5 pIC50 = 5.5 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 382 3 0 6 3.9 COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
CHEMBL3288649 118771 0 None -2 2 Rat 5.5 pIC50 = 5.5 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 382 3 0 6 3.9 COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
155538001 179124 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4475753 179124 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4580695 179124 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
155538001 179124 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4475753 179124 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4580695 179124 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
131636355 167645 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.6 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4114983 167645 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.6 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636341 154729 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 428 3 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3933840 154729 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 428 3 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCOCC3)cc(C)n1 nan
131636359 167551 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 3 0 5 4.3 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F nan
CHEMBL4114183 167551 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 3 0 5 4.3 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F nan
162665071 190507 0 None 1 2 Human 6.5 pIC50 = 6.5 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4781638 190507 0 None 1 2 Human 6.5 pIC50 = 6.5 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803454 190507 0 None 1 2 Human 6.5 pIC50 = 6.5 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
18548862 164718 0 None - 1 Rat 7.5 pIC50 = 7.5 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 415 4 1 6 4.1 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL408455 164718 0 None - 1 Rat 7.5 pIC50 = 7.5 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 415 4 1 6 4.1 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
134137754 154726 0 None 1 2 Human 7.5 pIC50 = 7.5 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 400 6 3 5 2.3 [N-]=[N+]=N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
CHEMBL3933829 154726 0 None 1 2 Human 7.5 pIC50 = 7.5 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 400 6 3 5 2.3 [N-]=[N+]=N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
131636320 157479 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 407 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3956003 157479 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 407 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCOCC3)cc(C)n1 nan
155550453 181048 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4549344 181048 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
155550453 181048 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4549344 181048 0 None - 1 Rat 6.5 pIC50 = 6.5 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
22448579 162557 0 None 4 2 Rat 7.5 pIC50 = 7.5 Functional
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 412 3 2 5 4.8 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL405895 162557 0 None 4 2 Rat 7.5 pIC50 = 7.5 Functional
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 412 3 2 5 4.8 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
131636302 166800 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 3 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4108010 166800 0 None - 1 Human 7.5 pIC50 = 7.5 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 3 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
22224825 165773 0 None - 1 Rat 7.4 pIC50 = 7.4 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL409638 165773 0 None - 1 Rat 7.4 pIC50 = 7.4 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
11211597 63082 0 None -1 3 Rat 7.4 pIC50 = 7.4 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629865 63082 0 None -1 3 Rat 7.4 pIC50 = 7.4 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
131636347 149789 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F nan
CHEMBL3894707 149789 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F nan
131636457 167328 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(Cl)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112521 167328 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(Cl)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636386 167741 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 6 0 6 4.4 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
CHEMBL4115662 167741 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 6 0 6 4.4 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
131636358 155785 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3942377 155785 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
44302608 107623 0 None -2 2 Human 4.4 pIC50 = 4.4 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 340 5 3 4 1.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2-c2ccccc2)C1 10.1016/s0960-894x(98)00352-7
CHEMBL293434 107623 0 None -2 2 Human 4.4 pIC50 = 4.4 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 340 5 3 4 1.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2-c2ccccc2)C1 10.1016/s0960-894x(98)00352-7
155531624 178452 0 None - 1 Rat 5.4 pIC50 = 5.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 387 4 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4466304 178452 0 None - 1 Rat 5.4 pIC50 = 5.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 387 4 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1 10.1021/acs.jmedchem.8b01266
155531624 178452 0 None - 1 Rat 5.4 pIC50 = 5.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 387 4 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4466304 178452 0 None - 1 Rat 5.4 pIC50 = 5.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 387 4 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1 10.1021/acs.jmedchem.8b01266
9952648 103083 0 None 1 2 Rat 7.4 pIC50 = 7.4 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261288 103083 0 None 1 2 Rat 7.4 pIC50 = 7.4 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
131636291 167065 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4110331 167065 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
44302856 109508 0 None 1 2 Human 4.4 pIC50 = 4.4 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 354 6 3 4 1.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(c2ccccc2)c2ccccc2)C1 10.1016/s0960-894x(98)00352-7
CHEMBL304919 109508 0 None 1 2 Human 4.4 pIC50 = 4.4 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 354 6 3 4 1.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(c2ccccc2)c2ccccc2)C1 10.1016/s0960-894x(98)00352-7
11235624 63079 0 None -6 3 Human 7.4 pIC50 = 7.4 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629862 63079 0 None -6 3 Human 7.4 pIC50 = 7.4 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636394 167357 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 4 4.6 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4112680 167357 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 4 4.6 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636398 167023 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 5 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
CHEMBL4109944 167023 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 5 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
134152341 160242 0 None -2 2 Human 6.4 pIC50 = 6.4 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3979475 160242 0 None -2 2 Human 6.4 pIC50 = 6.4 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
155542028 179870 0 None - 1 Rat 5.4 pIC50 = 5.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 4 1 5 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4520084 179870 0 None - 1 Rat 5.4 pIC50 = 5.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 4 1 5 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1 10.1021/acs.jmedchem.8b01266
155542028 179870 0 None - 1 Rat 5.4 pIC50 = 5.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 4 1 5 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4520084 179870 0 None - 1 Rat 5.4 pIC50 = 5.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 4 1 5 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1 10.1021/acs.jmedchem.8b01266
18548824 164515 0 None - 1 Rat 7.4 pIC50 = 7.4 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL408229 164515 0 None - 1 Rat 7.4 pIC50 = 7.4 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
18548824 164515 0 None - 1 Rat 7.4 pIC50 = 7.4 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL408229 164515 0 None - 1 Rat 7.4 pIC50 = 7.4 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
90643966 118775 0 None -1 2 Rat 5.4 pIC50 = 5.4 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 448 3 1 6 3.3 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(F)cc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288660 118775 0 None -1 2 Rat 5.4 pIC50 = 5.4 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 448 3 1 6 3.3 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(F)cc3)cc12 10.1016/j.bmcl.2014.04.051
11351088 63072 0 None - 1 Rat 8.4 pIC50 = 8.4 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.4 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629856 63072 0 None - 1 Rat 8.4 pIC50 = 8.4 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.4 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
22317928 63073 0 None - 1 Rat 8.4 pIC50 = 8.4 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 449 3 1 3 6.7 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629857 63073 0 None - 1 Rat 8.4 pIC50 = 8.4 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 449 3 1 3 6.7 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1 10.1016/j.bmcl.2010.09.125
11281280 63182 0 None 1 3 Rat 8.4 pIC50 = 8.4 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631859 63182 0 None 1 3 Rat 8.4 pIC50 = 8.4 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
131636425 167264 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4111952 167264 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
131636383 167521 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4113929 167521 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
69669747 190432 11 None -2 4 Human 8.4 pIC50 = 8.4 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4751065 190432 11 None -2 4 Human 8.4 pIC50 = 8.4 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802733 190432 11 None -2 4 Human 8.4 pIC50 = 8.4 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
78320560 166699 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
CHEMBL4107140 166699 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
78320248 167525 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4113962 167525 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636390 166861 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 442 3 0 6 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108541 166861 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 442 3 0 6 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
77461009 167076 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 3 0 5 5.2 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
CHEMBL4110444 167076 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 3 0 5 5.2 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
90354889 167482 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.8 CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC nan
CHEMBL4113601 167482 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.8 CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC nan
131636421 166749 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.4 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
CHEMBL4107565 166749 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.4 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
131636313 167380 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4112898 167380 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
131636356 167548 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 3 0 5 5.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4114150 167548 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 3 0 5 5.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636348 166641 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4106709 166641 0 None - 1 Human 8.4 pIC50 = 8.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636391 166887 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 428 3 0 6 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4108785 166887 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 428 3 0 6 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636431 167066 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.3 COc1ccc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
CHEMBL4110332 167066 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.3 COc1ccc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
131636429 167379 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4112889 167379 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
78320559 167682 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4115237 167682 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636295 167707 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4115390 167707 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
78320249 167043 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.8 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
CHEMBL4110153 167043 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.8 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
131636424 166680 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 460 4 0 6 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4106969 166680 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 460 4 0 6 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
131636279 150503 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3900589 150503 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
131636345 150892 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 0 5 4.7 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)F nan
CHEMBL3903640 150892 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 0 5 4.7 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)F nan
21309795 157602 0 None -3 2 Human 6.4 pIC50 = 6.4 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 327 4 3 3 1.8 N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.6b01119
CHEMBL3956934 157602 0 None -3 2 Human 6.4 pIC50 = 6.4 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 327 4 3 3 1.8 N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.6b01119
11281280 63182 0 None -5 3 Human 7.4 pIC50 = 7.4 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631859 63182 0 None -5 3 Human 7.4 pIC50 = 7.4 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
131636287 167289 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.7 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4112202 167289 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.7 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636411 167282 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.5 COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
CHEMBL4112136 167282 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.5 COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
44302686 207695 0 None -1 2 Human 4.4 pIC50 = 4.4 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 332 4 3 4 1.4 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2c(Cl)cccc2Cl)C1 10.1016/s0960-894x(98)00352-7
CHEMBL60164 207695 0 None -1 2 Human 4.4 pIC50 = 4.4 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 332 4 3 4 1.4 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2c(Cl)cccc2Cl)C1 10.1016/s0960-894x(98)00352-7
155540306 179678 0 None - 1 Rat 6.4 pIC50 = 6.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 424 6 1 7 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4516001 179678 0 None - 1 Rat 6.4 pIC50 = 6.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 424 6 1 7 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
90643968 118776 0 None -6 2 Rat 6.4 pIC50 = 6.4 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 370 2 0 5 4.1 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(F)cc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288662 118776 0 None -6 2 Rat 6.4 pIC50 = 6.4 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 370 2 0 5 4.1 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(F)cc3)cc12 10.1016/j.bmcl.2014.04.051
155540306 179678 0 None - 1 Rat 6.4 pIC50 = 6.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 424 6 1 7 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4516001 179678 0 None - 1 Rat 6.4 pIC50 = 6.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 424 6 1 7 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
131636392 167097 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 469 5 1 6 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1 nan
CHEMBL4110601 167097 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 469 5 1 6 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1 nan
44348939 125272 0 None -2 2 Human 6.4 pIC50 = 6.4 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 293 7 3 4 1.1 COc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
CHEMBL341457 125272 0 None -2 2 Human 6.4 pIC50 = 6.4 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 293 7 3 4 1.1 COc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
1373 9253 51 None -1 4 Human 5.4 pIC50 = 5.4 Functional
Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor
ChEMBL 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10.1021/jm060950g
139055582 9253 51 None -1 4 Human 5.4 pIC50 = 5.4 Functional
Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor
ChEMBL 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10.1021/jm060950g
446355 9253 51 None -1 4 Human 5.4 pIC50 = 5.4 Functional
Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor
ChEMBL 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10.1021/jm060950g
CHEMBL257626 9253 51 None -1 4 Human 5.4 pIC50 = 5.4 Functional
Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor
ChEMBL 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10.1021/jm060950g
DB04256 9253 51 None -1 4 Human 5.4 pIC50 = 5.4 Functional
Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor
ChEMBL 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10.1021/jm060950g
11777615 105637 0 None 2 2 Rat 4.4 pIC50 = 4.4 Functional
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 265 2 3 4 1.2 CC1(C)CC(N)(C(=O)O)c2ccc(C(=O)O)cc2O1 10.1016/S0960-894X(97)00177-7
CHEMBL278949 105637 0 None 2 2 Rat 4.4 pIC50 = 4.4 Functional
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 265 2 3 4 1.2 CC1(C)CC(N)(C(=O)O)c2ccc(C(=O)O)cc2O1 10.1016/S0960-894X(97)00177-7
10783272 92897 0 None -15 2 Human 5.4 pIC50 = 5.4 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 339 7 3 3 2.7 N[C@@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2311086 92897 0 None -15 2 Human 5.4 pIC50 = 5.4 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 339 7 3 3 2.7 N[C@@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
131636380 167497 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4113748 167497 0 None - 1 Human 7.4 pIC50 = 7.4 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
155538001 179124 0 None - 1 Rat 6.4 pIC50 = 6.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4475753 179124 0 None - 1 Rat 6.4 pIC50 = 6.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4580695 179124 0 None - 1 Rat 6.4 pIC50 = 6.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
155538001 179124 0 None - 1 Rat 6.4 pIC50 = 6.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4475753 179124 0 None - 1 Rat 6.4 pIC50 = 6.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4580695 179124 0 None - 1 Rat 6.4 pIC50 = 6.4 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
131636274 151416 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3908096 151416 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)cc(C)n1 nan
69669702 190454 0 None 3 2 Human 7.3 pIC50 = 7.3 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4756556 190454 0 None 3 2 Human 7.3 pIC50 = 7.3 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4802948 190454 0 None 3 2 Human 7.3 pIC50 = 7.3 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
131636368 166866 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.7 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4108571 166866 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.7 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
10732318 85518 0 None 6 2 Human 6.4 pIC50 = 6.4 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 291 8 3 3 1.9 NC(CCCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112585 85518 0 None 6 2 Human 6.4 pIC50 = 6.4 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 291 8 3 3 1.9 NC(CCCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
10385210 19804 0 None 2 3 Rat 4.4 pIC50 = 4.4 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1189910 19804 0 None 2 3 Rat 4.4 pIC50 = 4.4 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL539760 19804 0 None 2 3 Rat 4.4 pIC50 = 4.4 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1 10.1016/s0960-894x(01)00329-8
10250423 19785 0 None -1 2 Rat 4.4 pIC50 = 4.4 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%
ChEMBL 364 4 3 4 1.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1189797 19785 0 None -1 2 Rat 4.4 pIC50 = 4.4 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%
ChEMBL 364 4 3 4 1.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL539516 19785 0 None -1 2 Rat 4.4 pIC50 = 4.4 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%
ChEMBL 364 4 3 4 1.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1 10.1016/s0960-894x(01)00329-8
57338826 156406 0 None 1 5 Human 7.3 pIC50 = 7.3 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3947221 156406 0 None 1 5 Human 7.3 pIC50 = 7.3 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
131636459 167634 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.0 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F nan
CHEMBL4114912 167634 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.0 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F nan
44302931 170049 0 None - 1 Human 4.3 pIC50 = 4.3 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 270 4 3 4 0.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC2CCCCC2)C1 10.1016/s0960-894x(98)00352-7
CHEMBL418650 170049 0 None - 1 Human 4.3 pIC50 = 4.3 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 270 4 3 4 0.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC2CCCCC2)C1 10.1016/s0960-894x(98)00352-7
90643973 118779 0 None -1 2 Rat 5.3 pIC50 = 5.3 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 382 4 1 6 3.4 O=c1c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc2n1CCO 10.1016/j.bmcl.2014.04.051
CHEMBL3288674 118779 0 None -1 2 Rat 5.3 pIC50 = 5.3 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 382 4 1 6 3.4 O=c1c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc2n1CCO 10.1016/j.bmcl.2014.04.051
22224570 102690 0 None - 1 Rat 7.3 pIC50 = 7.3 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 378 3 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259269 102690 0 None - 1 Rat 7.3 pIC50 = 7.3 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 378 3 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1 10.1016/j.bmcl.2008.02.076
131636344 155093 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 4 0 5 4.2 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)ccn1 nan
CHEMBL3936936 155093 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 4 0 5 4.2 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)ccn1 nan
131636362 166791 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4107924 166791 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
22317491 63070 0 None - 1 Rat 7.3 pIC50 = 7.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629853 63070 0 None - 1 Rat 7.3 pIC50 = 7.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636437 150784 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1Cl nan
CHEMBL3902842 150784 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1Cl nan
1297 177031 36 None -1 2 Human 4.3 pIC50 = 4.3 Functional
Ability to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M ConcentrationAbility to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M Concentration
ChEMBL 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 10.1021/jm00019a002
CHEMBL444589 177031 36 None -1 2 Human 4.3 pIC50 = 4.3 Functional
Ability to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M ConcentrationAbility to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M Concentration
ChEMBL 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 10.1021/jm00019a002
162658340 190465 0 None 1 2 Human 7.3 pIC50 = 7.3 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4760856 190465 0 None 1 2 Human 7.3 pIC50 = 7.3 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803084 190465 0 None 1 2 Human 7.3 pIC50 = 7.3 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
131636321 156144 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(F)c(OCC(C)C)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3945334 156144 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(F)c(OCC(C)C)c3)n3c2CCOCC3)cc(C)n1 nan
70051296 96833 0 None -1 3 Human 5.3 pIC50 = 5.3 Functional
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
CHEMBL2381648 96833 0 None -1 3 Human 5.3 pIC50 = 5.3 Functional
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
22317724 63062 0 None - 1 Rat 8.3 pIC50 = 8.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 409 2 1 3 5.8 Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629845 63062 0 None - 1 Rat 8.3 pIC50 = 8.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 409 2 1 3 5.8 Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
53317987 63075 0 None - 1 Rat 8.3 pIC50 = 8.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 453 4 1 4 6.0 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629859 63075 0 None - 1 Rat 8.3 pIC50 = 8.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 453 4 1 4 6.0 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
11362246 63183 0 None - 1 Rat 8.3 pIC50 = 8.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 3 1 3 6.1 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631860 63183 0 None - 1 Rat 8.3 pIC50 = 8.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 3 1 3 6.1 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
53325611 63190 0 None - 1 Rat 8.3 pIC50 = 8.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 485 4 1 3 7.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631867 63190 0 None - 1 Rat 8.3 pIC50 = 8.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 485 4 1 3 7.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636413 166869 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 6 0 6 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
CHEMBL4108588 166869 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 6 0 6 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
131636381 167348 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4112623 167348 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636384 167580 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4114409 167580 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
78320251 167723 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 3 0 5 4.9 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
CHEMBL4115497 167723 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 3 0 5 4.9 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
131636430 167499 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 7 0 6 4.9 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
CHEMBL4113756 167499 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 7 0 6 4.9 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
90354553 166693 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.3 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
CHEMBL4107066 166693 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.3 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
131636464 167084 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.5 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C nan
CHEMBL4110505 167084 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.5 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C nan
131636420 167135 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4110839 167135 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
131636426 166716 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 441 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4107266 166716 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 441 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
78320557 167094 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 443 5 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4110578 167094 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 443 5 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
1393 8321 64 None 2 6 Human 8.3 pIC50 = 8.3 Functional
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm4000165
1396 8321 64 None 2 6 Human 8.3 pIC50 = 8.3 Functional
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm4000165
213056 8321 64 None 2 6 Human 8.3 pIC50 = 8.3 Functional
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm4000165
CHEMBL8759 8321 64 None 2 6 Human 8.3 pIC50 = 8.3 Functional
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm4000165
78324634 167081 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4110486 167081 0 None - 1 Human 8.3 pIC50 = 8.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636363 166819 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 2 0 4 5.9 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108148 166819 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 2 0 4 5.9 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354342 166999 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 5.0 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
CHEMBL4109709 166999 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 5.0 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
131636441 166916 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 5 0 5 5.2 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC nan
CHEMBL4109004 166916 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 5 0 5 5.2 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC nan
53320632 63069 0 None - 1 Rat 7.3 pIC50 = 7.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629852 63069 0 None - 1 Rat 7.3 pIC50 = 7.3 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636445 166742 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4107450 166742 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)ccn1 nan
1222 108514 63 None - 1 Human 4.3 pIC50 = 4.3 Functional
Antagonistic activity against mGluR2 was determinedAntagonistic activity against mGluR2 was determined
ChEMBL 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 10.1021/jm960059+
CHEMBL299683 108514 63 None - 1 Human 4.3 pIC50 = 4.3 Functional
Antagonistic activity against mGluR2 was determinedAntagonistic activity against mGluR2 was determined
ChEMBL 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 10.1021/jm960059+
6324634 154722 11 None 6 2 Human 4.3 pIC50 = 4.3 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00352-7
CHEMBL39338 154722 11 None 6 2 Human 4.3 pIC50 = 4.3 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00352-7
44302609 209412 0 None - 1 Human 4.3 pIC50 = 4.3 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 314 4 3 4 1.3 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc3ccccc3c2)C1 10.1016/s0960-894x(98)00352-7
CHEMBL61281 209412 0 None - 1 Human 4.3 pIC50 = 4.3 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 314 4 3 4 1.3 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc3ccccc3c2)C1 10.1016/s0960-894x(98)00352-7
6324634 154722 11 None 6 2 Human 4.3 pIC50 = 4.3 Functional
Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00091-2
CHEMBL39338 154722 11 None 6 2 Human 4.3 pIC50 = 4.3 Functional
Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00091-2
131636364 167640 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 3 0 5 4.0 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F nan
CHEMBL4114951 167640 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 3 0 5 4.0 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F nan
10091203 19723 0 None -2 3 Rat 4.3 pIC50 = 4.3 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1189303 19723 0 None -2 3 Rat 4.3 pIC50 = 4.3 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL538489 19723 0 None -2 3 Rat 4.3 pIC50 = 4.3 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1 10.1016/s0960-894x(01)00329-8
11269030 63078 0 None -1 3 Human 7.3 pIC50 = 7.3 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629861 63078 0 None -1 3 Human 7.3 pIC50 = 7.3 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
10201802 103422 0 None - 1 Rat 7.3 pIC50 = 7.3 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 413 3 1 5 4.4 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL263649 103422 0 None - 1 Rat 7.3 pIC50 = 7.3 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 413 3 1 5 4.4 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
10428048 10134 31 None -3 2 Human 6.3 pIC50 = 6.3 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1039/C3MD00110E
3955 10134 31 None -3 2 Human 6.3 pIC50 = 6.3 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1039/C3MD00110E
CHEMBL305406 10134 31 None -3 2 Human 6.3 pIC50 = 6.3 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1039/C3MD00110E
71566598 149468 15 None -1 3 Rat 7.3 pIC50 = 7.3 Functional
Negative allosteric modulation of rat mGluR2 by GTPgammaS binding assayNegative allosteric modulation of rat mGluR2 by GTPgammaS binding assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3892073 149468 15 None -1 3 Rat 7.3 pIC50 = 7.3 Functional
Negative allosteric modulation of rat mGluR2 by GTPgammaS binding assayNegative allosteric modulation of rat mGluR2 by GTPgammaS binding assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
131636332 158070 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3960577 158070 0 None - 1 Human 7.3 pIC50 = 7.3 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
155545491 180160 0 None - 1 Rat 6.3 pIC50 = 6.3 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 399 4 1 5 3.8 C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
CHEMBL4527834 180160 0 None - 1 Rat 6.3 pIC50 = 6.3 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 399 4 1 5 3.8 C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
155545491 180160 0 None - 1 Rat 6.3 pIC50 = 6.3 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 399 4 1 5 3.8 C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
CHEMBL4527834 180160 0 None - 1 Rat 6.3 pIC50 = 6.3 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 399 4 1 5 3.8 C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
137634033 163420 0 None -1 2 Human 5.3 pIC50 = 5.3 Functional
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4069251 163420 0 None -1 2 Human 5.3 pIC50 = 5.3 Functional
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
90643964 118773 0 None -1 2 Rat 6.3 pIC50 = 6.3 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 386 2 0 5 4.6 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(Cl)c3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288656 118773 0 None -1 2 Rat 6.3 pIC50 = 6.3 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 386 2 0 5 4.6 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(Cl)c3)cc12 10.1016/j.bmcl.2014.04.051
131636436 160341 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3980239 160341 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
155554668 181382 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 394 5 1 6 3.9 Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4557272 181382 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 394 5 1 6 3.9 Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
155554668 181382 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 394 5 1 6 3.9 Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4557272 181382 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 394 5 1 6 3.9 Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
131636322 152171 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 5 0 5 4.7 CCCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1F nan
CHEMBL3913916 152171 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 5 0 5 4.7 CCCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1F nan
22317741 63186 0 None - 1 Rat 8.2 pIC50 = 8.2 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631863 63186 0 None - 1 Rat 8.2 pIC50 = 8.2 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
22317620 63192 0 None - 1 Rat 8.2 pIC50 = 8.2 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 4 1 4 5.7 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631869 63192 0 None - 1 Rat 8.2 pIC50 = 8.2 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 4 1 4 5.7 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL5076351 221209 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay
ChEMBL None None None CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1 10.1021/acs.jmedchem.1c02004
90355554 166709 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 5 5.2 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl nan
CHEMBL4107197 166709 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 5 5.2 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl nan
131636428 167684 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 6 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1 nan
CHEMBL4115246 167684 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 6 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1 nan
131636307 166712 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4107211 166712 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
67637415 190466 0 None 2 2 Human 8.2 pIC50 = 8.2 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4759992 190466 0 None 2 2 Human 8.2 pIC50 = 8.2 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4803099 190466 0 None 2 2 Human 8.2 pIC50 = 8.2 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
131636377 166672 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 0 6 5.1 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
CHEMBL4106932 166672 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 0 6 5.1 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
117821319 125596 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 431 2 0 5 4.7 C[C@H]1CN(c2ccc(C(F)(F)F)c(Cl)c2)C(=O)c2c(-c3ccnc(C#N)c3)cnn21 10.1021/ml5005365
CHEMBL3421840 125596 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 431 2 0 5 4.7 C[C@H]1CN(c2ccc(C(F)(F)F)c(Cl)c2)C(=O)c2c(-c3ccnc(C#N)c3)cnn21 10.1021/ml5005365
131636438 158003 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OCC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3960039 158003 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OCC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
44309100 109408 0 None - 1 Rat 5.2 pIC50 = 5.2 Functional
Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding
ChEMBL 297 4 0 4 4.0 CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl 10.1016/j.bmcl.2007.10.026
CHEMBL304285 109408 0 None - 1 Rat 5.2 pIC50 = 5.2 Functional
Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding
ChEMBL 297 4 0 4 4.0 CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl 10.1016/j.bmcl.2007.10.026
131636340 151542 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 407 3 0 5 4.5 Cc1cc(-c2nc(-c3ccnc(F)c3)c3n2CCOCC3)ccc1OC(F)(F)F nan
CHEMBL3909077 151542 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 407 3 0 5 4.5 Cc1cc(-c2nc(-c3ccnc(F)c3)c3n2CCOCC3)ccc1OC(F)(F)F nan
44302930 107490 0 None - 1 Human 4.2 pIC50 = 4.2 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 278 5 3 4 0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CCc2ccccc2)C1 10.1016/s0960-894x(98)00352-7
CHEMBL292553 107490 0 None - 1 Human 4.2 pIC50 = 4.2 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 278 5 3 4 0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CCc2ccccc2)C1 10.1016/s0960-894x(98)00352-7
52944782 23719 0 None - 1 Human 4.2 pIC50 = 4.2 Functional
Antagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP levelAntagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP level
ChEMBL 241 4 3 3 0.9 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1C1CCCCC1 10.1016/j.bmc.2010.06.051
CHEMBL1253502 23719 0 None - 1 Human 4.2 pIC50 = 4.2 Functional
Antagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP levelAntagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP level
ChEMBL 241 4 3 3 0.9 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1C1CCCCC1 10.1016/j.bmc.2010.06.051
19702198 168101 16 None 1 2 Rat 4.2 pIC50 = 4.2 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O 10.1016/s0960-894x(01)00329-8
CHEMBL412445 168101 16 None 1 2 Rat 4.2 pIC50 = 4.2 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O 10.1016/s0960-894x(01)00329-8
131636335 160048 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3977681 160048 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCOCC3)cc(C)n1 nan
131636278 154245 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C nan
CHEMBL3930304 154245 0 None - 1 Human 7.2 pIC50 = 7.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C nan
10607617 85511 0 None -2 2 Human 5.2 pIC50 = 5.2 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 187 4 3 3 -0.1 CCC(N)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112579 85511 0 None -2 2 Human 5.2 pIC50 = 5.2 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 187 4 3 3 -0.1 CCC(N)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
134155683 158140 0 None 1 2 Human 7.2 pIC50 = 7.2 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 377 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
CHEMBL3961306 158140 0 None 1 2 Human 7.2 pIC50 = 7.2 Functional
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 377 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
155553540 180958 0 None - 1 Rat 5.2 pIC50 = 5.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 355 4 1 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4547431 180958 0 None - 1 Rat 5.2 pIC50 = 5.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 355 4 1 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
155553540 180958 0 None - 1 Rat 5.2 pIC50 = 5.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 355 4 1 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4547431 180958 0 None - 1 Rat 5.2 pIC50 = 5.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 355 4 1 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
155551226 180761 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4541942 180761 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
155559283 181637 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 380 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4563286 181637 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 380 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1 10.1021/acs.jmedchem.8b01266
155551226 180761 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4541942 180761 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
155559283 181637 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 380 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4563286 181637 0 None - 1 Rat 6.2 pIC50 = 6.2 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 380 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1 10.1021/acs.jmedchem.8b01266
11304010 63081 0 None -2 3 Human 8.2 pIC50 = 8.2 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629864 63081 0 None -2 3 Human 8.2 pIC50 = 8.2 Functional
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
22317892 63077 0 None - 1 Rat 8.2 pIC50 = 8.2 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 477 2 1 3 6.9 Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629860 63077 0 None - 1 Rat 8.2 pIC50 = 8.2 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 477 2 1 3 6.9 Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
22317279 63188 0 None - 1 Rat 8.2 pIC50 = 8.2 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 463 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631865 63188 0 None - 1 Rat 8.2 pIC50 = 8.2 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 463 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636308 167581 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
CHEMBL4114419 167581 0 None - 1 Human 8.2 pIC50 = 8.2 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
90354432 167598 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 1 6 4.4 COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
CHEMBL4114578 167598 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 1 6 4.4 COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
78319943 166690 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4107040 166690 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636404 167118 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4110709 167118 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354881 166870 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4108597 166870 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636327 167421 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 4 0 5 4.5 CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC nan
CHEMBL4113208 167421 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 4 0 5 4.5 CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC nan
1378 9195 54 None -2 14 Human 8.1 pIC50 = 8.1 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
1399 9195 54 None -2 14 Human 8.1 pIC50 = 8.1 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
9819927 9195 54 None -2 14 Human 8.1 pIC50 = 8.1 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
CHEMBL432038 9195 54 None -2 14 Human 8.1 pIC50 = 8.1 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
131636281 167463 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113495 167463 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354538 167141 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 485 5 0 5 5.8 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
CHEMBL4110899 167141 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 485 5 0 5 5.8 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
131636440 167693 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 5 0 5 4.8 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC nan
CHEMBL4115297 167693 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 5 0 5 4.8 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC nan
10979251 96835 0 None -5 3 Human 5.2 pIC50 = 5.2 Functional
Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL2381650 96835 0 None -5 3 Human 5.2 pIC50 = 5.2 Functional
Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
10979251 96835 0 None -5 3 Human 5.2 pIC50 = 5.2 Functional
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
CHEMBL2381650 96835 0 None -5 3 Human 5.2 pIC50 = 5.2 Functional
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
22317408 63067 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629850 63067 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636433 151355 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3907628 151355 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
10297067 103079 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 441 5 2 5 5.4 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL261263 103079 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 441 5 2 5 5.4 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
131636277 158433 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3963950 158433 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
18548910 102709 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 401 3 1 6 3.8 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL259340 102709 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 401 3 1 6 3.8 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
155565564 182349 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 5 1 5 4.8 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1 10.1021/acs.jmedchem.8b01266
CHEMBL4579281 182349 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 5 1 5 4.8 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1 10.1021/acs.jmedchem.8b01266
155565564 182349 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 5 1 5 4.8 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1 10.1021/acs.jmedchem.8b01266
CHEMBL4579281 182349 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 5 1 5 4.8 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1 10.1021/acs.jmedchem.8b01266
18548737 63177 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631854 63177 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
44302819 170015 0 None - 1 Human 4.1 pIC50 = 4.1 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 298 4 3 4 0.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Cl)C1 10.1016/s0960-894x(98)00352-7
CHEMBL418462 170015 0 None - 1 Human 4.1 pIC50 = 4.1 Functional
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 298 4 3 4 0.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Cl)C1 10.1016/s0960-894x(98)00352-7
155564600 182331 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1 10.1021/acs.jmedchem.8b01266
CHEMBL4578758 182331 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1 10.1021/acs.jmedchem.8b01266
155564600 182331 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1 10.1021/acs.jmedchem.8b01266
CHEMBL4578758 182331 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1 10.1021/acs.jmedchem.8b01266
162666357 190510 0 None 3 2 Human 7.1 pIC50 = 7.1 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4784701 190510 0 None 3 2 Human 7.1 pIC50 = 7.1 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803523 190510 0 None 3 2 Human 7.1 pIC50 = 7.1 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
137656301 165461 0 None - 1 Human 5.1 pIC50 = 5.1 Functional
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 324 5 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4093017 165461 0 None - 1 Human 5.1 pIC50 = 5.1 Functional
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 324 5 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
44300389 20431 0 None -1 2 Rat 4.1 pIC50 = 4.1 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 342 4 3 4 0.9 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1194613 20431 0 None -1 2 Rat 4.1 pIC50 = 4.1 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 342 4 3 4 0.9 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1 10.1016/s0960-894x(01)00329-8
CHEMBL552984 20431 0 None -1 2 Rat 4.1 pIC50 = 4.1 Functional
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 342 4 3 4 0.9 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1 10.1016/s0960-894x(01)00329-8
131636292 167305 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 353 2 0 4 4.5 Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4112325 167305 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 353 2 0 4 4.5 Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636439 160607 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OCC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3982561 160607 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OCC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
117821004 125595 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 400 3 0 4 4.9 CCC1CN(c2ccc(C(F)(F)F)cc2)C(=O)c2c(-c3ccnc(C)c3)cnn21 10.1021/ml5005365
CHEMBL3421839 125595 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 400 3 0 4 4.9 CCC1CN(c2ccc(C(F)(F)F)cc2)C(=O)c2c(-c3ccnc(C)c3)cnn21 10.1021/ml5005365
155511336 176318 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 431 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4435396 176318 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 431 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155511336 176318 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 431 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4435396 176318 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 431 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
11235624 63079 0 None -1 3 Rat 8.1 pIC50 = 8.1 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629862 63079 0 None -1 3 Rat 8.1 pIC50 = 8.1 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11442010 63083 0 None -2 3 Rat 8.1 pIC50 = 8.1 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629866 63083 0 None -2 3 Rat 8.1 pIC50 = 8.1 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
25210562 221745 25 None - 1 Human 8.1 pIC50 = 8.1 Functional
Negative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assayNegative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assay
ChEMBL None None None N#Cc1cc(C2=Nc3ccc(Br)cc3NC(=O)C2)ccn1 10.1021/acs.jmedchem.1c02004
CHEMBL5085417 221745 25 None - 1 Human 8.1 pIC50 = 8.1 Functional
Negative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assayNegative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assay
ChEMBL None None None N#Cc1cc(C2=Nc3ccc(Br)cc3NC(=O)C2)ccn1 10.1021/acs.jmedchem.1c02004
131636350 150600 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)ccn1 nan
CHEMBL3901364 150600 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)ccn1 nan
117824335 125594 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 2 0 4 4.5 Cc1cc(-c2cnn3c2C(=O)N(c2ccc(C(F)(F)F)cc2)C[C@@H]3C)ccn1 10.1021/ml5005365
CHEMBL3421838 125594 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 2 0 4 4.5 Cc1cc(-c2cnn3c2C(=O)N(c2ccc(C(F)(F)F)cc2)C[C@@H]3C)ccn1 10.1021/ml5005365
49836087 7847 0 None 16 2 Human 6.1 pIC50 = 6.1 Functional
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
6222 7847 0 None 16 2 Human 6.1 pIC50 = 6.1 Functional
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
CHEMBL1630805 7847 0 None 16 2 Human 6.1 pIC50 = 6.1 Functional
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
3335 9789 4 None 1 2 Human 5.1 pIC50 = 5.1 Functional
Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm960059+
5311344 9789 4 None 1 2 Human 5.1 pIC50 = 5.1 Functional
Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm960059+
CHEMBL39573 9789 4 None 1 2 Human 5.1 pIC50 = 5.1 Functional
Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm960059+
131636449 167197 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 461 5 0 6 5.3 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CCOCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4111376 167197 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 461 5 0 6 5.3 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CCOCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90643970 118777 0 None 1 2 Rat 6.1 pIC50 = 6.1 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 464 3 1 6 3.8 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(Cl)cc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288664 118777 0 None 1 2 Rat 6.1 pIC50 = 6.1 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 464 3 1 6 3.8 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(Cl)cc3)cc12 10.1016/j.bmcl.2014.04.051
10587622 85515 0 None -1 2 Human 6.1 pIC50 = 6.1 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 263 6 3 3 1.1 NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112582 85515 0 None -1 2 Human 6.1 pIC50 = 6.1 Functional
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 263 6 3 3 1.1 NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
10587622 85515 0 None -1 2 Human 6.1 pIC50 = 6.1 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 263 6 3 3 1.1 NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL2112582 85515 0 None -1 2 Human 6.1 pIC50 = 6.1 Functional
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 263 6 3 3 1.1 NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
90643956 118768 0 None -5 2 Rat 6.1 pIC50 = 6.1 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 352 2 0 5 3.9 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288639 118768 0 None -5 2 Rat 6.1 pIC50 = 6.1 Functional
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 352 2 0 5 3.9 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
155564325 182197 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 429 5 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4575990 182197 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 429 5 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155564325 182197 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 429 5 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4575990 182197 0 None - 1 Rat 7.1 pIC50 = 7.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 429 5 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155521127 177329 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 413 5 1 5 4.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4450016 177329 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 413 5 1 5 4.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
155521127 177329 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 413 5 1 5 4.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4450016 177329 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 413 5 1 5 4.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
76332991 112876 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 428 2 1 4 3.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(I)cc2N1 10.1039/C3MD00110E
CHEMBL3133882 112876 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 428 2 1 4 3.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(I)cc2N1 10.1039/C3MD00110E
76322144 112881 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 534 4 1 5 5.6 COc1cc2c(cc1-c1ccc(I)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1039/C3MD00110E
CHEMBL3133887 112881 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 534 4 1 5 5.6 COc1cc2c(cc1-c1ccc(I)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1039/C3MD00110E
155515940 176787 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 397 5 1 5 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4442453 176787 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 397 5 1 5 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
155515940 176787 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 397 5 1 5 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4442453 176787 0 None - 1 Rat 6.1 pIC50 = 6.1 Functional
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 397 5 1 5 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
9888376 101990 1 None - 1 Rat 8.1 pIC50 = 8.1 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL256011 101990 1 None - 1 Rat 8.1 pIC50 = 8.1 Functional
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
18548795 63175 0 None - 1 Rat 8.1 pIC50 = 8.1 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 399 2 1 4 5.4 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1 10.1016/j.bmcl.2010.09.125
CHEMBL1631757 63175 0 None - 1 Rat 8.1 pIC50 = 8.1 Functional
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 399 2 1 4 5.4 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1 10.1016/j.bmcl.2010.09.125
131636414 167033 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 483 7 0 6 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
CHEMBL4110033 167033 0 None - 1 Human 8.1 pIC50 = 8.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 483 7 0 6 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
131636334 156934 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3951588 156934 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
131636352 167214 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F nan
CHEMBL4111531 167214 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F nan
131636387 167699 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 453 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4115328 167699 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 453 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636371 166919 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 6 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
CHEMBL4109036 166919 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 6 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
131636452 167449 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 439 4 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC4COC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113408 167449 0 None - 1 Human 8.0 pIC50 = 8.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 439 4 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC4COC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
67633284 190426 0 None 5 2 Human 8.0 pIC50 = 8.0 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4748699 190426 0 None 5 2 Human 8.0 pIC50 = 8.0 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802655 190426 0 None 5 2 Human 8.0 pIC50 = 8.0 Functional
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
131636275 149639 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 5 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)ccn1 nan
CHEMBL3893337 149639 0 None - 1 Human 7.1 pIC50 = 7.1 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 5 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)ccn1 nan
76322143 112879 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 400 3 1 5 4.4 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1039/C3MD00110E
CHEMBL3133885 112879 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 400 3 1 5 4.4 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1039/C3MD00110E
131636330 155247 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.6 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3938055 155247 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.6 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL5089623 221996 2 None - 1 Human 7.0 pIC50 = 7.0 Functional
Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay
ChEMBL None None None COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1 10.1021/acs.jmedchem.1c02004
CHEMBL5089623 221996 2 None - 1 Human 7.0 pIC50 = 7.0 Functional
Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay
ChEMBL None None None COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1 10.1021/acs.jmedchem.1c02004
131636318 150372 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.6 Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3899445 150372 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.6 Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
131636288 167603 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 3 0 5 4.3 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1F nan
CHEMBL4114600 167603 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 3 0 5 4.3 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1F nan
90354465 155024 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OCC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3936284 155024 0 None - 1 Human 7.0 pIC50 = 7.0 Functional
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OCC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
44322537 213432 0 None - 0 Human 6.0 pKi = 6 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 517 7 0 7 6.2 CCC1=C(C(=O)OCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1021/jm000007r
CHEMBL89293 213432 0 None - 0 Human 6.0 pKi = 6 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 517 7 0 7 6.2 CCC1=C(C(=O)OCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1021/jm000007r
1393 8321 64 None 2 6 Human 8.0 pKi = 8.0 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000007r
1396 8321 64 None 2 6 Human 8.0 pKi = 8.0 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000007r
213056 8321 64 None 2 6 Human 8.0 pKi = 8.0 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000007r
CHEMBL8759 8321 64 None 2 6 Human 8.0 pKi = 8.0 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000007r
10428048 10134 31 None -3 2 Human 7.0 pKi = 7.0 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1021/jm000007r
3955 10134 31 None -3 2 Human 7.0 pKi = 7.0 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1021/jm000007r
CHEMBL305406 10134 31 None -3 2 Human 7.0 pKi = 7.0 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1021/jm000007r
44322840 119348 0 None - 0 Human 7.0 pKi = 7.0 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 201 2 4 4 -1.5 N[C@]1(C(=O)O)C2C(C[C@H]1O)[C@@H]2C(=O)O 10.1021/jm000007r
CHEMBL330097 119348 0 None - 0 Human 7.0 pKi = 7.0 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 201 2 4 4 -1.5 N[C@]1(C(=O)O)C2C(C[C@H]1O)[C@@H]2C(=O)O 10.1021/jm000007r
1415 9392 41 None - 2 Human 5.0 pKi = 5.0 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 245 3 4 3 -0.3 OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C 10.1021/jm000007r
3972752 9392 41 None - 2 Human 5.0 pKi = 5.0 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 245 3 4 3 -0.3 OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C 10.1021/jm000007r
CHEMBL86508 9392 41 None - 2 Human 5.0 pKi = 5.0 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 245 3 4 3 -0.3 OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C 10.1021/jm000007r
1310 9095 110 None -389 17 Human 4.9 pKi = 4.9 Functional
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
1369 9095 110 None -389 17 Human 4.9 pKi = 4.9 Functional
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
33032 9095 110 None -389 17 Human 4.9 pKi = 4.9 Functional
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
44272391 9095 110 None -389 17 Human 4.9 pKi = 4.9 Functional
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
88747398 9095 110 None -389 17 Human 4.9 pKi = 4.9 Functional
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
CHEMBL575060 9095 110 None -389 17 Human 4.9 pKi = 4.9 Functional
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
DB00142 9095 110 None -389 17 Human 4.9 pKi = 4.9 Functional
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
10359073 161753 1 None -1 2 Human 4.8 pKi = 4.8 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL40123 161753 1 None -1 2 Human 4.8 pKi = 4.8 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm000007r
10197984 9199 44 None 1 5 Human 8.6 pKi = 8.6 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm000007r
1394 9199 44 None 1 5 Human 8.6 pKi = 8.6 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm000007r
CHEMBL275079 9199 44 None 1 5 Human 8.6 pKi = 8.6 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm000007r
3246152 168071 31 None - 0 Human 5.7 pKi = 5.7 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 161 4 3 3 -0.5 C[C@@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL41221 168071 31 None - 0 Human 5.7 pKi = 5.7 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 161 4 3 3 -0.5 C[C@@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/jm000007r
1297 177031 36 None -1 2 Human 4.7 pKi = 4.7 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 10.1021/jm000007r
CHEMBL444589 177031 36 None -1 2 Human 4.7 pKi = 4.7 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 10.1021/jm000007r
1378 9195 54 None -2 14 Human 7.7 pKi = 7.7 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm000007r
1399 9195 54 None -2 14 Human 7.7 pKi = 7.7 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm000007r
9819927 9195 54 None -2 14 Human 7.7 pKi = 7.7 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm000007r
CHEMBL432038 9195 54 None -2 14 Human 7.7 pKi = 7.7 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm000007r
439282 148362 8 None - 0 Human 6.6 pKi = 6.6 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 159 4 3 3 -0.6 C=C(C[C@H](N)C(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL38499 148362 8 None - 0 Human 6.6 pKi = 6.6 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 159 4 3 3 -0.6 C=C(C[C@H](N)C(=O)O)C(=O)O 10.1021/jm000007r
11820180 24834 1 None - 0 Human 4.6 pKi = 4.6 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 203 4 3 6 -2.1 N[C@@H](CCn1oc(=O)[nH]c1=O)C(=O)O 10.1021/jm000007r
CHEMBL126608 24834 1 None - 0 Human 4.6 pKi = 4.6 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 203 4 3 6 -2.1 N[C@@H](CCn1oc(=O)[nH]c1=O)C(=O)O 10.1021/jm000007r
10058694 213382 1 None - 0 Human 8.4 pKi = 8.4 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CSC2C1[C@H]2C(=O)O 10.1021/jm000007r
CHEMBL88999 213382 1 None - 0 Human 8.4 pKi = 8.4 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CSC2C1[C@H]2C(=O)O 10.1021/jm000007r
4694355 105515 36 None - 1 Human 4.5 pKi = 4.5 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 257 2 4 3 -0.3 NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21 10.1021/jm000007r
CHEMBL277961 105515 36 None - 1 Human 4.5 pKi = 4.5 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 257 2 4 3 -0.3 NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21 10.1021/jm000007r
16739377 98951 0 None - 0 Rat 4.5 pKi = 4.5 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 253 4 3 5 1.3 NC(C(=O)O)c1cnn(O)c1CC1CCCCC1 10.1016/j.bmc.2007.02.047
CHEMBL242344 98951 0 None - 0 Rat 4.5 pKi = 4.5 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 253 4 3 5 1.3 NC(C(=O)O)c1cnn(O)c1CC1CCCCC1 10.1016/j.bmc.2007.02.047
16739377 98951 0 None - 0 Rat 4.5 pKi = 4.5 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 253 4 3 5 1.3 NC(C(=O)O)c1cnn(O)c1CC1CCCCC1 10.1016/j.bmc.2007.02.047
CHEMBL242344 98951 0 None - 0 Rat 4.5 pKi = 4.5 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 253 4 3 5 1.3 NC(C(=O)O)c1cnn(O)c1CC1CCCCC1 10.1016/j.bmc.2007.02.047
44322921 213616 1 None - 0 Human 6.5 pKi = 6.5 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)CC2CC1[C@H]2C(=O)O 10.1021/jm000007r
CHEMBL90501 213616 1 None - 0 Human 6.5 pKi = 6.5 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)CC2CC1[C@H]2C(=O)O 10.1021/jm000007r
59066632 213349 89 None 1 2 Human 4.5 pKi = 4.5 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm000007r
92136 213349 89 None 1 2 Human 4.5 pKi = 4.5 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL88804 213349 89 None 1 2 Human 4.5 pKi = 4.5 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm000007r
44322745 112943 0 None - 0 Human 4.4 pKi = 4.4 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 203 3 3 6 -2.1 C[C@](N)(Cn1c(=O)[nH]oc1=O)C(=O)O 10.1021/jm000007r
CHEMBL313713 112943 0 None - 0 Human 4.4 pKi = 4.4 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 203 3 3 6 -2.1 C[C@](N)(Cn1c(=O)[nH]oc1=O)C(=O)O 10.1021/jm000007r
1392 6861 48 None - 4 Human 6.4 pKi = 6.4 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
5310984 6861 48 None - 4 Human 6.4 pKi = 6.4 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
CHEMBL40086 6861 48 None - 4 Human 6.4 pKi = 6.4 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
10330132 108159 1 None - 2 Human 5.3 pKi = 5.3 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 189 2 4 5 -2.2 NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1021/jm000007r
CHEMBL297150 108159 1 None - 2 Human 5.3 pKi = 5.3 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 189 2 4 5 -2.2 NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1021/jm000007r
1368 9070 37 None 1 11 Human 6.3 pKi = 6.3 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm000007r
5310956 9070 37 None 1 11 Human 6.3 pKi = 6.3 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL280563 9070 37 None 1 11 Human 6.3 pKi = 6.3 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm000007r
104766 6822 42 None -2 14 Human 5.3 pKi = 5.3 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
1365 6822 42 None -2 14 Human 5.3 pKi = 5.3 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
CHEMBL34453 6822 42 None -2 14 Human 5.3 pKi = 5.3 Functional
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
6324634 154722 11 None 6 2 Human 4.3 pKi = 4.3 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL39338 154722 11 None 6 2 Human 4.3 pKi = 4.3 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm000007r
1222 108514 63 None - 1 Human 4.3 pKi = 4.3 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 10.1021/jm000007r
CHEMBL299683 108514 63 None - 1 Human 4.3 pKi = 4.3 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 10.1021/jm000007r
10198359 80733 9 None -10 4 Human 4.3 pKi = 4.3 Functional
Partial agonist potency against cloned Metabotropic glutamate receptor 2Partial agonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 221 3 3 3 -0.8 N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O 10.1021/jm000007r
CHEMBL2021372 80733 9 None -10 4 Human 4.3 pKi = 4.3 Functional
Partial agonist potency against cloned Metabotropic glutamate receptor 2Partial agonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 221 3 3 3 -0.8 N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O 10.1021/jm000007r
44428738 175529 0 None - 0 Rat 4.2 pKi = 4.2 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 275 6 3 5 1.4 NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1 10.1016/j.bmc.2007.02.047
CHEMBL437169 175529 0 None - 0 Rat 4.2 pKi = 4.2 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 275 6 3 5 1.4 NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1 10.1016/j.bmc.2007.02.047
44428738 175529 0 None - 0 Rat 4.2 pKi = 4.2 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 275 6 3 5 1.4 NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1 10.1016/j.bmc.2007.02.047
CHEMBL437169 175529 0 None - 0 Rat 4.2 pKi = 4.2 Functional
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 275 6 3 5 1.4 NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1 10.1016/j.bmc.2007.02.047
44322529 213645 1 None - 0 Human 7.1 pKi = 7.1 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1021/jm000007r
CHEMBL90675 213645 1 None - 0 Human 7.1 pKi = 7.1 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1021/jm000007r
1439 9247 15 None - 1 Human 4.1 pKi = 4.1 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm000007r
5311457 9247 15 None - 1 Human 4.1 pKi = 4.1 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm000007r
CHEMBL41013 9247 15 None - 1 Human 4.1 pKi = 4.1 Functional
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm000007r
1310 9095 110 None -457 17 Rat 8.3 pEC50 = 8.3 Functional
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 9095 110 None -457 17 Rat 8.3 pEC50 = 8.3 Functional
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 9095 110 None -457 17 Rat 8.3 pEC50 = 8.3 Functional
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 9095 110 None -457 17 Rat 8.3 pEC50 = 8.3 Functional
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 9095 110 None -457 17 Rat 8.3 pEC50 = 8.3 Functional
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 9095 110 None -457 17 Rat 8.3 pEC50 = 8.3 Functional
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 9095 110 None -457 17 Rat 8.3 pEC50 = 8.3 Functional
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1310 9095 110 None -389 17 Human 8.2 pEC50 = 8.2 Functional
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 9095 110 None -389 17 Human 8.2 pEC50 = 8.2 Functional
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 9095 110 None -389 17 Human 8.2 pEC50 = 8.2 Functional
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 9095 110 None -389 17 Human 8.2 pEC50 = 8.2 Functional
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 9095 110 None -389 17 Human 8.2 pEC50 = 8.2 Functional
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 9095 110 None -389 17 Human 8.2 pEC50 = 8.2 Functional
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 9095 110 None -389 17 Human 8.2 pEC50 = 8.2 Functional
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
25195461 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Functional
Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.
Guide to Pharmacology 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 25692015
8946 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Functional
Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.
Guide to Pharmacology 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 25692015
CHEMBL3337527 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Functional
Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.
Guide to Pharmacology 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 25692015
DB12059 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Functional
Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.
Guide to Pharmacology 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 25692015
1310 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
1369 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
33032 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
44272391 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
88747398 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
CHEMBL575060 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
DB00142 9095 110 None -389 17 Human 5.1 pEC50 = 5.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
11281345 6901 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 411 8 1 5 3.3 CCS(=O)(=O)N(c1ccc(cc1)Oc1ccc(cc1)C(=O)N)Cc1cccnc1 15717213
6258 6901 0 None - 1 Human 5.7 pEC50 = 5.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 411 8 1 5 3.3 CCS(=O)(=O)N(c1ccc(cc1)Oc1ccc(cc1)C(=O)N)Cc1cccnc1 15717213
25002940 7890 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 22364337
6320 7890 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 22364337
CHEMBL2029821 7890 0 None - 1 Human 6.4 pEC50 = 6.4 Functional
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 22364337
25125217 7343 25 None - 1 Human 6.7 pEC50 = 6.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 None
7678 7343 25 None - 1 Human 6.7 pEC50 = 6.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 None
CHEMBL3937907 7343 25 None - 1 Human 6.7 pEC50 = 6.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 None
DB16073 7343 25 None - 1 Human 6.7 pEC50 = 6.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 None
46182736 7776 0 None - 1 Rat 6.8 pEC50 = 6.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 21155570
6323 7776 0 None - 1 Rat 6.8 pEC50 = 6.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 21155570
CHEMBL1651219 7776 0 None - 1 Rat 6.8 pEC50 = 6.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 21155570
46190878 8653 7 None - 1 Human 6.9 pEC50 = 6.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 20005096
6253 8653 7 None - 1 Human 6.9 pEC50 = 6.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 20005096
CHEMBL595759 8653 7 None - 1 Human 6.9 pEC50 = 6.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 20005096
3954 7451 60 None 6 2 Human 7.0 pEC50 = 7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 16046122
9868580 7451 60 None 6 2 Human 7.0 pEC50 = 7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 16046122
CHEMBL593013 7451 60 None 6 2 Human 7.0 pEC50 = 7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 16046122
3372 7600 0 None - 1 Human 7.0 pEC50 = 7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 4 4.0 N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1 15717213
9864510 7600 0 None - 1 Human 7.0 pEC50 = 7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 4 4.0 N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1 15717213
CHEMBL4303163 7600 0 None - 1 Human 7.0 pEC50 = 7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 4 4.0 N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1 15717213
46830123 7859 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 20409708
6321 7859 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 20409708
CHEMBL1094763 7859 0 None - 1 Human 7.1 pEC50 = 7.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 20409708
46190877 8652 7 None - 1 Human 7.1 pEC50 = 7.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 20005096
6252 8652 7 None - 1 Human 7.1 pEC50 = 7.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 20005096
CHEMBL605836 8652 7 None - 1 Human 7.1 pEC50 = 7.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 20005096
6256 7796 0 None - 1 Rat 7.2 pEC50 = 7.2 Functional
UnclassifiedUnclassified
Guide to Pharmacology 382 6 0 5 3.5 Clc1cccc(c1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccn2 18812259
73755202 7796 0 None - 1 Rat 7.2 pEC50 = 7.2 Functional
UnclassifiedUnclassified
Guide to Pharmacology 382 6 0 5 3.5 Clc1cccc(c1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccn2 18812259
59234231 8924 4 None 1 2 Rat 7.3 pEC50 = 7.3 Functional
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6330 8924 4 None 1 2 Rat 7.3 pEC50 = 7.3 Functional
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6331 8924 4 None 1 2 Rat 7.3 pEC50 = 7.3 Functional
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
CHEMBL3337510 8924 4 None 1 2 Rat 7.3 pEC50 = 7.3 Functional
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
59234231 8924 4 None -1 2 Human 7.3 pEC50 = 7.3 Functional
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6330 8924 4 None -1 2 Human 7.3 pEC50 = 7.3 Functional
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6331 8924 4 None -1 2 Human 7.3 pEC50 = 7.3 Functional
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
CHEMBL3337510 8924 4 None -1 2 Human 7.3 pEC50 = 7.3 Functional
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6255 7774 0 None - 1 Rat 7.5 pEC50 = 7.5 Functional
UnclassifiedUnclassified
Guide to Pharmacology 416 6 0 5 3.9 Cn1c(CN2C[C@@H]3[C@H](C2)[C@H]3COCc2ccc(cn2)C(F)(F)F)nc2c1cccc2 18812259
73755201 7774 0 None - 1 Rat 7.5 pEC50 = 7.5 Functional
UnclassifiedUnclassified
Guide to Pharmacology 416 6 0 5 3.9 Cn1c(CN2C[C@@H]3[C@H](C2)[C@H]3COCc2ccc(cn2)C(F)(F)F)nc2c1cccc2 18812259
6254 7772 0 None - 1 Rat 7.6 pEC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 382 6 0 5 3.5 Clc1ccc(nc1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccc2 18812259
73755200 7772 0 None - 1 Rat 7.6 pEC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 382 6 0 5 3.5 Clc1ccc(nc1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccc2 18812259
44335556 8082 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 15717213
6257 8082 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 15717213
CHEMBL321968 8082 0 None - 1 Human 7.6 pEC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 15717213
44595851 10574 4 None -3 2 Human 7.7 pEC50 = 7.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
6259 10574 4 None -3 2 Human 7.7 pEC50 = 7.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
CHEMBL4092105 10574 4 None -3 2 Human 7.7 pEC50 = 7.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
49765871 8926 45 None - 1 Human 7.8 pEC50 = 7.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
6317 8926 45 None - 1 Human 7.8 pEC50 = 7.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
CHEMBL2179319 8926 45 None - 1 Human 7.8 pEC50 = 7.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
11362035 6831 1 None - 1 Human 7.9 pEC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 15149652
6328 6831 1 None - 1 Human 7.9 pEC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 15149652
6329 6831 1 None - 1 Human 7.9 pEC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 15149652
CHEMBL105296 6831 1 None - 1 Human 7.9 pEC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 15149652
44595851 10574 4 None 3 2 Rat 7.9 pEC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
6259 10574 4 None 3 2 Rat 7.9 pEC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
CHEMBL4092105 10574 4 None 3 2 Rat 7.9 pEC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
3335 9789 4 None -1 2 Rat 5.1 pIC50 = 5.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 8667369
5311344 9789 4 None -1 2 Rat 5.1 pIC50 = 5.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 8667369
CHEMBL39573 9789 4 None -1 2 Rat 5.1 pIC50 = 5.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 8667369
1402 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 12852748
1402 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 14500736
1402 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15149652
1402 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15717213
9825084 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 12852748
9825084 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 14500736
9825084 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15149652
9825084 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15717213
CHEMBL108939 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 12852748
CHEMBL108939 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 14500736
CHEMBL108939 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15149652
CHEMBL108939 6910 44 None - 1 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15717213
49858117 7875 4 None 5 2 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
6223 7875 4 None 5 2 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
CHEMBL1630806 7875 4 None 5 2 Human 5.8 pIC50 = 5.8 Functional
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
49858118 7894 0 None 10 2 Human 6.0 pIC50 = 6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
6224 7894 0 None 10 2 Human 6.0 pIC50 = 6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
CHEMBL1630807 7894 0 None 10 2 Human 6.0 pIC50 = 6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
49836087 7847 0 None 16 2 Human 6.1 pIC50 = 6.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
6222 7847 0 None 16 2 Human 6.1 pIC50 = 6.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
CHEMBL1630805 7847 0 None 16 2 Human 6.1 pIC50 = 6.1 Functional
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
10428048 10134 31 None 3 2 Rat 7.0 pIC50 = 7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10465539
3955 10134 31 None 3 2 Rat 7.0 pIC50 = 7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10465539
CHEMBL305406 10134 31 None 3 2 Rat 7.0 pIC50 = 7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10465539
6219 9363 0 None -1 3 Human 7.5 pIC50 = 7.5 Functional
UnclassifiedUnclassified
Guide to Pharmacology 401 1 1 3 4.0 N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I 17416742
73755191 9363 0 None -1 3 Human 7.5 pIC50 = 7.5 Functional
UnclassifiedUnclassified
Guide to Pharmacology 401 1 1 3 4.0 N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I 17416742
6221 9365 0 None -2 3 Human 7.5 pIC50 = 7.5 Functional
UnclassifiedUnclassified
Guide to Pharmacology 354 1 1 4 3.6 N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br 17416742
73755193 9365 0 None -2 3 Human 7.5 pIC50 = 7.5 Functional
UnclassifiedUnclassified
Guide to Pharmacology 354 1 1 4 3.6 N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br 17416742
11158623 10124 11 None 1 4 Rat 7.6 pIC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
11158623 10124 11 None 1 4 Rat 7.6 pIC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
6226 10124 11 None 1 4 Rat 7.6 pIC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
6226 10124 11 None 1 4 Rat 7.6 pIC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
CHEMBL1629855 10124 11 None 1 4 Rat 7.6 pIC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
CHEMBL1629855 10124 11 None 1 4 Rat 7.6 pIC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
6219 9363 0 None 1 3 Rat 7.6 pIC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 401 1 1 3 4.0 N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I 17416742
73755191 9363 0 None 1 3 Rat 7.6 pIC50 = 7.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 401 1 1 3 4.0 N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I 17416742
6220 9364 0 None -1 3 Rat 7.7 pIC50 = 7.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 405 2 1 3 5.4 O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1 17416742
73755192 9364 0 None -1 3 Rat 7.7 pIC50 = 7.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 405 2 1 3 5.4 O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1 17416742
6220 9364 0 None 1 3 Human 7.7 pIC50 = 7.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 405 2 1 3 5.4 O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1 17416742
73755192 9364 0 None 1 3 Human 7.7 pIC50 = 7.7 Functional
UnclassifiedUnclassified
Guide to Pharmacology 405 2 1 3 5.4 O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1 17416742
11158623 10124 11 None -7 4 Human 7.9 pIC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
6226 10124 11 None -7 4 Human 7.9 pIC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
CHEMBL1629855 10124 11 None -7 4 Human 7.9 pIC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
6221 9365 0 None 1 3 Rat 7.9 pIC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 354 1 1 4 3.6 N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br 17416742
73755193 9365 0 None 1 3 Rat 7.9 pIC50 = 7.9 Functional
UnclassifiedUnclassified
Guide to Pharmacology 354 1 1 4 3.6 N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br 17416742
6324 10126 0 None - 1 Rat 8.3 pIC50 = 8.3 Functional
UnclassifiedUnclassified
Guide to Pharmacology 512 2 1 6 4.5 FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F 21470207
73755205 10126 0 None - 1 Rat 8.3 pIC50 = 8.3 Functional
UnclassifiedUnclassified
Guide to Pharmacology 512 2 1 6 4.5 FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F 21470207
10047169 9998 1 None - 1 Human 6.5 pIC50 None 6.5 Functional
UnclassifiedUnclassified
Guide to Pharmacology 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 15317469
1403 9998 1 None - 1 Human 6.5 pIC50 None 6.5 Functional
UnclassifiedUnclassified
Guide to Pharmacology 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 15317469
CHEMBL182371 9998 1 None - 1 Human 6.5 pIC50 None 6.5 Functional
UnclassifiedUnclassified
Guide to Pharmacology 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 15317469
10275802 6895 0 None - 1 Human 6.6 pIC50 None 6.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 12852748
10275802 6895 0 None - 1 Human 6.6 pIC50 None 6.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 14500736
10275802 6895 0 None - 1 Human 6.6 pIC50 None 6.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15717213
1401 6895 0 None - 1 Human 6.6 pIC50 None 6.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 12852748
1401 6895 0 None - 1 Human 6.6 pIC50 None 6.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 14500736
1401 6895 0 None - 1 Human 6.6 pIC50 None 6.6 Functional
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15717213


Get vendors


Ligands (move mouse cursor over ligand name to see structure) Receptor Assay information Chemical information
Sel. page Similar-
ity		 Common
name		 GPCRdb
ID		 #Vendors

 Reference
ligand		 Fold
selectivity		 # Tested
GPCRs		 Species

 p-value
(-log)		 Activity
Type		 Activity
Relation		 Activity
Value		 Assay
Type		 Assay
Description		 Source

 Mol
weight		 Rot
Bonds		 H don

 H acc

 LogP

 Smiles

 DOI
9794208 96825 4 None - 0 Human 9.8 pEC50 = 9.8 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 4 -1.3 N[C@@]1(C(=O)O)CC(=O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
CHEMBL2381640 96825 4 None - 0 Human 9.8 pEC50 = 9.8 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 4 -1.3 N[C@@]1(C(=O)O)CC(=O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
139119037 96837 2 None - 0 Human 9.3 pEC50 = 9.3 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
15479143 96837 2 None - 0 Human 9.3 pEC50 = 9.3 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
CHEMBL2381652 96837 2 None - 0 Human 9.3 pEC50 = 9.3 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
70051926 96826 2 None - 0 Human 8.9 pEC50 = 8.9 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 197 2 3 3 -0.3 C=C1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
CHEMBL2381641 96826 2 None - 0 Human 8.9 pEC50 = 8.9 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 197 2 3 3 -0.3 C=C1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
44335501 116434 0 None - 0 Human 7.0 pEC50 = 7 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 428 7 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL322465 116434 0 None - 0 Human 7.0 pEC50 = 7 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 428 7 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
50993966 64105 0 None - 0 Rat 7.0 pEC50 = 7 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 449 7 1 3 5.9 CC(C)CN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
CHEMBL1651212 64105 0 None - 0 Rat 7.0 pEC50 = 7 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 449 7 1 3 5.9 CC(C)CN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
24815976 206538 0 None - 3 Human 7.0 pEC50 = 7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593745 206538 0 None - 3 Human 7.0 pEC50 = 7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
24815883 208241 0 None - 2 Human 7.0 pEC50 = 7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL604993 208241 0 None - 2 Human 7.0 pEC50 = 7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225581 208766 0 None - 3 Human 7.0 pEC50 = 7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL608103 208766 0 None - 3 Human 7.0 pEC50 = 7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
11768848 122030 11 None - 1 Human 5.0 pEC50 = 5 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@H]1CC(=O)O 10.1039/C1MD00186H
CHEMBL3347671 122030 11 None - 1 Human 5.0 pEC50 = 5 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@H]1CC(=O)O 10.1039/C1MD00186H
10198359 80733 9 None - 1 Human 5.0 pEC50 = 5 Binding
Concentration required to inhibit mGluR2 receptorConcentration required to inhibit mGluR2 receptor
ChEMBL 221 3 3 3 -0.8 N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O 10.1016/s0960-894x(98)00265-0
CHEMBL2021372 80733 9 None - 1 Human 5.0 pEC50 = 5 Binding
Concentration required to inhibit mGluR2 receptorConcentration required to inhibit mGluR2 receptor
ChEMBL 221 3 3 3 -0.8 N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O 10.1016/s0960-894x(98)00265-0
90643871 118641 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 418 11 2 5 5.0 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287693 118641 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 418 11 2 5 5.0 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
164617451 191731 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 11 2 6 5.3 COc1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc(C(=O)O)c1 10.1016/j.bmcl.2021.128342
CHEMBL4853794 191731 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 11 2 6 5.3 COc1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc(C(=O)O)c1 10.1016/j.bmcl.2021.128342
90643884 118667 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 12 2 6 4.6 CCCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O 10.1021/jm5000563
CHEMBL3287719 118667 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 12 2 6 4.6 CCCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O 10.1021/jm5000563
89735528 144775 0 None - 0 Human 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1cccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1 10.1016/j.bmcl.2016.01.021
CHEMBL3764544 144775 0 None - 0 Human 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1cccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1 10.1016/j.bmcl.2016.01.021
90643857 118670 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 CCCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287722 118670 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 CCCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
10050046 72847 0 None - 0 Human 6.0 pEC50 = 6.0 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 463 12 2 7 3.5 CCCc1c(OCCCCOc2ccc(C(=O)NS(C)(=O)=O)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL183756 72847 0 None - 0 Human 6.0 pEC50 = 6.0 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 463 12 2 7 3.5 CCCc1c(OCCCCOc2ccc(C(=O)NS(C)(=O)=O)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
11656255 130089 0 None - 0 Human 6.0 pEC50 = 6.0 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 498 8 1 5 6.9 CCCCC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL361570 130089 0 None - 0 Human 6.0 pEC50 = 6.0 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 498 8 1 5 6.9 CCCCC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
90643896 118652 0 None - 0 Rat 6.0 pEC50 = 6.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 388 10 2 6 3.8 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(C)=O)c(O)c1C 10.1021/jm5000563
CHEMBL3287704 118652 0 None - 0 Rat 6.0 pEC50 = 6.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 388 10 2 6 3.8 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(C)=O)c(O)c1C 10.1021/jm5000563
68109941 162901 0 None - 1 Human 8.0 pEC50 = 8.0 Binding
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4063313 162901 0 None - 1 Human 8.0 pEC50 = 8.0 Binding
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
53390518 89469 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c(Cl)c1 10.1021/jm3005306
CHEMBL2179635 89469 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c(Cl)c1 10.1021/jm3005306
53390519 89470 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 441 6 1 3 5.8 Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
CHEMBL2179636 89470 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 441 6 1 3 5.8 Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
23521689 11615 0 None - 0 Human 6.0 pEC50 = 6.0 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 4 3.7 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(=O)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104248 11615 0 None - 0 Human 6.0 pEC50 = 6.0 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 4 3.7 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(=O)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
89735510 144675 0 None - 0 Human 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 1 5 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(CO)c3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3763263 144675 0 None - 0 Human 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 1 5 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(CO)c3)nc21 10.1016/j.bmcl.2016.01.021
164610619 191533 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4850952 191533 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
164627219 193160 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(OC[C@@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4875653 193160 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(OC[C@@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
44578904 188348 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 409 6 0 4 5.0 Cn1c(CN2C[C@@H]3C(COc4cccc(-c5ccccc5)c4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL476791 188348 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 409 6 0 4 5.0 Cn1c(CN2C[C@@H]3C(COc4cccc(-c5ccccc5)c4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
90643904 118661 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 11 2 6 4.5 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287713 118661 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 11 2 6 4.5 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
90643900 118656 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 402 11 2 6 4.2 CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2OC)c(C)c1O 10.1021/jm5000563
CHEMBL3287708 118656 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 402 11 2 6 4.2 CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2OC)c(C)c1O 10.1021/jm5000563
71117141 154227 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 435 4 0 8 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21 nan
CHEMBL3930164 154227 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 435 4 0 8 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21 nan
69929497 147066 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 434 3 0 7 2.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3cccnc3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805900 147066 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 434 3 0 7 2.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3cccnc3)nc21 10.1021/acsmedchemlett.5b00459
90643881 118662 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 11 2 6 4.5 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287714 118662 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 11 2 6 4.5 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
11648184 69817 0 None - 0 Human 5.9 pEC50 = 5.9 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 454 5 1 4 5.9 CC1(C2CCCC2)Cc2cc(CCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL178823 69817 0 None - 0 Human 5.9 pEC50 = 5.9 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 454 5 1 4 5.9 CC1(C2CCCC2)Cc2cc(CCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
71681826 96836 0 None -4 2 Human 5.9 pEC50 = 5.9 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
CHEMBL2381651 96836 0 None -4 2 Human 5.9 pEC50 = 5.9 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
162649186 190423 0 None - 0 Rat 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1205 32 6 12 12.5 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4748285 190423 0 None - 0 Rat 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1205 32 6 12 12.5 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4802609 190423 0 None - 0 Rat 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1205 32 6 12 12.5 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
1310 9095 110 None -13 18 Rat 4.9 pEC50 = 4.9 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
1369 9095 110 None -13 18 Rat 4.9 pEC50 = 4.9 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
33032 9095 110 None -13 18 Rat 4.9 pEC50 = 4.9 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
44272391 9095 110 None -13 18 Rat 4.9 pEC50 = 4.9 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
88747398 9095 110 None -13 18 Rat 4.9 pEC50 = 4.9 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
CHEMBL575060 9095 110 None -13 18 Rat 4.9 pEC50 = 4.9 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
DB00142 9095 110 None -13 18 Rat 4.9 pEC50 = 4.9 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
71681825 96830 0 None - 0 Human 7.9 pEC50 = 7.9 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 226 3 3 4 -0.2 [N-]=[N+]=N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
CHEMBL2381645 96830 0 None - 0 Human 7.9 pEC50 = 7.9 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 226 3 3 4 -0.2 [N-]=[N+]=N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
104766 6822 42 None -11 11 Human 4.9 pEC50 = 4.9 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
1365 6822 42 None -11 11 Human 4.9 pEC50 = 4.9 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
CHEMBL34453 6822 42 None -11 11 Human 4.9 pEC50 = 4.9 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
11583075 70264 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 442 5 1 5 5.3 O=C1c2c(cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c2Cl)CC1C1CCCC1 10.1016/j.bmcl.2005.01.077
CHEMBL179939 70264 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 442 5 1 5 5.3 O=C1c2c(cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c2Cl)CC1C1CCCC1 10.1016/j.bmcl.2005.01.077
162647509 190416 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1134 27 6 12 10.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4744407 190416 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1134 27 6 12 10.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4802513 190416 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1134 27 6 12 10.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
56929215 118624 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287671 118624 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
90643902 118659 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 390 10 2 5 4.4 CCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
CHEMBL3287711 118659 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 390 10 2 5 4.4 CCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
67056056 146979 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 429 2 0 7 3.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)OC(C)(C)C)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3804910 146979 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 429 2 0 7 3.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)OC(C)(C)C)nc21 10.1021/acsmedchemlett.5b00459
46190878 8653 7 None - 1 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
6253 8653 7 None - 1 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
CHEMBL595759 8653 7 None - 1 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
46225407 206516 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 427 3 0 5 4.1 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccc(F)cc21 10.1016/j.bmcl.2009.11.032
CHEMBL593532 206516 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 427 3 0 5 4.1 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccc(F)cc21 10.1016/j.bmcl.2009.11.032
46225359 206608 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 418 5 0 6 3.9 Clc1cnc(N2CCN(Cc3nc4ccccc4n3Cc3ccccc3)CC2)nc1 10.1016/j.bmcl.2009.11.032
CHEMBL594236 206608 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 418 5 0 6 3.9 Clc1cnc(N2CCN(Cc3nc4ccccc4n3Cc3ccccc3)CC2)nc1 10.1016/j.bmcl.2009.11.032
46225334 206825 0 None - 1 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 358 3 0 4 3.7 Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595607 206825 0 None - 1 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 358 3 0 4 3.7 Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225358 208641 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 485 5 0 5 5.5 FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3n2Cc2ccccc2)CC1 10.1016/j.bmcl.2009.11.032
CHEMBL607195 208641 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 485 5 0 5 5.5 FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3n2Cc2ccccc2)CC1 10.1016/j.bmcl.2009.11.032
24815439 208714 1 None - 3 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL607689 208714 1 None - 3 Human 6.9 pEC50 = 6.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225384 206676 4 None - 0 Human 4.9 pEC50 = 4.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 328 3 1 5 2.3 Clc1cnc(N2CCN(Cc3nc4ccccc4[nH]3)CC2)nc1 10.1016/j.bmcl.2009.11.032
CHEMBL594673 206676 4 None - 0 Human 4.9 pEC50 = 4.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 328 3 1 5 2.3 Clc1cnc(N2CCN(Cc3nc4ccccc4[nH]3)CC2)nc1 10.1016/j.bmcl.2009.11.032
46225383 206876 0 None - 0 Human 4.9 pEC50 = 4.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 395 3 1 4 4.0 FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3[nH]2)CC1 10.1016/j.bmcl.2009.11.032
CHEMBL595991 206876 0 None - 0 Human 4.9 pEC50 = 4.9 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 395 3 1 4 4.0 FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3[nH]2)CC1 10.1016/j.bmcl.2009.11.032
69929646 147097 0 None - 0 Human 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 329 2 1 6 1.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3806226 147097 0 None - 0 Human 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 329 2 1 6 1.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4)nc21 10.1021/acsmedchemlett.5b00459
127038185 144721 0 None - 0 Human 4.9 pEC50 = 4.9 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 248 2 0 4 2.4 COc1ccc2c(c1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3763995 144721 0 None - 0 Human 4.9 pEC50 = 4.9 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 248 2 0 4 2.4 COc1ccc2c(c1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
90643868 118638 0 None - 0 Rat 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
CHEMBL3287690 118638 0 None - 0 Rat 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
164608826 191246 0 None - 0 Rat 7.9 pEC50 = 7.9 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 11 2 6 5.3 COc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
CHEMBL4846872 191246 0 None - 0 Rat 7.9 pEC50 = 7.9 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 11 2 6 5.3 COc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
68108429 156458 0 None - 0 Human 7.9 pEC50 = 7.9 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 448 5 0 4 5.7 FC(F)(F)c1c(CN2CCC(c3ccccc3Cl)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
CHEMBL3947590 156458 0 None - 0 Human 7.9 pEC50 = 7.9 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 448 5 0 4 5.7 FC(F)(F)c1c(CN2CCC(c3ccccc3Cl)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
53390677 89463 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 451 6 1 5 6.0 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
CHEMBL2179629 89463 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 451 6 1 5 6.0 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
53390520 89471 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 445 6 1 3 5.7 O=C(O)c1cc(F)cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1 10.1021/jm3005306
CHEMBL2179637 89471 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 445 6 1 3 5.7 O=C(O)c1cc(F)cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1 10.1021/jm3005306
6604704 108177 35 None - 0 Human 4.9 pEC50 = 4.9 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 173 2 3 3 -0.3 N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1 10.1021/jm970719q
CHEMBL29726 108177 35 None - 0 Human 4.9 pEC50 = 4.9 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 173 2 3 3 -0.3 N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1 10.1021/jm970719q
49822195 152960 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 432 5 0 4 5.2 FC(F)(F)c1c(CN2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
CHEMBL3919978 152960 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 432 5 0 4 5.2 FC(F)(F)c1c(CN2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
162657776 190462 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1176 30 6 12 11.7 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4759458 190462 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1176 30 6 12 11.7 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4803052 190462 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1176 30 6 12 11.7 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
25195461 8925 48 None - 1 Human 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 8925 48 None - 1 Human 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 8925 48 None - 1 Human 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 8925 48 None - 1 Human 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
86765132 118673 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 428 10 2 5 5.6 Cc1c(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cccc1C(=O)O 10.1021/jm5000563
CHEMBL3287725 118673 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 428 10 2 5 5.6 Cc1c(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cccc1C(=O)O 10.1021/jm5000563
164613604 191963 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 430 9 2 6 4.9 COc1ccc(C(=O)O)cc1O[C@@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4857426 191963 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 430 9 2 6 4.9 COc1ccc(C(=O)O)cc1O[C@@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
11362035 6831 1 None - 1 Human 7.9 pEC50 = 7.9 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2004.04.017
6328 6831 1 None - 1 Human 7.9 pEC50 = 7.9 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2004.04.017
6329 6831 1 None - 1 Human 7.9 pEC50 = 7.9 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2004.04.017
CHEMBL105296 6831 1 None - 1 Human 7.9 pEC50 = 7.9 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2004.04.017
23521659 11618 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 414 6 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104260 11618 0 None - 0 Human 6.9 pEC50 = 6.9 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 414 6 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
23521713 116546 0 None - 0 Human 5.9 pEC50 = 5.9 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 3 4.6 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(C)c2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL323138 116546 0 None - 0 Human 5.9 pEC50 = 5.9 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 3 4.6 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(C)c2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
49822116 153770 13 None - 1 Human 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 153770 13 None - 1 Human 5.9 pEC50 = 5.9 Binding
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
44395191 73074 0 None - 0 Human 5.9 pEC50 = 5.9 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 396 10 2 7 3.6 CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL184838 73074 0 None - 0 Human 5.9 pEC50 = 5.9 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 396 10 2 7 3.6 CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
164621278 192311 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(OC[C@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4862801 192311 0 None - 0 Rat 6.9 pEC50 = 6.9 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(OC[C@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
25195461 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 8925 48 None - 1 Human 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
49765871 8926 45 None - 1 Human 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1016/j.bmc.2022.116614
6317 8926 45 None - 1 Human 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1016/j.bmc.2022.116614
CHEMBL2179319 8926 45 None - 1 Human 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1016/j.bmc.2022.116614
90643858 118643 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Agonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assayAgonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287695 118643 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Agonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assayAgonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
90643905 118663 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 10 2 5 4.8 Cc1c(OCCCCOc2ccc(C(=O)C(C)C)c(O)c2C)cccc1C(=O)O 10.1021/jm5000563
CHEMBL3287715 118663 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 10 2 5 4.8 Cc1c(OCCCCOc2ccc(C(=O)C(C)C)c(O)c2C)cccc1C(=O)O 10.1021/jm5000563
67056141 146987 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 4 0 8 2.9 Cc1cc(CN2CC3CCC2CN3c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)no1 10.1021/acsmedchemlett.5b00459
CHEMBL3805017 146987 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 4 0 8 2.9 Cc1cc(CN2CC3CCC2CN3c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)no1 10.1021/acsmedchemlett.5b00459
68107810 152932 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 432 5 0 4 5.2 Fc1ccccc1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
CHEMBL3919807 152932 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 432 5 0 4 5.2 Fc1ccccc1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
68108457 155335 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3938796 155335 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
127039577 144743 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 462 6 1 5 5.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(OCc3cccc(-c4cc(F)cc(C(=O)O)c4)c3)cc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764173 144743 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 462 6 1 5 5.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(OCc3cccc(-c4cc(F)cc(C(=O)O)c4)c3)cc21 10.1016/j.bmcl.2016.01.021
9885608 11623 1 None - 0 Human 5.8 pEC50 = 5.8 Binding
Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1 10.1021/jm034015u
CHEMBL104296 11623 1 None - 0 Human 5.8 pEC50 = 5.8 Binding
Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1 10.1021/jm034015u
9885608 11623 1 None - 0 Human 5.8 pEC50 = 5.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL104296 11623 1 None - 0 Human 5.8 pEC50 = 5.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
90643863 118633 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 434 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287683 118633 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 434 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
90643865 118635 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 418 11 2 5 5.0 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287687 118635 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 418 11 2 5 5.0 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
90643878 118649 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287701 118649 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
90668092 116314 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of mGluR2 (unknown origin) by FLIPR assayPositive allosteric modulation of mGluR2 (unknown origin) by FLIPR assay
ChEMBL 306 6 1 3 4.1 CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221831 116314 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of mGluR2 (unknown origin) by FLIPR assayPositive allosteric modulation of mGluR2 (unknown origin) by FLIPR assay
ChEMBL 306 6 1 3 4.1 CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
46225371 206602 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 453 6 0 6 4.1 COCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL594204 206602 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 453 6 0 6 4.1 COCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225372 208144 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 356 4 0 6 2.8 CCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL604472 208144 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 356 4 0 6 2.8 CCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225582 208394 0 None - 2 Human 6.8 pEC50 = 6.8 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL605831 208394 0 None - 2 Human 6.8 pEC50 = 6.8 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
3461070 124124 1 None - 0 Human 4.8 pEC50 = 4.8 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 307 3 0 5 2.3 Cn1c(CN2CCN(c3ccccn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL339714 124124 1 None - 0 Human 4.8 pEC50 = 4.8 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 307 3 0 5 2.3 Cn1c(CN2CCN(c3ccccn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
44335554 116000 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCC(CC)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL321746 116000 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCC(CC)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
71479388 147001 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805139 147001 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
23521708 11597 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(COc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104191 11597 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(COc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
23521727 11674 0 None - 0 Human 5.8 pEC50 = 5.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 366 7 0 3 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Cc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL104541 11674 0 None - 0 Human 5.8 pEC50 = 5.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 366 7 0 3 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Cc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
44335514 11723 0 None - 0 Human 5.8 pEC50 = 5.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 360 6 0 4 3.3 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104785 11723 0 None - 0 Human 5.8 pEC50 = 5.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 360 6 0 4 3.3 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
44404948 77329 0 None - 1 Rat 4.8 pEC50 = 4.8 Binding
Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells
ChEMBL 214 2 3 5 -1.0 NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1 10.1021/jm0504499
CHEMBL194787 77329 0 None - 1 Rat 4.8 pEC50 = 4.8 Binding
Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells
ChEMBL 214 2 3 5 -1.0 NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1 10.1021/jm0504499
1310 9095 110 None -13 18 Rat 4.8 pEC50 = 4.8 Binding
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
1369 9095 110 None -13 18 Rat 4.8 pEC50 = 4.8 Binding
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
33032 9095 110 None -13 18 Rat 4.8 pEC50 = 4.8 Binding
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
44272391 9095 110 None -13 18 Rat 4.8 pEC50 = 4.8 Binding
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
88747398 9095 110 None -13 18 Rat 4.8 pEC50 = 4.8 Binding
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
CHEMBL575060 9095 110 None -13 18 Rat 4.8 pEC50 = 4.8 Binding
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
DB00142 9095 110 None -13 18 Rat 4.8 pEC50 = 4.8 Binding
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
90643895 118651 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 388 10 2 6 3.8 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(C)=O)c(O)c1C 10.1021/jm5000563
CHEMBL3287703 118651 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 388 10 2 6 3.8 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(C)=O)c(O)c1C 10.1021/jm5000563
90643880 118657 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 402 11 2 6 4.2 CCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O 10.1021/jm5000563
CHEMBL3287709 118657 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 402 11 2 6 4.2 CCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O 10.1021/jm5000563
24905705 190801 1 None - 0 Rat 5.8 pEC50 = 5.8 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL482081 190801 1 None - 0 Rat 5.8 pEC50 = 5.8 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
25195461 8925 48 None - 1 Human 5.8 pEC50 = 5.8 Binding
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 8925 48 None - 1 Human 5.8 pEC50 = 5.8 Binding
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 8925 48 None - 1 Human 5.8 pEC50 = 5.8 Binding
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 8925 48 None - 1 Human 5.8 pEC50 = 5.8 Binding
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
164616255 191727 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 445 10 2 5 5.1 CNC(=O)c1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1F 10.1016/j.bmcl.2021.128342
CHEMBL4853748 191727 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 445 10 2 5 5.1 CNC(=O)c1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1F 10.1016/j.bmcl.2021.128342
11663312 70243 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 497 7 0 4 7.8 O=C1c2c(cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c2Cl)CC1C1CCCC1 10.1016/j.bmcl.2005.01.077
CHEMBL179839 70243 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 497 7 0 4 7.8 O=C1c2c(cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c2Cl)CC1C1CCCC1 10.1016/j.bmcl.2005.01.077
24905705 190801 1 None - 0 Rat 5.8 pEC50 = 5.8 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL482081 190801 1 None - 0 Rat 5.8 pEC50 = 5.8 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
44335555 11808 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.4 CCC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL105193 11808 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.4 CCC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
49765871 8926 45 None - 1 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 8926 45 None - 1 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 8926 45 None - 1 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
134156113 157650 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 483 5 0 5 5.3 FC(F)(F)c1c(CN2CCN(c3ccc(Cl)cc3Cl)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
CHEMBL3957311 157650 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 483 5 0 5 5.3 FC(F)(F)c1c(CN2CCN(c3ccc(Cl)cc3Cl)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
71117730 150709 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21 nan
CHEMBL3902193 150709 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21 nan
46182736 7776 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm3005306
6323 7776 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm3005306
CHEMBL1651219 7776 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm3005306
53390521 89472 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 457 7 1 4 5.5 COc1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)cc1C(=O)O 10.1021/jm3005306
CHEMBL2179638 89472 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 457 7 1 4 5.5 COc1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)cc1C(=O)O 10.1021/jm3005306
46182736 7776 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm1012165
6323 7776 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm1012165
CHEMBL1651219 7776 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm1012165
1402 6910 44 None - 0 Human 5.8 pEC50 = 5.8 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.08.020
9825084 6910 44 None - 0 Human 5.8 pEC50 = 5.8 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.08.020
CHEMBL108939 6910 44 None - 0 Human 5.8 pEC50 = 5.8 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.08.020
90643882 118664 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 404 10 2 5 4.6 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)C(C)C)c1O 10.1021/jm5000563
CHEMBL3287716 118664 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 404 10 2 5 4.6 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)C(C)C)c1O 10.1021/jm5000563
90643876 118647 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1cc(OCCCCOc2ccc(C(=O)CC(C)C)c(O)c2C)ccc1C(=O)O 10.1021/jm5000563
CHEMBL3287699 118647 0 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1cc(OCCCCOc2ccc(C(=O)CC(C)C)c(O)c2C)ccc1C(=O)O 10.1021/jm5000563
44335578 116451 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 402 8 0 4 4.2 CCC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL322588 116451 0 None - 0 Human 7.8 pEC50 = 7.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 402 8 0 4 4.2 CCC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
66787355 163004 0 None - 1 Human 7.7 pEC50 = 7.7 Binding
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4064589 163004 0 None - 1 Human 7.7 pEC50 = 7.7 Binding
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
23521698 115323 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 384 7 0 3 4.5 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(F)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL320151 115323 0 None - 0 Human 6.8 pEC50 = 6.8 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 384 7 0 3 4.5 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(F)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
11648824 64100 1 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 488 6 1 3 7.4 Cc1c(OCc2cccc(-c3ccc(Cl)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1021/jm1012165
CHEMBL1651207 64100 1 None - 0 Rat 6.8 pEC50 = 6.8 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 488 6 1 3 7.4 Cc1c(OCc2cccc(-c3ccc(Cl)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1021/jm1012165
1310 9095 110 None -22 18 Human 5.8 pEC50 = 5.8 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
1369 9095 110 None -22 18 Human 5.8 pEC50 = 5.8 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
33032 9095 110 None -22 18 Human 5.8 pEC50 = 5.8 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
44272391 9095 110 None -22 18 Human 5.8 pEC50 = 5.8 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
88747398 9095 110 None -22 18 Human 5.8 pEC50 = 5.8 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
CHEMBL575060 9095 110 None -22 18 Human 5.8 pEC50 = 5.8 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
DB00142 9095 110 None -22 18 Human 5.8 pEC50 = 5.8 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
1310 9095 110 None -13 18 Rat 5.8 pEC50 = 5.8 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
1369 9095 110 None -13 18 Rat 5.8 pEC50 = 5.8 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
33032 9095 110 None -13 18 Rat 5.8 pEC50 = 5.8 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
44272391 9095 110 None -13 18 Rat 5.8 pEC50 = 5.8 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
88747398 9095 110 None -13 18 Rat 5.8 pEC50 = 5.8 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
CHEMBL575060 9095 110 None -13 18 Rat 5.8 pEC50 = 5.8 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
DB00142 9095 110 None -13 18 Rat 5.8 pEC50 = 5.8 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
89497771 144772 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 1 5 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(CO)cc3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764530 144772 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 1 5 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(CO)cc3)nc21 10.1016/j.bmcl.2016.01.021
1310 9095 110 None -13 18 Rat 5.7 pEC50 = 5.7 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
1369 9095 110 None -13 18 Rat 5.7 pEC50 = 5.7 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
33032 9095 110 None -13 18 Rat 5.7 pEC50 = 5.7 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
44272391 9095 110 None -13 18 Rat 5.7 pEC50 = 5.7 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
88747398 9095 110 None -13 18 Rat 5.7 pEC50 = 5.7 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
CHEMBL575060 9095 110 None -13 18 Rat 5.7 pEC50 = 5.7 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
DB00142 9095 110 None -13 18 Rat 5.7 pEC50 = 5.7 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
10407808 73449 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 386 11 2 5 4.5 CCCc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL185419 73449 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 386 11 2 5 4.5 CCCc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
90643887 118671 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 6 5.3 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287723 118671 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 6 5.3 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1021/jm5000563
89735344 144822 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 0 5 3.5 COc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765257 144822 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 0 5 3.5 COc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
11213605 71239 3 None - 0 Human 6.7 pEC50 = 6.7 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 471 8 0 4 7.4 CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL181364 71239 3 None - 0 Human 6.7 pEC50 = 6.7 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 471 8 0 4 7.4 CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
127042771 144831 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(S(C)(=O)=O)c3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3765337 144831 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(S(C)(=O)=O)c3)nc21 10.1016/j.bmcl.2016.01.021
90643869 118639 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287691 118639 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
89497792 144814 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(C#N)cc3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3765103 144814 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(C#N)cc3)nc21 10.1016/j.bmcl.2016.01.021
164611067 191395 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O 10.1016/j.bmcl.2021.128342
CHEMBL4849142 191395 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O 10.1016/j.bmcl.2021.128342
11633075 72164 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 416 5 1 5 4.8 CC(C)C1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL182946 72164 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 416 5 1 5 4.8 CC(C)C1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
25125217 7343 25 None - 1 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.6b00913
7678 7343 25 None - 1 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.6b00913
CHEMBL3937907 7343 25 None - 1 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.6b00913
DB16073 7343 25 None - 1 Human 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.6b00913
24815434 206475 0 None - 3 Human 6.7 pEC50 = 6.7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593196 206475 0 None - 3 Human 6.7 pEC50 = 6.7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225335 206826 0 None - 1 Human 6.7 pEC50 = 6.7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595608 206826 0 None - 1 Human 6.7 pEC50 = 6.7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225583 206953 0 None - 3 Human 6.7 pEC50 = 6.7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL596527 206953 0 None - 3 Human 6.7 pEC50 = 6.7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225408 208653 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 427 3 0 5 4.1 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(F)ccc21 10.1016/j.bmcl.2009.11.032
CHEMBL607313 208653 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 427 3 0 5 4.1 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(F)ccc21 10.1016/j.bmcl.2009.11.032
46225387 206542 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 477 3 0 5 5.0 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C(F)(F)F)ccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593756 206542 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 477 3 0 5 5.0 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C(F)(F)F)ccc21 10.1016/j.bmcl.2009.11.032
56968082 150689 0 None - 0 Human 8.6 pEC50 = 8.6 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 428 5 0 4 5.3 CC1(c2ccccc2)CCCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)C1 10.1021/acs.jmedchem.6b00913
CHEMBL3901998 150689 0 None - 0 Human 8.6 pEC50 = 8.6 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 428 5 0 4 5.3 CC1(c2ccccc2)CCCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)C1 10.1021/acs.jmedchem.6b00913
25051025 189246 0 None - 0 Rat 7.7 pEC50 = 7.7 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ncccc21 10.1016/j.bmcl.2008.09.026
CHEMBL478646 189246 0 None - 0 Rat 7.7 pEC50 = 7.7 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ncccc21 10.1016/j.bmcl.2008.09.026
53390433 89466 0 None - 0 Rat 7.7 pEC50 = 7.7 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 443 6 2 4 5.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1O 10.1021/jm3005306
CHEMBL2179632 89466 0 None - 0 Rat 7.7 pEC50 = 7.7 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 443 6 2 4 5.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1O 10.1021/jm3005306
66799514 89478 0 None - 0 Rat 7.7 pEC50 = 7.7 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 431 4 1 2 6.3 O=C(O)c1cc(-c2cccc(-c3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm3005306
CHEMBL2179646 89478 0 None - 0 Rat 7.7 pEC50 = 7.7 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 431 4 1 2 6.3 O=C(O)c1cc(-c2cccc(-c3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm3005306
23521677 114231 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 378 7 0 3 4.5 C=C(c1ccccc1)c1cccc(N(Cc2cccnc2)S(=O)(=O)CC)c1 10.1016/j.bmcl.2004.04.017
CHEMBL318309 114231 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 378 7 0 3 4.5 C=C(c1ccccc1)c1cccc(N(Cc2cccnc2)S(=O)(=O)CC)c1 10.1016/j.bmcl.2004.04.017
53390754 89475 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 490 7 1 7 6.0 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)cc([N+](=O)[O-])c1 10.1021/jm3005306
CHEMBL2179643 89475 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 490 7 1 7 6.0 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)cc([N+](=O)[O-])c1 10.1021/jm3005306
90643897 118653 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 372 9 2 5 4.1 CC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287705 118653 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 372 9 2 5 4.1 CC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
104766 6822 42 None -11 11 Human 5.7 pEC50 = 5.7 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970719q
1365 6822 42 None -11 11 Human 5.7 pEC50 = 5.7 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970719q
CHEMBL34453 6822 42 None -11 11 Human 5.7 pEC50 = 5.7 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970719q
25195461 8925 48 None - 1 Human 5.7 pEC50 = 5.7 Binding
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 8925 48 None - 1 Human 5.7 pEC50 = 5.7 Binding
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 8925 48 None - 1 Human 5.7 pEC50 = 5.7 Binding
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 8925 48 None - 1 Human 5.7 pEC50 = 5.7 Binding
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
10002415 172805 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 423 11 2 7 4.0 CCCc1c(OCCCCN(C)c2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL425540 172805 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 423 11 2 7 4.0 CCCc1c(OCCCCN(C)c2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
90643889 118674 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1021/jm5000563
CHEMBL3287726 118674 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1021/jm5000563
49822115 8927 21 None - 1 Human 7.7 pEC50 = 7.7 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
8947 8927 21 None - 1 Human 7.7 pEC50 = 7.7 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL3947764 8927 21 None - 1 Human 7.7 pEC50 = 7.7 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
11275666 96832 1 None -15 2 Human 7.7 pEC50 = 7.7 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
CHEMBL2381647 96832 1 None -15 2 Human 7.7 pEC50 = 7.7 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
164627946 193163 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 10 2 5 5.6 Cc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
CHEMBL4875695 193163 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 10 2 5 5.6 Cc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
44335500 11894 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 360 6 0 4 3.0 COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL105671 11894 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 360 6 0 4 3.0 COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
23521734 116537 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(COc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL323080 116537 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(COc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
25051018 191128 0 None - 0 Rat 5.7 pEC50 = 5.7 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 334 5 0 5 2.7 Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccncc21 10.1016/j.bmcl.2008.09.026
CHEMBL484398 191128 0 None - 0 Rat 5.7 pEC50 = 5.7 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 334 5 0 5 2.7 Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccncc21 10.1016/j.bmcl.2008.09.026
54761054 144859 0 None - 2 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765778 144859 0 None - 2 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
71136691 150399 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 394 3 0 5 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21 nan
CHEMBL3899706 150399 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 394 3 0 5 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21 nan
134157889 160995 0 None - 0 Human 7.7 pEC50 = 7.7 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 465 5 0 5 4.7 Fc1ccc(N2CCCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3985987 160995 0 None - 0 Human 7.7 pEC50 = 7.7 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 465 5 0 5 4.7 Fc1ccc(N2CCCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
50993967 64106 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 433 6 1 3 5.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651213 64106 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 433 6 1 3 5.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
51037131 147062 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 356 2 0 5 3.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCC4CCCCC43)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805883 147062 0 None - 0 Human 5.7 pEC50 = 5.7 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 356 2 0 5 3.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCC4CCCCC43)nc21 10.1021/acsmedchemlett.5b00459
90643860 118626 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287675 118626 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
164611059 191358 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4848600 191358 0 None - 0 Rat 6.7 pEC50 = 6.7 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
11496256 70560 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 456 5 1 5 5.7 CC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL180186 70560 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 456 5 1 5 5.7 CC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
11656483 130381 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 514 9 1 6 6.3 CC1(C2CCCC2)Cc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL361837 130381 0 None - 0 Human 6.7 pEC50 = 6.7 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 514 9 1 6 6.3 CC1(C2CCCC2)Cc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
90643873 118644 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 456 13 2 6 5.4 Cc1c(OCCCCOCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287696 118644 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 456 13 2 6 5.4 Cc1c(OCCCCOCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
9979770 73112 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.3 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL185054 73112 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.3 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.08.020
49765871 8926 45 None - 1 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 8926 45 None - 1 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 8926 45 None - 1 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
44335614 12059 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 446 9 0 6 3.3 CCOC(=O)C(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL106561 12059 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 446 9 0 6 3.3 CCOC(=O)C(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
45082292 122029 2 None -3 3 Human 4.6 pEC50 = 4.6 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O 10.1039/C1MD00186H
CHEMBL3347670 122029 2 None -3 3 Human 4.6 pEC50 = 4.6 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O 10.1039/C1MD00186H
90643906 118665 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 10 2 5 4.8 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287717 118665 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 10 2 5 4.8 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
49822116 153770 13 None - 1 Human 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 153770 13 None - 1 Human 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
90643875 118646 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 460 11 2 5 6.1 Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287698 118646 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 460 11 2 5 6.1 Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
44578992 188401 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 333 5 0 4 3.3 Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL477376 188401 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 333 5 0 4 3.3 Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
44335556 8082 0 None - 0 Human 7.6 pEC50 = 7.6 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 10.1016/j.bmcl.2004.04.017
6257 8082 0 None - 0 Human 7.6 pEC50 = 7.6 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 10.1016/j.bmcl.2004.04.017
CHEMBL321968 8082 0 None - 0 Human 7.6 pEC50 = 7.6 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 10.1016/j.bmcl.2004.04.017
53390753 89476 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 463 6 1 5 6.3 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1F 10.1021/jm3005306
CHEMBL2179644 89476 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 463 6 1 5 6.3 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1F 10.1021/jm3005306
44395327 73699 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 438 11 2 7 4.7 CCCc1c(OC(C)CCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL186584 73699 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 438 11 2 7 4.7 CCCc1c(OC(C)CCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
90643862 118632 0 None - 0 Rat 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 458 11 1 4 6.7 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1C 10.1021/jm5000563
CHEMBL3287682 118632 0 None - 0 Rat 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 458 11 1 4 6.7 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1C 10.1021/jm5000563
44401995 76851 4 None - 0 Rat 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 13 3 6 4.9 Cc1c(OCCCCOc2ccc(CCC(=O)O)c(O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL193982 76851 4 None - 0 Rat 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 13 3 6 4.9 Cc1c(OCCCCOc2ccc(CCC(=O)O)c(O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
71117222 152863 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 441 4 0 7 2.6 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
CHEMBL3919237 152863 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 441 4 0 7 2.6 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
53390676 89460 0 None - 0 Rat 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 465 7 1 5 6.1 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(CC5CC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
CHEMBL2179626 89460 0 None - 0 Rat 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 465 7 1 5 6.1 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(CC5CC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
54761054 144859 0 None - 2 Rat 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765778 144859 0 None - 2 Rat 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
44335650 11574 0 None - 0 Human 5.6 pEC50 = 5.6 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 7 1 4 3.5 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(O)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104129 11574 0 None - 0 Human 5.6 pEC50 = 5.6 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 7 1 4 3.5 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(O)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
25050850 198567 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cnccc21 10.1016/j.bmcl.2008.09.026
CHEMBL519817 198567 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cnccc21 10.1016/j.bmcl.2008.09.026
46225385 208142 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 439 4 0 6 4.0 COc1ccc2c(c1)nc(CN1CCN(c3nc(Cl)ccc3C(F)(F)F)CC1)n2C 10.1016/j.bmcl.2009.11.032
CHEMBL604469 208142 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 439 4 0 6 4.0 COc1ccc2c(c1)nc(CN1CCN(c3nc(Cl)ccc3C(F)(F)F)CC1)n2C 10.1016/j.bmcl.2009.11.032
46225375 208652 0 None - 0 Human 5.6 pEC50 = 5.6 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 437 5 0 5 4.8 CCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL607311 208652 0 None - 0 Human 5.6 pEC50 = 5.6 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 437 5 0 5 4.8 CCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
60096211 96834 0 None -5 2 Human 6.6 pEC50 = 6.6 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
CHEMBL2381649 96834 0 None -5 2 Human 6.6 pEC50 = 6.6 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
164619969 192308 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(O[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4862778 192308 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(O[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
25195461 8925 48 None - 1 Human 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 8925 48 None - 1 Human 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 8925 48 None - 1 Human 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 8925 48 None - 1 Human 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
90643891 118629 0 None - 0 Rat 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 424 11 1 4 6.0 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1C 10.1021/jm5000563
CHEMBL3287678 118629 0 None - 0 Rat 5.6 pEC50 = 5.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 424 11 1 4 6.0 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1C 10.1021/jm5000563
90643898 118654 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 376 9 2 5 4.0 CC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
CHEMBL3287706 118654 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 376 9 2 5 4.0 CC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
44578946 188381 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 375 6 0 4 4.5 CC(C)c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
CHEMBL477169 188381 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 375 6 0 4 4.5 CC(C)c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
44578947 188382 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 367 5 0 4 4.0 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL477170 188382 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 367 5 0 4 4.0 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
25110722 196316 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cn4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL514218 196316 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cn4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
68108294 154065 0 None - 0 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 444 6 0 5 4.8 COC1(c2ccccc2)CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
CHEMBL3928875 154065 0 None - 0 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 444 6 0 5 4.8 COC1(c2ccccc2)CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
68108567 160532 0 None - 0 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1cccc(F)c1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
CHEMBL3981882 160532 0 None - 0 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1cccc(F)c1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
89735130 144728 0 None - 0 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3C#N)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764057 144728 0 None - 0 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3C#N)nc21 10.1016/j.bmcl.2016.01.021
71128768 151358 0 None - 0 Human 7.6 pEC50 = 7.6 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 441 4 0 7 2.7 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
CHEMBL3907644 151358 0 None - 0 Human 7.6 pEC50 = 7.6 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 441 4 0 7 2.7 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
50993968 64107 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 469 6 1 3 6.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(c3ccccc3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651214 64107 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 469 6 1 3 6.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(c3ccccc3)C4=O)c2)ccc1Cl 10.1021/jm1012165
164619502 192979 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4872955 192979 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
25195461 8925 48 None - 1 Human 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 8925 48 None - 1 Human 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 8925 48 None - 1 Human 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 8925 48 None - 1 Human 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
44335577 12654 3 None - 0 Human 7.6 pEC50 = 7.6 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 402 8 0 4 4.0 CC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL107948 12654 3 None - 0 Human 7.6 pEC50 = 7.6 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 402 8 0 4 4.0 CC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
49765871 8926 45 None - 1 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 8926 45 None - 1 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 8926 45 None - 1 Human 7.6 pEC50 = 7.6 Binding
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
11677757 72875 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 500 8 1 6 6.0 CC1(C2CCCC2)Cc2cc(OCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL183911 72875 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 500 8 1 6 6.0 CC1(C2CCCC2)Cc2cc(OCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
1402 6910 44 None - 0 Human 6.6 pEC50 = 6.6 Binding
Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1021/jm034015u
9825084 6910 44 None - 0 Human 6.6 pEC50 = 6.6 Binding
Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1021/jm034015u
CHEMBL108939 6910 44 None - 0 Human 6.6 pEC50 = 6.6 Binding
Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1021/jm034015u
50994049 64108 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 475 6 1 3 6.6 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651215 64108 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 475 6 1 3 6.6 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
11598292 136953 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 486 7 1 6 5.6 CC1(C2CCCC2)Cc2cc(OCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL367823 136953 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 486 7 1 6 5.6 CC1(C2CCCC2)Cc2cc(OCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
164611777 191704 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4853369 191704 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
164621310 192344 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 429 10 2 6 5.0 Cc1ncc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
CHEMBL4863303 192344 0 None - 0 Rat 7.6 pEC50 = 7.6 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 429 10 2 6 5.0 Cc1ncc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
11344646 133554 1 None -1 2 Human 7.5 pEC50 = 7.5 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
CHEMBL365368 133554 1 None -1 2 Human 7.5 pEC50 = 7.5 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
162650303 190427 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1064 22 6 12 8.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4748549 190427 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1064 22 6 12 8.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4802664 190427 0 None - 0 Rat 6.6 pEC50 = 6.6 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1064 22 6 12 8.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
11625861 72634 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 416 6 1 5 4.9 CCCC1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL183541 72634 0 None - 0 Human 6.6 pEC50 = 6.6 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 416 6 1 5 4.9 CCCC1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
71136188 152533 0 None - 0 Human 5.6 pEC50 = 5.6 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 384 3 1 6 1.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21 nan
CHEMBL3916627 152533 0 None - 0 Human 5.6 pEC50 = 5.6 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 384 3 1 6 1.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21 nan
44335626 12166 0 None - 0 Human 7.5 pEC50 = 7.5 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 428 7 0 4 4.7 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCCCC2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL107114 12166 0 None - 0 Human 7.5 pEC50 = 7.5 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 428 7 0 4 4.7 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCCCC2)c1 10.1016/j.bmcl.2004.04.017
51036108 147005 0 None - 0 Human 7.5 pEC50 = 7.5 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 441 3 0 9 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805203 147005 0 None - 0 Human 7.5 pEC50 = 7.5 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 441 3 0 9 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21 10.1021/acsmedchemlett.5b00459
127052897 147086 0 None - 0 Human 7.5 pEC50 = 7.5 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3806137 147086 0 None - 0 Human 7.5 pEC50 = 7.5 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
1310 9095 110 None -22 18 Human 6.5 pEC50 = 6.5 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
1369 9095 110 None -22 18 Human 6.5 pEC50 = 6.5 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
33032 9095 110 None -22 18 Human 6.5 pEC50 = 6.5 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
44272391 9095 110 None -22 18 Human 6.5 pEC50 = 6.5 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
88747398 9095 110 None -22 18 Human 6.5 pEC50 = 6.5 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
CHEMBL575060 9095 110 None -22 18 Human 6.5 pEC50 = 6.5 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
DB00142 9095 110 None -22 18 Human 6.5 pEC50 = 6.5 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
11697718 70956 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 431 8 0 4 6.7 CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(C)c(C)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL180871 70956 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 431 8 0 4 6.7 CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(C)c(C)c2C1=O 10.1016/j.bmcl.2005.01.077
164624801 192990 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4873125 192990 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
71136186 158848 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 431 3 0 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21 nan
CHEMBL3967432 158848 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 431 3 0 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21 nan
25110723 196418 0 None - 0 Rat 7.5 pEC50 = 7.5 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cn4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL515034 196418 0 None - 0 Rat 7.5 pEC50 = 7.5 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cn4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
1377 8122 26 None -1 6 Rat 6.5 pEC50 = 6.5 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm00009a001
5310979 8122 26 None -1 6 Rat 6.5 pEC50 = 6.5 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm00009a001
CHEMBL284193 8122 26 None -1 6 Rat 6.5 pEC50 = 6.5 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm00009a001
50994823 64112 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 475 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CCN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651221 64112 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 475 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CCN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
44578996 188364 0 None - 0 Rat 5.5 pEC50 = 5.5 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 6 0 4 4.1 c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C4CC4)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
CHEMBL476965 188364 0 None - 0 Rat 5.5 pEC50 = 5.5 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 6 0 4 4.1 c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C4CC4)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
10251009 73555 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 410 11 2 7 4.1 CCCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL185911 73555 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 410 11 2 7 4.1 CCCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
164611874 191893 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 9 2 5 5.4 Cc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O 10.1016/j.bmcl.2021.128342
CHEMBL4856242 191893 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 9 2 5 5.4 Cc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O 10.1016/j.bmcl.2021.128342
56651050 144736 0 None - 0 Human 7.5 pEC50 = 7.5 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 294 2 0 3 4.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)cc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764108 144736 0 None - 0 Human 7.5 pEC50 = 7.5 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 294 2 0 3 4.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)cc21 10.1016/j.bmcl.2016.01.021
44335670 11735 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 366 7 0 3 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Cc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104818 11735 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 366 7 0 3 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Cc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
50994757 64111 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 463 6 1 5 6.3 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)oc4c3)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651220 64111 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 463 6 1 5 6.3 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)oc4c3)c2)ccc1Cl 10.1021/jm1012165
89735684 144804 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1ccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)cc1 10.1016/j.bmcl.2016.01.021
CHEMBL3764850 144804 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1ccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)cc1 10.1016/j.bmcl.2016.01.021
46225336 206827 0 None - 1 Human 6.5 pEC50 = 6.5 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 363 3 0 6 3.5 Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595609 206827 0 None - 1 Human 6.5 pEC50 = 6.5 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 363 3 0 6 3.5 Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225320 207962 0 None - 1 Human 6.5 pEC50 = 6.5 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL603443 207962 0 None - 1 Human 6.5 pEC50 = 6.5 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225569 208141 0 None - 1 Human 6.5 pEC50 = 6.5 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL604467 208141 0 None - 1 Human 6.5 pEC50 = 6.5 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
44335573 11596 0 None - 0 Human 7.5 pEC50 = 7.5 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 388 7 0 4 3.8 CC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104190 11596 0 None - 0 Human 7.5 pEC50 = 7.5 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 388 7 0 4 3.8 CC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
10846649 108008 4 None - 0 Human 6.5 pEC50 = 6.5 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@H]2C(=O)O 10.1021/jm970719q
CHEMBL296054 108008 4 None - 0 Human 6.5 pEC50 = 6.5 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@H]2C(=O)O 10.1021/jm970719q
11743092 71364 0 None - 0 Human 5.5 pEC50 = 5.5 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 12 2 7 4.4 CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL181648 71364 0 None - 0 Human 5.5 pEC50 = 5.5 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 12 2 7 4.4 CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
51036916 147091 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 350 2 0 5 3.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCc4ccccc43)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3806176 147091 0 None - 0 Human 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 350 2 0 5 3.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCc4ccccc43)nc21 10.1021/acsmedchemlett.5b00459
90643893 118631 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287680 118631 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
9999945 73912 0 None - 0 Human 5.5 pEC50 = 5.5 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 382 9 2 7 3.3 CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL187537 73912 0 None - 0 Human 5.5 pEC50 = 5.5 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 382 9 2 7 3.3 CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
90643883 118666 0 None - 0 Rat 7.5 pEC50 = 7.5 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 12 2 6 4.6 CCCC(=O)c1ccc(OCCCCOc2c(OC)cccc2C(=O)O)c(C)c1O 10.1021/jm5000563
CHEMBL3287718 118666 0 None - 0 Rat 7.5 pEC50 = 7.5 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 12 2 6 4.6 CCCC(=O)c1ccc(OCCCCOc2c(OC)cccc2C(=O)O)c(C)c1O 10.1021/jm5000563
10047169 9998 1 None - 0 Human 6.5 pEC50 = 6.5 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.08.020
1403 9998 1 None - 0 Human 6.5 pEC50 = 6.5 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.08.020
CHEMBL182371 9998 1 None - 0 Human 6.5 pEC50 = 6.5 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.08.020
1377 8122 26 None -1 6 Rat 6.5 pEC50 = 6.5 Binding
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
5310979 8122 26 None -1 6 Rat 6.5 pEC50 = 6.5 Binding
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL284193 8122 26 None -1 6 Rat 6.5 pEC50 = 6.5 Binding
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
53321382 64109 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 551 7 1 3 7.5 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(Cc3ccc(C(F)(F)F)cc3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651216 64109 0 None - 0 Rat 6.5 pEC50 = 6.5 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 551 7 1 3 7.5 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(Cc3ccc(C(F)(F)F)cc3)C4=O)c2)ccc1Cl 10.1021/jm1012165
59066632 213349 89 None - 1 Rat 4.5 pEC50 = 4.5 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm020122x
92136 213349 89 None - 1 Rat 4.5 pEC50 = 4.5 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm020122x
CHEMBL88804 213349 89 None - 1 Rat 4.5 pEC50 = 4.5 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm020122x
6603885 108978 23 None - 0 Rat 4.5 pEC50 = 4.5 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 158 2 3 5 -0.5 N[C@H](C(=O)O)c1cc(O)no1 10.1021/jm00009a001
6971208 108978 23 None - 0 Rat 4.5 pEC50 = 4.5 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 158 2 3 5 -0.5 N[C@H](C(=O)O)c1cc(O)no1 10.1021/jm00009a001
CHEMBL30285 108978 23 None - 0 Rat 4.5 pEC50 = 4.5 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 158 2 3 5 -0.5 N[C@H](C(=O)O)c1cc(O)no1 10.1021/jm00009a001
59066632 213349 89 None - 1 Rat 4.5 pEC50 = 4.5 Binding
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9703597
92136 213349 89 None - 1 Rat 4.5 pEC50 = 4.5 Binding
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9703597
CHEMBL88804 213349 89 None - 1 Rat 4.5 pEC50 = 4.5 Binding
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9703597
23521697 11799 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 400 7 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCC2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL105151 11799 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 400 7 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCC2)c1 10.1016/j.bmcl.2004.04.017
69930179 147050 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 433 3 0 6 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3ccccc3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805718 147050 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 433 3 0 6 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3ccccc3)nc21 10.1021/acsmedchemlett.5b00459
23521709 171244 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Oc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL421406 171244 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Oc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
44404948 77329 0 None - 1 Rat 4.4 pEC50 = 4.4 Binding
Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells
ChEMBL 214 2 3 5 -1.0 NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1 10.1021/jm0504499
CHEMBL194787 77329 0 None - 1 Rat 4.4 pEC50 = 4.4 Binding
Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells
ChEMBL 214 2 3 5 -1.0 NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1 10.1021/jm0504499
69929785 146973 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 407 3 0 8 2.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4c3ncccn3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3804845 146973 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 407 3 0 8 2.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4c3ncccn3)nc21 10.1021/acsmedchemlett.5b00459
9837114 122043 0 None - 0 Human 4.4 pEC50 = 4.4 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 203 4 3 6 -0.4 N[C@H](CCc1nsnc1O)C(=O)O 10.1039/C1MD00186H
CHEMBL334842 122043 0 None - 0 Human 4.4 pEC50 = 4.4 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 203 4 3 6 -0.4 N[C@H](CCc1nsnc1O)C(=O)O 10.1039/C1MD00186H
9837114 122043 0 None - 0 Rat 4.4 pEC50 = 4.4 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 203 4 3 6 -0.4 N[C@H](CCc1nsnc1O)C(=O)O 10.1021/jm020122x
CHEMBL334842 122043 0 None - 0 Rat 4.4 pEC50 = 4.4 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 203 4 3 6 -0.4 N[C@H](CCc1nsnc1O)C(=O)O 10.1021/jm020122x
11691077 71468 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 456 5 1 5 5.7 CC1(C2CCCC2)Cc2cc(OCc3cccc(-c4nn[nH]n4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL181869 71468 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 456 5 1 5 5.7 CC1(C2CCCC2)Cc2cc(OCc3cccc(-c4nn[nH]n4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
164624284 192808 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4870631 192808 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
54761055 144665 1 None - 0 Human 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(S(C)(=O)=O)cc3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3763172 144665 1 None - 0 Human 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(S(C)(=O)=O)cc3)nc21 10.1016/j.bmcl.2016.01.021
69092138 149573 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 464 6 1 4 5.8 Fc1ccc([C@H]2CC[C@@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3892865 149573 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 464 6 1 4 5.8 Fc1ccc([C@H]2CC[C@@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
1368 9070 37 None -3 11 Human 6.4 pEC50 = 6.4 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
5310956 9070 37 None -3 11 Human 6.4 pEC50 = 6.4 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
CHEMBL280563 9070 37 None -3 11 Human 6.4 pEC50 = 6.4 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
10318576 73487 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 396 10 2 7 3.7 CCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL185602 73487 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 396 10 2 7 3.7 CCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
3954 7451 60 None - 1 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm3005306
9868580 7451 60 None - 1 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm3005306
CHEMBL593013 7451 60 None - 1 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm3005306
3954 7451 60 None - 1 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm1012165
9868580 7451 60 None - 1 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm1012165
CHEMBL593013 7451 60 None - 1 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm1012165
10560963 171296 1 None - 0 Human 4.4 pEC50 = 4.4 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@@H]2C(=O)O 10.1021/jm970719q
CHEMBL42148 171296 1 None - 0 Human 4.4 pEC50 = 4.4 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@@H]2C(=O)O 10.1021/jm970719q
164610692 191681 0 None - 0 Rat 5.4 pEC50 = 5.4 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 459 10 1 5 5.4 Cc1c(OCCCCOc2ccc(F)c(C(=O)N(C)C)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4853089 191681 0 None - 0 Rat 5.4 pEC50 = 5.4 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 459 10 1 5 5.4 Cc1c(OCCCCOc2ccc(F)c(C(=O)N(C)C)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
49765871 8926 45 None - 1 Human 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 8926 45 None - 1 Human 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 8926 45 None - 1 Human 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
46225584 206454 0 None - 3 Human 7.4 pEC50 = 7.4 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 408 3 0 4 5.0 Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593056 206454 0 None - 3 Human 7.4 pEC50 = 7.4 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 408 3 0 4 5.0 Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
49765871 8926 45 None - 1 Human 8.3 pEC50 = 8.3 Binding
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 8926 45 None - 1 Human 8.3 pEC50 = 8.3 Binding
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 8926 45 None - 1 Human 8.3 pEC50 = 8.3 Binding
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
90643858 118643 0 None - 0 Rat 7.4 pEC50 = 7.4 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287695 118643 0 None - 0 Rat 7.4 pEC50 = 7.4 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
71116701 151637 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 387 4 1 4 2.4 CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O nan
CHEMBL3909811 151637 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 387 4 1 4 2.4 CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O nan
1310 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
1369 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
33032 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
44272391 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
88747398 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
CHEMBL575060 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
DB00142 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
1310 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
1369 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
33032 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
44272391 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
88747398 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
CHEMBL575060 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
DB00142 9095 110 None -13 18 Rat 5.4 pEC50 = 5.4 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
139054390 211702 106 None -1 5 Rat 5.4 pEC50 = 5.4 Binding
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O 10.1021/jm9703597
23327 211702 106 None -1 5 Rat 5.4 pEC50 = 5.4 Binding
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O 10.1021/jm9703597
CHEMBL76232 211702 106 None -1 5 Rat 5.4 pEC50 = 5.4 Binding
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O 10.1021/jm9703597
10465478 28557 0 None - 0 Human 4.4 pEC50 = 4.4 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 203 4 3 6 -0.4 N[C@@H](CCc1nsnc1O)C(=O)O 10.1039/C1MD00186H
CHEMBL131922 28557 0 None - 0 Human 4.4 pEC50 = 4.4 Binding
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 203 4 3 6 -0.4 N[C@@H](CCc1nsnc1O)C(=O)O 10.1039/C1MD00186H
10465478 28557 0 None - 0 Rat 4.4 pEC50 = 4.4 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 203 4 3 6 -0.4 N[C@@H](CCc1nsnc1O)C(=O)O 10.1021/jm020122x
CHEMBL131922 28557 0 None - 0 Rat 4.4 pEC50 = 4.4 Binding
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 203 4 3 6 -0.4 N[C@@H](CCc1nsnc1O)C(=O)O 10.1021/jm020122x
90643892 118630 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287679 118630 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
25050849 191021 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cccnc21 10.1016/j.bmcl.2008.09.026
CHEMBL483569 191021 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cccnc21 10.1016/j.bmcl.2008.09.026
23521725 12472 0 None - 0 Human 5.4 pEC50 = 5.4 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 4 3.7 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(=O)c2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL107806 12472 0 None - 0 Human 5.4 pEC50 = 5.4 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 4 3.7 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(=O)c2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
10026879 73803 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 452 13 2 7 5.0 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL187077 73803 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 452 13 2 7 5.0 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.08.020
90643879 118650 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 456 12 2 6 5.4 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
CHEMBL3287702 118650 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 456 12 2 6 5.4 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
51036701 146977 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 302 2 0 5 2.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCCC3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3804903 146977 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 302 2 0 5 2.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCCC3)nc21 10.1021/acsmedchemlett.5b00459
71116772 154447 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 456 4 1 8 3.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21 nan
CHEMBL3931730 154447 0 None - 0 Human 7.4 pEC50 = 7.4 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 456 4 1 8 3.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21 nan
23521693 12127 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL106909 12127 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
11496550 70665 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 473 5 1 4 5.8 CC(=O)NC(=O)c1ccc(COc2cc3c(c(Cl)c2Cl)C(=O)C(C)(C2CCCC2)C3)cc1 10.1016/j.bmcl.2005.01.077
CHEMBL180455 70665 0 None - 0 Human 6.4 pEC50 = 6.4 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 473 5 1 4 5.8 CC(=O)NC(=O)c1ccc(COc2cc3c(c(Cl)c2Cl)C(=O)C(C)(C2CCCC2)C3)cc1 10.1016/j.bmcl.2005.01.077
164615875 192223 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 9 2 5 5.4 Cc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4861618 192223 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 9 2 5 5.4 Cc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
49822116 153770 13 None - 1 Human 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 153770 13 None - 1 Human 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
90643861 118627 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287676 118627 0 None - 0 Rat 6.4 pEC50 = 6.4 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
90643867 118637 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287689 118637 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
49765871 8926 45 None - 1 Human 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 8926 45 None - 1 Human 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 8926 45 None - 1 Human 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
127038550 144841 0 None - 0 Human 5.3 pEC50 = 5.3 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3S(C)(=O)=O)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3765412 144841 0 None - 0 Human 5.3 pEC50 = 5.3 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3S(C)(=O)=O)nc21 10.1016/j.bmcl.2016.01.021
90643888 118672 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 6 5.3 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287724 118672 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 6 5.3 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1021/jm5000563
71681824 96831 0 None - 0 Human 7.3 pEC50 = 7.3 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
CHEMBL2381646 96831 0 None - 0 Human 7.3 pEC50 = 7.3 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
53390605 89462 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 467 7 1 5 6.3 CC(C)Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
CHEMBL2179628 89462 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 467 7 1 5 6.3 CC(C)Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
1310 9095 110 None -22 18 Human 5.3 pEC50 = 5.3 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
1369 9095 110 None -22 18 Human 5.3 pEC50 = 5.3 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
33032 9095 110 None -22 18 Human 5.3 pEC50 = 5.3 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
44272391 9095 110 None -22 18 Human 5.3 pEC50 = 5.3 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
88747398 9095 110 None -22 18 Human 5.3 pEC50 = 5.3 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
CHEMBL575060 9095 110 None -22 18 Human 5.3 pEC50 = 5.3 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
DB00142 9095 110 None -22 18 Human 5.3 pEC50 = 5.3 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
164623088 192264 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4862244 192264 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
71574840 93046 0 None - 0 Rat 5.3 pEC50 = 5.3 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 204 7 4 4 -0.8 NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL2312685 93046 0 None - 0 Rat 5.3 pEC50 = 5.3 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 204 7 4 4 -0.8 NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
89497505 144706 0 None - 0 Human 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 378 3 1 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cc(C(C)(C)O)ccc3C#N)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3763754 144706 0 None - 0 Human 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 378 3 1 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cc(C(C)(C)O)ccc3C#N)nc21 10.1016/j.bmcl.2016.01.021
164610947 192030 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 415 10 2 6 4.7 Cc1c(OCCCCOc2cncc(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4858387 192030 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 415 10 2 6 4.7 Cc1c(OCCCCOc2cncc(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
71574840 93046 0 None - 0 Rat 4.3 pEC50 = 4.3 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 204 7 4 4 -0.8 NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL2312685 93046 0 None - 0 Rat 4.3 pEC50 = 4.3 Binding
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 204 7 4 4 -0.8 NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
44395282 129935 0 None - 0 Human 6.3 pEC50 = 6.3 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.4 CCCc1c(OCCCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL361248 129935 0 None - 0 Human 6.3 pEC50 = 6.3 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.4 CCCc1c(OCCCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
46182745 64101 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm3005306
CHEMBL1651208 64101 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm3005306
46182745 64101 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 461 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651208 64101 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 461 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
90643899 118655 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 372 9 2 5 4.1 CC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287707 118655 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 372 9 2 5 4.1 CC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
164620553 192548 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4866466 192548 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
46225386 206541 0 None - 0 Human 7.3 pEC50 = 7.3 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 434 3 0 6 3.8 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C#N)ccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593755 206541 0 None - 0 Human 7.3 pEC50 = 7.3 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 434 3 0 6 3.8 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C#N)ccc21 10.1016/j.bmcl.2009.11.032
11690041 71642 0 None - 0 Human 5.3 pEC50 = 5.3 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 408 6 1 5 4.5 CC1(C2CCCC2)Cc2cc(OCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL182138 71642 0 None - 0 Human 5.3 pEC50 = 5.3 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 408 6 1 5 4.5 CC1(C2CCCC2)Cc2cc(OCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
104766 6822 42 None -3 11 Rat 5.3 pEC50 = 5.3 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
1365 6822 42 None -3 11 Rat 5.3 pEC50 = 5.3 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
CHEMBL34453 6822 42 None -3 11 Rat 5.3 pEC50 = 5.3 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
46225373 206603 0 None - 0 Human 6.3 pEC50 = 6.3 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 386 6 0 7 2.4 COCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL594205 206603 0 None - 0 Human 6.3 pEC50 = 6.3 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 386 6 0 7 2.4 COCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225337 206756 0 None - 1 Human 6.3 pEC50 = 6.3 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 375 3 0 5 3.3 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595151 206756 0 None - 1 Human 6.3 pEC50 = 6.3 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 375 3 0 5 3.3 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
851990 206484 4 None - 0 Human 5.3 pEC50 = 5.3 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 306 3 0 4 2.9 Cn1c(CN2CCN(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593300 206484 4 None - 0 Human 5.3 pEC50 = 5.3 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 306 3 0 4 2.9 Cn1c(CN2CCN(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
164618046 192241 0 None - 0 Rat 5.3 pEC50 = 5.3 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 471 10 1 6 5.1 COc1ccc(C(=O)N(C)C)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4861837 192241 0 None - 0 Rat 5.3 pEC50 = 5.3 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 471 10 1 6 5.1 COc1ccc(C(=O)N(C)C)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
71116730 155841 0 None - 0 Human 7.3 pEC50 = 7.3 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 424 3 1 6 2.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21 nan
CHEMBL3942904 155841 0 None - 0 Human 7.3 pEC50 = 7.3 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 424 3 1 6 2.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21 nan
90643864 118634 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 460 11 2 5 6.1 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287684 118634 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 460 11 2 5 6.1 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
44578997 188365 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)nc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL476966 188365 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)nc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
164625596 192521 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 10 2 5 5.6 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4866163 192521 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 10 2 5 5.6 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
11699129 138743 0 None - 0 Human 6.3 pEC50 = 6.3 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 509 6 1 5 5.2 CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)NS(C)(=O)=O)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL369526 138743 0 None - 0 Human 6.3 pEC50 = 6.3 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 509 6 1 5 5.2 CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)NS(C)(=O)=O)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
90643885 118668 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 CCCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287720 118668 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 CCCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
117972250 149090 3 None - 1 Human 6.3 pEC50 = 6.3 Binding
Agonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assayAgonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885379 149090 3 None - 1 Human 6.3 pEC50 = 6.3 Binding
Agonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assayAgonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
71128783 146986 0 None - 0 Human 6.3 pEC50 = 6.3 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 397 3 0 7 2.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCN(C(=O)c4ccon4)CC3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805005 146986 0 None - 0 Human 6.3 pEC50 = 6.3 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 397 3 0 7 2.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCN(C(=O)c4ccon4)CC3)nc21 10.1021/acsmedchemlett.5b00459
162677305 190572 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1078 23 6 12 9.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4800093 190572 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1078 23 6 12 9.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4804159 190572 0 None - 0 Rat 7.3 pEC50 = 7.3 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1078 23 6 12 9.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
71116952 154092 0 None - 0 Human 7.3 pEC50 = 7.3 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
CHEMBL3929070 154092 0 None - 0 Human 7.3 pEC50 = 7.3 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
10775369 185144 1 None - 0 Human 4.3 pEC50 = 4.3 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@H]2C[C@@H]1[C@@H]2C(=O)O 10.1021/jm970719q
CHEMBL46527 185144 1 None - 0 Human 4.3 pEC50 = 4.3 Binding
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@H]2C[C@@H]1[C@@H]2C(=O)O 10.1021/jm970719q
11684927 70250 0 None - 0 Human 6.3 pEC50 = 6.3 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 511 7 0 4 8.2 CC1(C2CCCC2)Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL179876 70250 0 None - 0 Human 6.3 pEC50 = 6.3 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 511 7 0 4 8.2 CC1(C2CCCC2)Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
90643877 118648 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1cc(OCCCCOc2ccc(C(=O)CC3CCCC3)c(O)c2C)ccc1C(=O)O 10.1021/jm5000563
CHEMBL3287700 118648 0 None - 0 Rat 6.3 pEC50 = 6.3 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1cc(OCCCCOc2ccc(C(=O)CC3CCCC3)c(O)c2C)ccc1C(=O)O 10.1021/jm5000563
68108604 154182 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 480 7 0 5 5.2 Fc1ccc(COC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3929786 154182 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 480 7 0 5 5.2 Fc1ccc(COC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
68107740 158322 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 466 6 0 5 5.0 Fc1ccc(OC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3963034 158322 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 466 6 0 5 5.0 Fc1ccc(OC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
89735006 144723 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3764005 144723 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
88593167 157538 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 482 5 0 4 5.8 FC(F)(F)c1c(CN2CCC(c3ccccc3)(C(F)(F)F)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
CHEMBL3956434 157538 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 482 5 0 4 5.8 FC(F)(F)c1c(CN2CCC(c3ccccc3)(C(F)(F)F)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
53390675 89461 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 465 6 1 5 6.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
CHEMBL2179627 89461 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 465 6 1 5 6.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
11676185 72364 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 422 7 1 5 4.8 CC1(C2CCCC2)Cc2cc(OCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL183234 72364 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 422 7 1 5 4.8 CC1(C2CCCC2)Cc2cc(OCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
44390403 129114 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 457 7 0 4 7.1 Cc1c(OCc2cccc(CSc3ccncc3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2005.01.077
CHEMBL359909 129114 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 457 7 0 4 7.1 Cc1c(OCc2cccc(CSc3ccncc3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2005.01.077
50994051 64110 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 463 8 1 3 6.3 CC(C)CCN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
CHEMBL1651217 64110 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 463 8 1 3 6.3 CC(C)CCN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
11663353 130016 1 None - 0 Human 6.2 pEC50 = 6.2 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 499 6 2 6 5.1 CC1(C2CCCC2)Cc2cc(OCC(=O)Nc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL361358 130016 1 None - 0 Human 6.2 pEC50 = 6.2 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 499 6 2 6 5.1 CC1(C2CCCC2)Cc2cc(OCC(=O)Nc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
54761054 144859 0 None - 2 Human 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation of human mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of human mGluR2 by GTP-gamma-S binding assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765778 144859 0 None - 2 Human 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation of human mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of human mGluR2 by GTP-gamma-S binding assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
90643870 118640 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
CHEMBL3287692 118640 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
54761054 144859 0 None - 2 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765778 144859 0 None - 2 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
11691314 188679 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 470 6 2 4 6.5 Cc1c(OCc2cccc(-c3ccc(O)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2020.127212
CHEMBL4779278 188679 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 470 6 2 4 6.5 Cc1c(OCc2cccc(-c3ccc(O)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2020.127212
162660656 190485 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1120 26 6 12 10.2 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4762369 190485 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1120 26 6 12 10.2 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4803219 190485 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1120 26 6 12 10.2 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
90643901 118658 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 386 10 2 5 4.5 CCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287710 118658 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 386 10 2 5 4.5 CCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
23521692 115350 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 436 8 0 4 4.6 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL320292 115350 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 436 8 0 4 4.6 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
11691221 130105 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 464 5 1 5 5.4 CC1(c2ccccc2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL361633 130105 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 464 5 1 5 5.4 CC1(c2ccccc2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
54761054 144859 0 None - 2 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1021/acsmedchemlett.5b00459
CHEMBL3765778 144859 0 None - 2 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1021/acsmedchemlett.5b00459
164616933 191844 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1ccc(C(=O)O)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4855540 191844 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1ccc(C(=O)O)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
46225357 206576 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 423 4 0 5 4.4 CCn1c(CN2CCN(c3nc(C(F)(F)F)ccc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL594011 206576 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 423 4 0 5 4.4 CCn1c(CN2CCN(c3nc(C(F)(F)F)ccc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
11310142 9200 19 None 1 2 Human 7.2 pEC50 = 7.2 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm4000165
11614 9200 19 None 1 2 Human 7.2 pEC50 = 7.2 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm4000165
CHEMBL192051 9200 19 None 1 2 Human 7.2 pEC50 = 7.2 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm4000165
51036108 147005 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 441 3 0 9 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805203 147005 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 441 3 0 9 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21 10.1021/acsmedchemlett.5b00459
90643872 118642 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287694 118642 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
25050844 191022 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2ncccc21 10.1016/j.bmcl.2008.09.026
CHEMBL483570 191022 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2ncccc21 10.1016/j.bmcl.2008.09.026
44335613 175919 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 432 9 0 6 2.9 CCOC(=O)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL440328 175919 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 432 9 0 6 2.9 CCOC(=O)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
53390678 89459 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 425 5 1 5 5.2 Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
CHEMBL2179625 89459 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 425 5 1 5 5.2 Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
69093542 154205 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(F)(F)c1c(CN2CCCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
CHEMBL3929950 154205 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(F)(F)c1c(CN2CCCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
25195461 8925 48 None - 1 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 8925 48 None - 1 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 8925 48 None - 1 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 8925 48 None - 1 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
53390604 89464 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 481 8 1 5 6.7 CC(C)CCn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
CHEMBL2179630 89464 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 481 8 1 5 6.7 CC(C)CCn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
49822116 153770 13 None - 1 Human 5.2 pEC50 = 5.2 Binding
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 153770 13 None - 1 Human 5.2 pEC50 = 5.2 Binding
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
127052897 147086 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3806137 147086 0 None - 0 Human 6.2 pEC50 = 6.2 Binding
Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
11568710 187199 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(-c3cccc(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2020.127212
CHEMBL4752318 187199 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(-c3cccc(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2020.127212
71116726 152054 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 438 3 0 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21 nan
CHEMBL3912982 152054 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 438 3 0 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21 nan
90643866 118636 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 5 5.5 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287688 118636 0 None - 0 Rat 6.2 pEC50 = 6.2 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 5 5.5 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
44578905 188367 0 None - 0 Rat 8.2 pEC50 = 8.2 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 369 5 0 4 3.6 Cn1c(CN2C[C@@H]3C(COc4cc(F)ccc4F)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL476998 188367 0 None - 0 Rat 8.2 pEC50 = 8.2 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 369 5 0 4 3.6 Cn1c(CN2C[C@@H]3C(COc4cc(F)ccc4F)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
11084869 96828 2 None - 1 Human 8.1 pEC50 = 8.1 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
CHEMBL2381643 96828 2 None - 1 Human 8.1 pEC50 = 8.1 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
70052526 96827 2 None - 1 Human 8.1 pEC50 = 8.1 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
CHEMBL2381642 96827 2 None - 1 Human 8.1 pEC50 = 8.1 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
50993963 64102 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 435 6 1 3 5.6 CC(C)N1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
CHEMBL1651209 64102 0 None - 0 Rat 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 435 6 1 3 5.6 CC(C)N1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
89735186 144680 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 295 2 0 4 3.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3763395 144680 0 None - 0 Human 7.2 pEC50 = 7.2 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 295 2 0 4 3.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)nc21 10.1016/j.bmcl.2016.01.021
10249222 11783 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 3 4.6 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(C)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL105065 11783 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 3 4.6 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(C)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
90643886 118669 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 404 11 2 5 4.8 CCCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
CHEMBL3287721 118669 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 404 11 2 5 4.8 CCCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
53390680 89474 0 None - 0 Rat 6.1 pEC50 = 6.1 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 459 6 1 5 6.4 Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(=O)n(C4CCCC4)sc3c2)c1 10.1021/jm3005306
CHEMBL2179642 89474 0 None - 0 Rat 6.1 pEC50 = 6.1 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 459 6 1 5 6.4 Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(=O)n(C4CCCC4)sc3c2)c1 10.1021/jm3005306
1310 9095 110 None -22 18 Human 5.1 pEC50 = 5.1 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
1369 9095 110 None -22 18 Human 5.1 pEC50 = 5.1 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
33032 9095 110 None -22 18 Human 5.1 pEC50 = 5.1 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
44272391 9095 110 None -22 18 Human 5.1 pEC50 = 5.1 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
88747398 9095 110 None -22 18 Human 5.1 pEC50 = 5.1 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
CHEMBL575060 9095 110 None -22 18 Human 5.1 pEC50 = 5.1 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
DB00142 9095 110 None -22 18 Human 5.1 pEC50 = 5.1 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
127052897 147086 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3806137 147086 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
164614107 191909 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4856556 191909 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
1368 9070 37 None 1 11 Rat 6.1 pEC50 = 6.1 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
5310956 9070 37 None 1 11 Rat 6.1 pEC50 = 6.1 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
CHEMBL280563 9070 37 None 1 11 Rat 6.1 pEC50 = 6.1 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
44395381 72913 0 None - 0 Human 5.1 pEC50 = 5.1 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 10 2 8 3.5 CCCc1c(OCCCC(=O)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL184098 72913 0 None - 0 Human 5.1 pEC50 = 5.1 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 10 2 8 3.5 CCCc1c(OCCCC(=O)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
11539379 72372 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 436 8 1 5 5.2 CC1(C2CCCC2)Cc2cc(OCCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL183286 72372 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 436 8 1 5 5.2 CC1(C2CCCC2)Cc2cc(OCCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
25195461 8925 48 None - 1 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 8925 48 None - 1 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 8925 48 None - 1 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 8925 48 None - 1 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
104766 6822 42 None -3 11 Rat 5.1 pEC50 = 5.1 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
1365 6822 42 None -3 11 Rat 5.1 pEC50 = 5.1 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
CHEMBL34453 6822 42 None -3 11 Rat 5.1 pEC50 = 5.1 Binding
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
49822116 153770 13 None - 1 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 153770 13 None - 1 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
168278157 197138 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 435 4 0 3 6.4 Fc1ccc(C2CCC(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1016/j.bmc.2022.116614
CHEMBL5177038 197138 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 435 4 0 3 6.4 Fc1ccc(C2CCC(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1016/j.bmc.2022.116614
164616491 192170 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 430 9 2 6 4.9 COc1ccc(C(=O)O)cc1OC[C@@H](C)Oc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4860693 192170 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 430 9 2 6 4.9 COc1ccc(C(=O)O)cc1OC[C@@H](C)Oc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
23521714 11578 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 378 7 0 3 4.5 C=C(c1ccccc1)c1ccc(N(Cc2cccnc2)S(=O)(=O)CC)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL104140 11578 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 378 7 0 3 4.5 C=C(c1ccccc1)c1ccc(N(Cc2cccnc2)S(=O)(=O)CC)cc1 10.1016/j.bmcl.2004.04.017
11516962 70671 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 402 4 1 5 4.5 CC1(C)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL180488 70671 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 402 4 1 5 4.5 CC1(C)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
46190877 8652 7 None - 3 Human 7.1 pEC50 = 7.1 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
6252 8652 7 None - 3 Human 7.1 pEC50 = 7.1 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
CHEMBL605836 8652 7 None - 3 Human 7.1 pEC50 = 7.1 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
24849462 206537 0 None - 3 Human 7.1 pEC50 = 7.1 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593744 206537 0 None - 3 Human 7.1 pEC50 = 7.1 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225374 206633 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 370 5 0 6 3.2 CCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL594428 206633 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 370 5 0 6 3.2 CCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
24849789 206913 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 324 3 0 4 3.0 Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL596270 206913 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 324 3 0 4 3.0 Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
798232 206914 9 None - 1 Human 6.1 pEC50 = 6.1 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 340 3 0 4 3.5 Cn1c(CN2CCN(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL596271 206914 9 None - 1 Human 6.1 pEC50 = 6.1 Binding
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 340 3 0 4 3.5 Cn1c(CN2CCN(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
44578948 188400 0 None - 0 Rat 8.1 pEC50 = 8.1 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 385 5 0 4 4.1 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4F)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL477375 188400 0 None - 0 Rat 8.1 pEC50 = 8.1 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 385 5 0 4 4.1 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4F)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
71681823 96829 0 None - 0 Human 8.1 pEC50 = 8.1 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 226 3 3 4 -0.2 [N-]=[N+]=N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
CHEMBL2381644 96829 0 None - 0 Human 8.1 pEC50 = 8.1 Binding
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 226 3 3 4 -0.2 [N-]=[N+]=N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
66799669 89465 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 457 7 1 4 5.5 COc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
CHEMBL2179631 89465 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 457 7 1 4 5.5 COc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
53390432 89467 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 487 8 1 5 5.5 COc1cc(C(=O)O)cc(OC)c1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
CHEMBL2179633 89467 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 487 8 1 5 5.5 COc1cc(C(=O)O)cc(OC)c1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
50993964 64103 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 447 7 1 3 5.7 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(CC3CC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651210 64103 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 447 7 1 3 5.7 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(CC3CC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
89735530 144801 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(C#N)c3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764820 144801 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(C#N)c3)nc21 10.1016/j.bmcl.2016.01.021
164620998 192652 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4868114 192652 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
89735654 144726 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 313 2 0 4 3.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3F)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764024 144726 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 313 2 0 4 3.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3F)nc21 10.1016/j.bmcl.2016.01.021
90643903 118660 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 386 10 2 5 4.5 CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287712 118660 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 386 10 2 5 4.5 CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
90643859 118625 0 None - 0 Rat 6.1 pEC50 = 6.1 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287672 118625 0 None - 0 Rat 6.1 pEC50 = 6.1 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
69092138 155514 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 464 6 1 4 5.8 Fc1ccc([C@H]2CC[C@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3940264 155514 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 464 6 1 4 5.8 Fc1ccc([C@H]2CC[C@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
164612248 191669 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(O[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4852903 191669 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(O[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
11648510 70042 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 471 7 0 4 7.3 CC(C)C1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL179171 70042 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 471 7 0 4 7.3 CC(C)C1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
11712790 188035 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 484 7 1 4 6.8 COc1ccc(-c2cccc(COc3cc4c(c(C)c3C)C(=O)C(C3CCCC3)C4)c2)cc1C(=O)O 10.1016/j.bmcl.2020.127212
CHEMBL4761801 188035 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 484 7 1 4 6.8 COc1ccc(-c2cccc(COc3cc4c(c(C)c3C)C(=O)C(C3CCCC3)C4)c2)cc1C(=O)O 10.1016/j.bmcl.2020.127212
44578949 188322 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 401 5 0 4 4.3 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL476551 188322 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 401 5 0 4 4.3 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
25050845 191167 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2cnccc21 10.1016/j.bmcl.2008.09.026
CHEMBL484578 191167 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2cnccc21 10.1016/j.bmcl.2008.09.026
86691853 144852 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 339 3 1 5 3.2 Cc1ccc(CO)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765537 144852 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 339 3 1 5 3.2 Cc1ccc(CO)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
164609025 191220 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 10 2 5 5.9 Cc1c(OCCCCOc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4846460 191220 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 10 2 5 5.9 Cc1c(OCCCCOc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
10343566 73474 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 446 9 2 7 3.8 CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL185529 73474 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 446 9 2 7 3.8 CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O 10.1016/j.bmcl.2004.08.020
44335615 116843 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 460 9 0 6 3.7 CCOC(=O)C(C)(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL323541 116843 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 460 9 0 6 3.7 CCOC(=O)C(C)(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
71119170 155551 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 468 4 1 5 1.9 CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
CHEMBL3940610 155551 0 None - 0 Human 7.1 pEC50 = 7.1 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 468 4 1 5 1.9 CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
66786069 163240 0 None - 1 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4067290 163240 0 None - 1 Human 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
11654949 54245 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 432 5 1 3 6.2 CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)O)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL154542 54245 0 None - 0 Human 6.1 pEC50 = 6.1 Binding
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 432 5 1 3 6.2 CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)O)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
71136746 155379 0 None - 0 Human 8.0 pEC50 = 8.0 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
CHEMBL3939174 155379 0 None - 0 Human 8.0 pEC50 = 8.0 Binding
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
68107813 151769 0 None - 0 Human 8.0 pEC50 = 8.0 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 450 5 0 4 5.4 Fc1cccc(F)c1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
CHEMBL3910866 151769 0 None - 0 Human 8.0 pEC50 = 8.0 Binding
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 450 5 0 4 5.4 Fc1cccc(F)c1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
53390517 89468 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1ccc(Cl)c(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1 10.1021/jm3005306
CHEMBL2179634 89468 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1ccc(Cl)c(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1 10.1021/jm3005306
50993965 64104 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 447 6 1 3 5.8 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651211 64104 0 None - 0 Rat 7.1 pEC50 = 7.1 Binding
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 447 6 1 3 5.8 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
44395299 73824 0 None - 0 Human 6.0 pEC50 = 6.0 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.4 CCCc1c(OC(C)CCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL187151 73824 0 None - 0 Human 6.0 pEC50 = 6.0 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.4 CCCc1c(OC(C)CCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
162644103 190398 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1106 25 6 12 9.8 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4777845 190398 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1106 25 6 12 9.8 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4802343 190398 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1106 25 6 12 9.8 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
10413231 131815 0 None - 0 Human 7.0 pEC50 = 7.0 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 488 11 2 7 4.8 CC(C)CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL364324 131815 0 None - 0 Human 7.0 pEC50 = 7.0 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 488 11 2 7 4.8 CC(C)CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O 10.1016/j.bmcl.2004.08.020
10070087 74011 0 None - 0 Human 6.0 pEC50 = 6.0 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 409 11 3 7 4.0 CCCc1c(OCCCCNc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL187959 74011 0 None - 0 Human 6.0 pEC50 = 6.0 Binding
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 409 11 3 7 4.0 CCCc1c(OCCCCNc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
162646759 190411 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1148 28 6 12 11.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4740929 190411 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1148 28 6 12 11.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4802473 190411 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1148 28 6 12 11.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
90643874 118645 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 434 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287697 118645 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 434 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
44578903 188347 0 None - 0 Rat 6.0 pEC50 = 6.0 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 5 0 4 3.7 c1ccc(OCC2[C@H]3CN(Cc4nc5cccc6c5n4CCC6)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
CHEMBL476790 188347 0 None - 0 Rat 6.0 pEC50 = 6.0 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 5 0 4 3.7 c1ccc(OCC2[C@H]3CN(Cc4nc5cccc6c5n4CCC6)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
44578995 188345 0 None - 0 Rat 5.0 pEC50 = 5.0 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 330 5 0 3 4.0 c1ccc(OCC2[C@H]3CN(Cc4cnc5ccccc5c4)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
CHEMBL476756 188345 0 None - 0 Rat 5.0 pEC50 = 5.0 Binding
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 330 5 0 3 4.0 c1ccc(OCC2[C@H]3CN(Cc4cnc5ccccc5c4)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
90643890 118628 0 None - 0 Rat 6.0 pEC50 = 6.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 398 11 1 4 5.5 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1C 10.1021/jm5000563
CHEMBL3287677 118628 0 None - 0 Rat 6.0 pEC50 = 6.0 Binding
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 398 11 1 4 5.5 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1C 10.1021/jm5000563
49822116 153770 13 None - 1 Human 6.0 pEC50 = 6.0 Binding
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 153770 13 None - 1 Human 6.0 pEC50 = 6.0 Binding
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
162666879 190512 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1092 24 6 12 9.4 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4786847 190512 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1092 24 6 12 9.4 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4803552 190512 0 None - 0 Rat 7.0 pEC50 = 7.0 Binding
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1092 24 6 12 9.4 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
53390837 89477 0 None - 0 Rat 6.0 pEC50 = 6.0 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 506 6 0 5 6.8 CN(C)C(=O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
CHEMBL2179645 89477 0 None - 0 Rat 6.0 pEC50 = 6.0 Binding
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 506 6 0 5 6.8 CN(C)C(=O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
89554832 149579 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 484 7 2 6 4.4 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3892899 149579 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 484 7 2 6 4.4 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
71565964 151028 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 7 1 4 5.2 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1 nan
CHEMBL3904730 151028 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 7 1 4 5.2 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1 nan
124201729 153340 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 2 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@@H](O)Cc3ccc(Cl)nc3)cc2n1 nan
CHEMBL3922857 153340 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 2 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@@H](O)Cc3ccc(Cl)nc3)cc2n1 nan
89554927 153660 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 1 5 3.7 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1 nan
CHEMBL3925389 153660 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 1 5 3.7 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1 nan
71566125 153828 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 6 1 4 5.1 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1 nan
CHEMBL3926942 153828 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 6 1 4 5.1 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1 nan
89554857 154877 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 520 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
CHEMBL3935153 154877 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 520 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
71565965 155063 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 7 1 4 5.4 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1 nan
CHEMBL3936681 155063 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 7 1 4 5.4 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1 nan
71566127 155416 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 415 6 1 4 4.9 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1 nan
CHEMBL3939455 155416 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 415 6 1 4 4.9 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1 nan
89554768 156230 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 6 1 4 4.8 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1 nan
CHEMBL3946016 156230 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 6 1 4 4.8 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1 nan
71566207 157133 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 5 3.5 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3953157 157133 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 5 3.5 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554874 160250 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cccnc3)cc2n1 nan
CHEMBL3979547 160250 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cccnc3)cc2n1 nan
89554726 167490 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL4113710 167490 0 None - 0 Human 8.0 pIC50 = 8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
156012009 184136 0 None - 0 Human 8.0 pIC50 = 8 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4637618 184136 0 None - 0 Human 8.0 pIC50 = 8 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1)C(F)(F)F 10.1016/j.bmcl.2020.127066
22317767 63064 0 None - 0 Rat 8.0 pIC50 = 8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629847 63064 0 None - 0 Rat 8.0 pIC50 = 8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11269030 63078 0 None - 0 Rat 8.0 pIC50 = 8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629861 63078 0 None - 0 Rat 8.0 pIC50 = 8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
22317741 63186 0 None - 0 Rat 8.0 pIC50 = 8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631863 63186 0 None - 0 Rat 8.0 pIC50 = 8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
22317279 63188 0 None - 0 Rat 8.0 pIC50 = 8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 463 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631865 63188 0 None - 0 Rat 8.0 pIC50 = 8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 463 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
71566440 150420 0 None - 0 Human 7.0 pIC50 = 7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 300 2 1 2 3.8 NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccccc2n1 nan
CHEMBL3899883 150420 0 None - 0 Human 7.0 pIC50 = 7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 300 2 1 2 3.8 NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccccc2n1 nan
22224818 153456 0 None - 0 Rat 6.0 pIC50 = 6.0 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 2 1 4 3.9 CN1CCN(C(=O)c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)CC1 10.1016/j.bmcl.2007.10.026
CHEMBL392381 153456 0 None - 0 Rat 6.0 pIC50 = 6.0 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 2 1 4 3.9 CN1CCN(C(=O)c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)CC1 10.1016/j.bmcl.2007.10.026
71565597 160735 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 4 1 4 2.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCS3(=O)=O)cc2n1 nan
CHEMBL3983624 160735 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 4 1 4 2.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCS3(=O)=O)cc2n1 nan
9905849 210832 0 None - 0 Rat 6.0 pIC50 = 6.0 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 337 4 0 4 4.9 Clc1ccc(/C(=C/n2cncn2)OC2CCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
CHEMBL69970 210832 0 None - 0 Rat 6.0 pIC50 = 6.0 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 337 4 0 4 4.9 Clc1ccc(/C(=C/n2cncn2)OC2CCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
71565672 158043 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 3 3.0 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3960294 158043 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 3 3.0 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
89554824 159316 0 None - 0 Human 6.0 pIC50 = 6.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 464 5 1 6 4.3 CC(C)c1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
CHEMBL3971590 159316 0 None - 0 Human 6.0 pIC50 = 6.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 464 5 1 6 4.3 CC(C)c1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
89554770 150869 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3903459 150869 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554787 156688 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 455 5 1 6 3.4 NC(=O)c1cc(-c2cnn(C(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3949371 156688 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 455 5 1 6 3.4 NC(=O)c1cc(-c2cnn(C(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
89554900 157935 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 434 6 1 5 4.2 COc1c(F)cc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F nan
CHEMBL3959588 157935 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 434 6 1 5 4.2 COc1c(F)cc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F nan
89554749 158784 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
CHEMBL3966866 158784 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
89554828 166996 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OC(C)(C)C4)ccc23)cn1 nan
CHEMBL4109697 166996 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OC(C)(C)C4)ccc23)cn1 nan
89545222 167157 3 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4111091 167157 3 None - 0 Human 8.0 pIC50 = 8.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
10115228 102948 0 None - 0 Rat 8.0 pIC50 = 8.0 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 456 5 1 6 4.8 CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL260642 102948 0 None - 0 Rat 8.0 pIC50 = 8.0 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 456 5 1 6 4.8 CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
57459488 90678 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 414 5 0 5 4.9 COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206441 90678 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 414 5 0 5 4.9 COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
57459494 90679 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 414 5 0 5 4.9 COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206442 90679 0 None - 0 Human 8.0 pIC50 = 8.0 Binding
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 414 5 0 5 4.9 COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
10428048 10134 31 None - 1 Rat 7.0 pIC50 = 7.0 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
3955 10134 31 None - 1 Rat 7.0 pIC50 = 7.0 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
CHEMBL305406 10134 31 None - 1 Rat 7.0 pIC50 = 7.0 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
71566276 151202 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 381 5 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC4CF)ccc23)cn1 nan
CHEMBL3906311 151202 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 381 5 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC4CF)ccc23)cn1 nan
117642007 152509 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@](O)(c1cn(Cc2ccc3c(-c4cccnc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL3916486 152509 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@](O)(c1cn(Cc2ccc3c(-c4cccnc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
89554827 160107 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 5 3.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(C(F)(F)F)CC4)ccc23)cn1 nan
CHEMBL3978247 160107 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 5 3.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(C(F)(F)F)CC4)ccc23)cn1 nan
89554725 167604 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.9 C[C@@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
CHEMBL4114602 167604 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.9 C[C@@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
44309100 109408 0 None - 0 Rat 4.9 pIC50 = 4.9 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 297 4 0 4 4.0 CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl 10.1016/s0960-894x(99)00346-7
CHEMBL304285 109408 0 None - 0 Rat 4.9 pIC50 = 4.9 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 297 4 0 4 4.0 CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl 10.1016/s0960-894x(99)00346-7
89554830 158649 0 None - 0 Human 5.9 pIC50 = 5.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 2 5 2.5 NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3965612 158649 0 None - 0 Human 5.9 pIC50 = 5.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 2 5 2.5 NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
89554917 149914 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 2 4 3.6 CC(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
CHEMBL3895775 149914 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 2 4 3.6 CC(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
89554812 151354 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 3 5 2.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)(O)CC3)cc2n1 nan
CHEMBL3907626 151354 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 3 5 2.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)(O)CC3)cc2n1 nan
89554781 166772 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC[C@@H](F)C3)cc2n1 nan
CHEMBL4107730 166772 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC[C@@H](F)C3)cc2n1 nan
53320741 63189 0 None - 0 Rat 6.9 pIC50 = 6.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 471 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-c4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631866 63189 0 None - 0 Rat 6.9 pIC50 = 6.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 471 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-c4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
71566277 149543 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 451 5 1 5 4.6 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(C5CC5)nc(C(F)(F)F)c4)ccc23)cn1 nan
CHEMBL3892604 149543 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 451 5 1 5 4.6 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(C5CC5)nc(C(F)(F)F)c4)ccc23)cn1 nan
71566125 153828 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 6 1 4 5.1 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1 nan
CHEMBL3926942 153828 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 6 1 4 5.1 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1 nan
89554755 158647 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3965606 158647 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
89554749 158784 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
CHEMBL3966866 158784 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
89554734 166940 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@@H](C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL4109210 166940 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@@H](C(F)(F)F)C4)ccc23)cn1 nan
22224657 102947 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260636 102947 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
18548739 167144 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL411095 167144 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
156016312 184512 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 487 6 2 6 4.5 CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4642428 184512 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 487 6 2 6 4.5 CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
22317847 63184 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 420 2 1 4 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631861 63184 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 420 2 1 4 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
9952648 103083 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL261288 103083 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
18548739 167144 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL411095 167144 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
89554801 149642 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.9 C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
CHEMBL3893351 149642 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.9 C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
18548785 63180 0 None - 0 Rat 6.9 pIC50 = 6.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 415 3 2 6 3.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3nncc3CO)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631857 63180 0 None - 0 Rat 6.9 pIC50 = 6.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 415 3 2 6 3.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3nncc3CO)c1)=N2 10.1016/j.bmcl.2010.09.125
44309123 210649 0 None - 0 Rat 5.9 pIC50 = 5.9 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 365 4 0 4 5.7 Clc1ccc(/C(=C/n2cncn2)OC2CCCCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
CHEMBL68739 210649 0 None - 0 Rat 5.9 pIC50 = 5.9 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 365 4 0 4 5.7 Clc1ccc(/C(=C/n2cncn2)OC2CCCCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
71565668 157198 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC3=O)cc2n1 nan
CHEMBL3953821 157198 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC3=O)cc2n1 nan
71566518 159067 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1 nan
CHEMBL3969392 159067 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1 nan
71566202 159148 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 3 1 3 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCCC3)cc2n1 nan
CHEMBL3970177 159148 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 3 1 3 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCCC3)cc2n1 nan
53323293 63068 0 None - 0 Rat 6.9 pIC50 = 6.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629851 63068 0 None - 0 Rat 6.9 pIC50 = 6.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
71565594 149805 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 2 4 4.2 CC(C)(C)OC(=O)NCc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3894815 149805 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 2 4 4.2 CC(C)(C)OC(=O)NCc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
123632099 150180 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 426 6 1 4 4.9 [C-]#[N+]c1ccc(CCc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3897968 150180 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 426 6 1 4 4.9 [C-]#[N+]c1ccc(CCc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1 nan
89554871 150354 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 435 4 1 5 3.6 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCCC(C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3899261 150354 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 435 4 1 5 3.6 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCCC(C(F)(F)F)C4)ccc23)cn1 nan
71565883 154345 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 6 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C5CC5)C4)ccc23)cn1 nan
CHEMBL3930893 154345 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 6 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C5CC5)C4)ccc23)cn1 nan
89554967 155458 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 0 5 3.6 COC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)c(F)c2n1 nan
CHEMBL3939827 155458 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 0 5 3.6 COC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)c(F)c2n1 nan
89554841 155675 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 382 4 1 4 4.0 N#Cc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3941663 155675 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 382 4 1 4 4.0 N#Cc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554833 167574 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 4 1 6 3.9 Cc1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)sn1 nan
CHEMBL4114374 167574 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 4 1 6 3.9 Cc1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)sn1 nan
89554925 167590 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 5 1 6 3.7 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C(F)F)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4114497 167590 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 5 1 6 3.7 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C(F)F)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
9909080 162061 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 402 2 1 4 4.7 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL402886 162061 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 402 2 1 4 4.7 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
156015264 184321 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4640203 184321 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
22317724 63062 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 409 2 1 3 5.8 Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629845 63062 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 409 2 1 3 5.8 Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
11212447 63191 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 2 4 5.0 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631868 63191 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 2 4 5.0 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
22317620 63192 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 4 1 4 5.7 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631869 63192 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 4 1 4 5.7 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
53326017 63195 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 1 4 5.5 COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631872 63195 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 1 4 5.5 COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
44450454 102895 0 None - 0 Rat 6.9 pIC50 = 6.9 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 381 2 1 5 3.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Br)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260343 102895 0 None - 0 Rat 6.9 pIC50 = 6.9 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 381 2 1 5 3.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Br)cc2N1 10.1016/j.bmcl.2008.02.076
11347391 73626 0 None 2 2 Rat 6.9 pIC50 = 6.9 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 309 5 3 4 0.8 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186214 73626 0 None 2 2 Rat 6.9 pIC50 = 6.9 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 309 5 3 4 0.8 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
71566520 151326 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 287 2 1 3 3.2 Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(C#N)c1 nan
CHEMBL3907349 151326 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 287 2 1 3 3.2 Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(C#N)c1 nan
89554899 154298 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 364 4 2 4 2.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3)cc2n1 nan
CHEMBL3930631 154298 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 364 4 2 4 2.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3)cc2n1 nan
89554784 149529 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 5 3.3 COC(=O)[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3892501 149529 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 5 3.3 COC(=O)[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
156010547 183943 0 None - 0 Human 5.9 pIC50 = 5.9 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 280 1 1 4 2.4 O=c1[nH]nc2nc(-c3ccc(F)cc3)c3ccccc3n12 10.1016/j.bmcl.2020.127066
CHEMBL4634351 183943 0 None - 0 Human 5.9 pIC50 = 5.9 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 280 1 1 4 2.4 O=c1[nH]nc2nc(-c3ccc(F)cc3)c3ccccc3n12 10.1016/j.bmcl.2020.127066
117642134 153838 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 5 1 4 3.4 CO[C@H]1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
CHEMBL3927029 153838 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 5 1 4 3.4 CO[C@H]1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
44309303 210842 0 None - 0 Rat 5.9 pIC50 = 5.9 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.0 FC(F)(F)c1ccc(/C(=C/n2cncn2)OC2CCCCCC2)cc1 10.1016/s0960-894x(99)00346-7
CHEMBL70026 210842 0 None - 0 Rat 5.9 pIC50 = 5.9 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.0 FC(F)(F)c1ccc(/C(=C/n2cncn2)OC2CCCCCC2)cc1 10.1016/s0960-894x(99)00346-7
117644742 154412 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 3 1 3 3.1 COc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1 nan
CHEMBL3931394 154412 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 3 1 3 3.1 COc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1 nan
89554852 154917 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 432 4 2 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3935453 154917 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 432 4 2 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)(F)F)C3)cc2n1 nan
89554870 155018 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 5 1 6 3.2 COc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1 nan
CHEMBL3936247 155018 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 5 1 6 3.2 COc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1 nan
71566126 155561 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 2 5 4.5 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1 nan
CHEMBL3940665 155561 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 2 5 4.5 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1 nan
89554745 156369 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 2 4 4.1 Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3946940 156369 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 2 4 4.1 Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
71566207 157133 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 5 3.5 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3953157 157133 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 5 3.5 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554909 167113 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 468 5 1 6 4.1 C[C@@H]1CN(Cc2ccc3c(-c4cnc(CF)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4110690 167113 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 468 5 1 6 4.1 C[C@@H]1CN(Cc2ccc3c(-c4cnc(CF)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
89554960 167494 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 4 0 7 3.3 COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)c(F)c2n1 nan
CHEMBL4113735 167494 0 None - 0 Human 7.9 pIC50 = 7.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 4 0 7 3.3 COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)c(F)c2n1 nan
22317185 63065 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 410 2 2 4 5.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629848 63065 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 410 2 2 4 5.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
22317918 63074 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 3 2 4 5.3 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629858 63074 0 None - 0 Rat 7.9 pIC50 = 7.9 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 3 2 4 5.3 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1 10.1016/j.bmcl.2010.09.125
22448874 102073 0 None - 0 Rat 6.9 pIC50 = 6.9 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 493 5 2 6 4.3 CN(CCO)c1cc2c(cc1C#Cc1ccc(F)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL256424 102073 0 None - 0 Rat 6.9 pIC50 = 6.9 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 493 5 2 6 4.3 CN(CCO)c1cc2c(cc1C#Cc1ccc(F)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
89554836 167403 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 451 4 2 7 3.2 C[C@@H]1CN(Cc2ccc3c(-c4cnc(N)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4113073 167403 0 None - 0 Human 6.9 pIC50 = 6.9 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 451 4 2 7 3.2 C[C@@H]1CN(Cc2ccc3c(-c4cnc(N)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
156017916 184584 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4cccc(F)c4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4643527 184584 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4cccc(F)c4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554840 157293 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 3 0 5 4.5 Cn1cc(-c2cc(C#N)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1 nan
CHEMBL3954534 157293 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 3 0 5 4.5 Cn1cc(-c2cc(C#N)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1 nan
89554892 157380 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL3955188 157380 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 10.1021/acs.jmedchem.8b01266
71566275 158419 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC45CC5)ccc23)cn1 nan
CHEMBL3963813 158419 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC45CC5)ccc23)cn1 nan
117642068 161054 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 5 2.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)CC4)ccc23)cn1 nan
CHEMBL3986471 161054 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 5 2.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)CC4)ccc23)cn1 nan
71566522 156122 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 266 2 1 2 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3945170 156122 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 266 2 1 2 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1 10.1016/j.bmcl.2020.127066
49765871 8926 45 None - 1 Human 7.8 pIC50 = 7.8 Binding
Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
6317 8926 45 None - 1 Human 7.8 pIC50 = 7.8 Binding
Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
CHEMBL2179319 8926 45 None - 1 Human 7.8 pIC50 = 7.8 Binding
Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
89554911 149772 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
CHEMBL3894556 149772 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
89554889 151582 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 368 4 1 6 2.6 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C#N)c4)ccc23)cn1 nan
CHEMBL3909377 151582 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 368 4 1 6 2.6 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C#N)c4)ccc23)cn1 nan
89554788 153161 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)cc2n1 nan
CHEMBL3921588 153161 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)cc2n1 nan
89554753 153552 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3924490 153552 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
117642146 155266 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 472 6 2 5 4.5 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3938177 155266 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 472 6 2 5 4.5 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
71566048 157503 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1 nan
CHEMBL3956202 157503 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1 nan
89554977 157920 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 5 2 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccc(CO)nc3)c(F)c2n1 nan
CHEMBL3959505 157920 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 5 2 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccc(CO)nc3)c(F)c2n1 nan
117641924 159186 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3970507 159186 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
71565961 160274 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 5 1 6 3.0 CCn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3979694 160274 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 5 1 6 3.0 CCn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1 nan
124201730 167181 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 2 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@H](O)Cc3ccc(Cl)nc3)cc2n1 nan
CHEMBL4111267 167181 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 2 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@H](O)Cc3ccc(Cl)nc3)cc2n1 nan
44434257 158206 0 None - 0 Rat 5.8 pIC50 = 5.8 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 318 1 1 2 4.5 Cc1ccc2c(c1)NC(=O)CC(c1cccc(C(F)(F)F)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL396181 158206 0 None - 0 Rat 5.8 pIC50 = 5.8 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 318 1 1 2 4.5 Cc1ccc2c(c1)NC(=O)CC(c1cccc(C(F)(F)F)c1)=N2 10.1016/j.bmcl.2007.10.026
22224695 95479 0 None - 0 Rat 6.8 pIC50 = 6.8 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 1 1 2 5.2 O=C1CC(c2cccc(I)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
CHEMBL236035 95479 0 None - 0 Rat 6.8 pIC50 = 6.8 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 1 1 2 5.2 O=C1CC(c2cccc(I)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
89543901 157353 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3955040 157353 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
71565963 159491 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 487 5 1 6 3.5 NC(=O)c1cc(-c2cnn(CC(F)(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3973004 159491 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 487 5 1 6 3.5 NC(=O)c1cc(-c2cnn(CC(F)(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
89554753 153552 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3924490 153552 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
89554752 154161 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3929631 154161 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
71565525 156695 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 363 4 1 4 2.9 NC(=O)c1cc(C2=CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3949476 156695 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 363 4 1 4 2.9 NC(=O)c1cc(C2=CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
71566048 157503 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1 nan
CHEMBL3956202 157503 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1 nan
89554891 167439 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1 nan
CHEMBL4113348 167439 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1 nan
9952648 103083 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261288 103083 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
9952648 103083 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL261288 103083 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
89554732 166949 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4109248 166949 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
156017027 184506 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4642338 184506 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F 10.1016/j.bmcl.2020.127066
53325611 63190 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 485 4 1 3 7.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631867 63190 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 485 4 1 3 7.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
22448864 95957 0 None - 0 Rat 6.8 pIC50 = 6.8 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 494 2 1 6 3.7 N#Cc1cccc(C2=Nc3cc(N4CCS(=O)(=O)CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236669 95957 0 None - 0 Rat 6.8 pIC50 = 6.8 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 494 2 1 6 3.7 N#Cc1cccc(C2=Nc3cc(N4CCS(=O)(=O)CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554793 153119 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 2 4 4.0 CC(C)(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
CHEMBL3921230 153119 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 2 4 4.0 CC(C)(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
89554846 149927 0 None - 0 Human 5.8 pIC50 = 5.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 1 6 3.1 Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)o1 nan
CHEMBL3895854 149927 0 None - 0 Human 5.8 pIC50 = 5.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 1 6 3.1 Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)o1 nan
89545189 159674 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1 nan
CHEMBL3974648 159674 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1 nan
71565885 160213 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 6 1 7 1.6 COCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL3979211 160213 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 6 1 7 1.6 COCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
89554890 167644 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL4114982 167644 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
71566522 156122 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 266 2 1 2 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1 nan
CHEMBL3945170 156122 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 266 2 1 2 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1 nan
89554932 156698 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 2.8 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCC(F)CC4)ccc23)cn1 nan
CHEMBL3949512 156698 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 2.8 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCC(F)CC4)ccc23)cn1 nan
71566349 160947 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 326 2 1 2 3.8 NC(=O)c1cc(-c2ccc(Br)cc2)c2ccccc2n1 nan
CHEMBL3985577 160947 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 326 2 1 2 3.8 NC(=O)c1cc(-c2ccc(Br)cc2)c2ccccc2n1 nan
89554829 149729 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL3894162 149729 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
71565596 151570 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.3 CC1CCC(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 nan
CHEMBL3909273 151570 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.3 CC1CCC(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 nan
89554881 155027 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1 nan
CHEMBL3936318 155027 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1 nan
89554933 158202 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 490 6 2 5 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
CHEMBL3961788 158202 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 490 6 2 5 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
22224852 102639 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259054 102639 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
18548908 103039 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 404 2 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261051 103039 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 404 2 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
22224670 103042 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 415 3 1 5 4.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261081 103042 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 415 3 1 5 4.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
89554950 154997 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 443 5 1 5 4.5 Cc1cn(C2CCN(Cc3ccc4c(-c5ccc(F)cc5)cc(C(N)=O)nc4c3)CC2)cn1 nan
CHEMBL3936050 154997 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 443 5 1 5 4.5 Cc1cn(C2CCN(Cc3ccc4c(-c5ccc(F)cc5)cc(C(N)=O)nc4c3)CC2)cn1 nan
117642183 160154 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 354 4 0 4 4.5 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 nan
CHEMBL3978639 160154 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 354 4 0 4 4.5 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 nan
22224972 104471 0 None - 0 Rat 6.8 pIC50 = 6.8 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 430 2 1 4 5.4 Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)c(C)n1 10.1016/j.bmcl.2007.12.005
CHEMBL271319 104471 0 None - 0 Rat 6.8 pIC50 = 6.8 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 430 2 1 4 5.4 Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)c(C)n1 10.1016/j.bmcl.2007.12.005
11503055 9179 3 None - 0 Human 4.8 pIC50 = 4.8 Binding
Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1016/j.bmcl.2012.04.112
9694 9179 3 None - 0 Human 4.8 pIC50 = 4.8 Binding
Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1016/j.bmcl.2012.04.112
CHEMBL2204436 9179 3 None - 0 Human 4.8 pIC50 = 4.8 Binding
Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1016/j.bmcl.2012.04.112
71566435 159433 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 318 2 1 2 3.9 NC(=O)c1cc(-c2c(F)cc(Cl)cc2F)c2ccccc2n1 nan
CHEMBL3972482 159433 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 318 2 1 2 3.9 NC(=O)c1cc(-c2c(F)cc(Cl)cc2F)c2ccccc2n1 nan
89554799 167575 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCN4CCC[C@@H]4C3)cc2n1 nan
CHEMBL4114381 167575 0 None - 0 Human 6.8 pIC50 = 6.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCN4CCC[C@@H]4C3)cc2n1 nan
89554919 150568 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 435 4 1 6 3.2 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3901084 150568 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 435 4 1 6 3.2 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C(F)(F)F)C4)ccc23)cn1 nan
71566204 155471 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 1 4 4.1 COc1cc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)ccn1 nan
CHEMBL3939934 155471 0 None - 0 Human 7.8 pIC50 = 7.8 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 1 4 4.1 COc1cc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)ccn1 nan
22448830 96212 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 416 3 1 5 4.3 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL237091 96212 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 416 3 1 5 4.3 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
22448689 104331 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 457 4 1 6 4.6 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL270616 104331 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 457 4 1 6 4.6 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
22317408 63067 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629850 63067 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11211597 63082 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629865 63082 0 None - 0 Rat 7.8 pIC50 = 7.8 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
89554780 152161 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 3 4.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3C(F)(F)F)cc2n1 nan
CHEMBL3913806 152161 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 3 4.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3C(F)(F)F)cc2n1 nan
89554777 152075 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 2 4 2.9 CC(=O)NC1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
CHEMBL3913090 152075 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 2 4 2.9 CC(=O)NC1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
89554839 160171 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 445 5 1 6 3.3 NC(=O)c1cc(-c2cnn(C3CC3)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3978791 160171 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 445 5 1 6 3.3 NC(=O)c1cc(-c2cnn(C3CC3)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
89554772 151569 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 5 1 5 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4ccccn4)nc4ccccc43)cc2n1 nan
CHEMBL3909260 151569 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 5 1 5 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4ccccn4)nc4ccccc43)cc2n1 nan
89554745 156369 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 2 4 4.1 Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3946940 156369 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 2 4 4.1 Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554794 159178 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 5 1 3 5.2 Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3970463 159178 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 5 1 3 5.2 Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554732 166949 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL4109248 166949 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
10297067 103079 0 None - 0 Rat 7.7 pIC50 = 7.7 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 441 5 2 5 5.4 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL261263 103079 0 None - 0 Rat 7.7 pIC50 = 7.7 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 441 5 2 5 5.4 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
156016312 184512 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 487 6 2 6 4.5 CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4642428 184512 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 487 6 2 6 4.5 CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
156018942 184649 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 507 6 2 6 4.6 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4644424 184649 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 507 6 2 6 4.6 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554861 156603 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 287 2 1 3 3.2 Cc1ccc2c(-c3ccc(C#N)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3948794 156603 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 287 2 1 3 3.2 Cc1ccc2c(-c3ccc(C#N)cc3)cc(C(N)=O)nc2c1 nan
71565804 150693 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 444 6 2 5 4.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CCCC4)cn3)cc2n1 nan
CHEMBL3902047 150693 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 444 6 2 5 4.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CCCC4)cn3)cc2n1 nan
89554886 166661 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL4106809 166661 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
11158623 10124 11 None 8 2 Rat 8.7 pIC50 = 8.7 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
6226 10124 11 None 8 2 Rat 8.7 pIC50 = 8.7 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
CHEMBL1629855 10124 11 None 8 2 Rat 8.7 pIC50 = 8.7 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
11351088 63072 0 None - 0 Rat 8.7 pIC50 = 8.7 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.4 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629856 63072 0 None - 0 Rat 8.7 pIC50 = 8.7 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.4 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
22317928 63073 0 None - 0 Rat 8.7 pIC50 = 8.7 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 449 3 1 3 6.7 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629857 63073 0 None - 0 Rat 8.7 pIC50 = 8.7 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 449 3 1 3 6.7 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1 10.1016/j.bmcl.2010.09.125
11406781 63199 0 None - 0 Rat 8.7 pIC50 = 8.7 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631876 63199 0 None - 0 Rat 8.7 pIC50 = 8.7 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
1378 9195 54 None -2 10 Human 8.5 pIC50 = 8.5 Binding
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmc.2008.02.066
1399 9195 54 None -2 10 Human 8.5 pIC50 = 8.5 Binding
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmc.2008.02.066
9819927 9195 54 None -2 10 Human 8.5 pIC50 = 8.5 Binding
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmc.2008.02.066
CHEMBL432038 9195 54 None -2 10 Human 8.5 pIC50 = 8.5 Binding
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmc.2008.02.066
89554746 150533 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 5 1 3 4.9 CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3900813 150533 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 5 1 3 4.9 CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554931 154334 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 5 1 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cnc(C4CC4)nc3)c(F)c2n1 nan
CHEMBL3930820 154334 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 5 1 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cnc(C4CC4)nc3)c(F)c2n1 nan
1397 9307 15 None -1 5 Rat 7.7 pIC50 = 7.7 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
9886034 9307 15 None -1 5 Rat 7.7 pIC50 = 7.7 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186453 9307 15 None -1 5 Rat 7.7 pIC50 = 7.7 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
22224970 162271 0 None - 0 Rat 7.7 pIC50 = 7.7 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL404080 162271 0 None - 0 Rat 7.7 pIC50 = 7.7 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1 10.1016/j.bmcl.2007.12.005
135544097 162444 0 None - 0 Rat 7.7 pIC50 = 7.7 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 437 2 2 6 4.0 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL404886 162444 0 None - 0 Rat 7.7 pIC50 = 7.7 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 437 2 2 6 4.0 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
22317715 63071 0 None - 0 Rat 7.7 pIC50 = 7.7 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629854 63071 0 None - 0 Rat 7.7 pIC50 = 7.7 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
9885546 117315 0 None - 1 Human 6.7 pIC50 = 6.7 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
CHEMBL325140 117315 0 None - 1 Human 6.7 pIC50 = 6.7 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
1378 9195 54 None -2 10 Human 6.7 pIC50 = 6.7 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(01)00656-4
1399 9195 54 None -2 10 Human 6.7 pIC50 = 6.7 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(01)00656-4
9819927 9195 54 None -2 10 Human 6.7 pIC50 = 6.7 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(01)00656-4
CHEMBL432038 9195 54 None -2 10 Human 6.7 pIC50 = 6.7 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(01)00656-4
44309302 210841 0 None - 0 Rat 5.7 pIC50 = 5.7 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 345 5 0 4 4.8 Clc1cccc(Cl)c1/C(=C/n1cncn1)OCc1ccccc1 10.1016/s0960-894x(99)00346-7
CHEMBL70025 210841 0 None - 0 Rat 5.7 pIC50 = 5.7 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 345 5 0 4 4.8 Clc1cccc(Cl)c1/C(=C/n1cncn1)OCc1ccccc1 10.1016/s0960-894x(99)00346-7
89554729 153173 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 514 8 2 7 4.4 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(OC)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3921665 153173 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 514 8 2 7 4.4 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(OC)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
121447916 176727 3 None - 0 Human 6.7 pIC50 = 6.7 Binding
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 409 4 1 5 2.8 C[C@H]1CN(Cc2ccc3c(c2)c(=O)c(C(N)=O)cn3-c2ccc(F)cc2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
CHEMBL4441595 176727 3 None - 0 Human 6.7 pIC50 = 6.7 Binding
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 409 4 1 5 2.8 C[C@H]1CN(Cc2ccc3c(c2)c(=O)c(C(N)=O)cn3-c2ccc(F)cc2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
66791078 149452 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 489 6 2 6 4.5 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL3891986 149452 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 489 6 2 6 4.5 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
89554746 150533 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 5 1 3 4.9 CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3900813 150533 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 5 1 3 4.9 CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
71566596 150924 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 4 1 4 2.5 CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3903901 150924 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 4 1 4 2.5 CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
89554855 153320 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 1 6 2.9 COc1ncccc1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1F nan
CHEMBL3922719 153320 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 1 6 2.9 COc1ncccc1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1F nan
89554970 153992 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 4 0 7 3.3 COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)c(F)c2n1 nan
CHEMBL3928272 153992 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 4 0 7 3.3 COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)c(F)c2n1 nan
71566599 154084 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 3.8 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1 nan
CHEMBL3929001 154084 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 3.8 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1 nan
89554806 155996 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CCC(O)(c1nnnn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(F)(F)F nan
CHEMBL3944124 155996 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CCC(O)(c1nnnn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(F)(F)F nan
89554883 156980 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 1 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2cc(F)c(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3951983 156980 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 1 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2cc(F)c(CN3C(=O)CCC3=O)cc2n1 nan
71566130 158660 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 384 5 1 6 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(C5CC5)nc4)ccc23)cn1 nan
CHEMBL3965748 158660 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 384 5 1 6 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(C5CC5)nc4)ccc23)cn1 nan
89554794 159178 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 5 1 3 5.2 Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3970463 159178 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 5 1 3 5.2 Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554759 166825 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL4108213 166825 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
71566672 159608 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 391 4 1 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3973949 159608 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 391 4 1 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
22224962 103078 0 None - 0 Rat 6.7 pIC50 = 6.7 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 342 3 1 4 4.2 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C3CC3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261251 103078 0 None - 0 Rat 6.7 pIC50 = 6.7 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 342 3 1 4 4.2 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C3CC3)cc2N1 10.1016/j.bmcl.2008.02.076
11559750 102730 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O 10.1016/j.bmc.2008.02.066
CHEMBL259435 102730 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O 10.1016/j.bmc.2008.02.066
89554860 152149 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 2 6 1.7 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4C(=O)NC(C)(C)C4=O)ccc23)cn1 nan
CHEMBL3913733 152149 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 2 6 1.7 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4C(=O)NC(C)(C)C4=O)ccc23)cn1 nan
71566519 160622 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 292 3 1 3 3.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1 nan
CHEMBL3982696 160622 0 None - 0 Human 6.7 pIC50 = 6.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 292 3 1 3 3.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1 nan
89554797 149893 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 398 6 1 5 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1 nan
CHEMBL3895570 149893 0 None - 0 Human 7.7 pIC50 = 7.7 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 398 6 1 5 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1 nan
22448579 162557 0 None - 0 Rat 7.7 pIC50 = 7.7 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 412 3 2 5 4.8 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL405895 162557 0 None - 0 Rat 7.7 pIC50 = 7.7 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 412 3 2 5 4.8 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
11084869 96828 2 None - 1 Human 7.7 pIC50 = 7.7 Binding
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL2381643 96828 2 None - 1 Human 7.7 pIC50 = 7.7 Binding
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
11405687 73231 0 None 2 2 Rat 7.6 pIC50 = 7.6 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185210 73231 0 None 2 2 Rat 7.6 pIC50 = 7.6 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
117646988 156260 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 4 1 5 2.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COCC3=O)cc2n1 nan
CHEMBL3946311 156260 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 4 1 5 2.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COCC3=O)cc2n1 nan
10192719 72888 0 None 2 2 Rat 6.6 pIC50 = 6.6 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 233 3 3 4 -0.8 CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL183956 72888 0 None 2 2 Rat 6.6 pIC50 = 6.6 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 233 3 3 4 -0.8 CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
89554911 149772 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
CHEMBL3894556 149772 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
71565881 149803 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 380 4 1 4 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3Cl)cc2n1 nan
CHEMBL3894799 149803 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 380 4 1 4 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3Cl)cc2n1 nan
71566672 159608 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 4 1 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1 nan
CHEMBL3973949 159608 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 4 1 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1 nan
89554767 160194 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3978978 160194 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
9891158 162365 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 476 6 1 6 4.8 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL404463 162365 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 476 6 1 6 4.8 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
22317491 63070 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629853 63070 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
1378 9195 54 None -1 10 Rat 7.6 pIC50 = 7.6 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
1399 9195 54 None -1 10 Rat 7.6 pIC50 = 7.6 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
9819927 9195 54 None -1 10 Rat 7.6 pIC50 = 7.6 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
CHEMBL432038 9195 54 None -1 10 Rat 7.6 pIC50 = 7.6 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
89554965 151301 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 432 4 2 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3C(F)(F)F)cc2n1 nan
CHEMBL3907125 151301 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 432 4 2 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3C(F)(F)F)cc2n1 nan
89554894 156884 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4(C)C)ccc23)cn1 nan
CHEMBL3951081 156884 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4(C)C)ccc23)cn1 nan
89554916 160708 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC5(CC5)C4)ccc23)cn1 nan
CHEMBL3983396 160708 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC5(CC5)C4)ccc23)cn1 nan
156014599 183952 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 1 6 5.0 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(C)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4634754 183952 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 1 6 5.0 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(C)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554911 149772 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
CHEMBL3894556 149772 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
71565884 150203 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 4 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3898121 150203 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 4 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
71565736 159352 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CCC(O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F nan
CHEMBL3971819 159352 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CCC(O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F nan
89554728 159653 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 6 1 6 3.0 CC(C)CC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL3974406 159653 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 6 1 6 3.0 CC(C)CC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
89554776 159932 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 478 5 1 4 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(CC(F)(F)F)nc4ccccc43)cc2n1 nan
CHEMBL3976706 159932 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 478 5 1 4 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(CC(F)(F)F)nc4ccccc43)cc2n1 nan
11257636 175151 0 None 1 2 Rat 7.6 pIC50 = 7.6 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 385 6 3 4 2.4 N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL434536 175151 0 None 1 2 Rat 7.6 pIC50 = 7.6 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 385 6 3 4 2.4 N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
22448659 161381 0 None - 0 Rat 5.6 pIC50 = 5.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 434 4 2 5 3.3 N#Cc1cccc(C2=Nc3cc(OCC(N)=O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL399186 161381 0 None - 0 Rat 5.6 pIC50 = 5.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 434 4 2 5 3.3 N#Cc1cccc(C2=Nc3cc(OCC(N)=O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89555004 150409 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 7 1 4 3.2 COCCN(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3899807 150409 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 7 1 4 3.2 COCCN(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554821 154128 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 5 2.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)C4)ccc23)cn1 nan
CHEMBL3929361 154128 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 5 2.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)C4)ccc23)cn1 nan
89554837 154617 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC5(CC4)CC5)ccc23)cn1 nan
CHEMBL3933004 154617 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC5(CC4)CC5)ccc23)cn1 nan
117641885 149794 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@H](C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3894759 149794 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@H](C(F)(F)F)C4)ccc23)cn1 nan
89554923 153224 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 4 1 5 3.3 Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cc(C)n1 nan
CHEMBL3922052 153224 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 4 1 5 3.3 Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cc(C)n1 nan
89554968 156366 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 4 1 5 3.4 CC1(C)OC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3946909 156366 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 4 1 5 3.4 CC1(C)OC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
89554820 156653 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 5 3.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3949126 156653 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 5 3.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(C(F)(F)F)C4)ccc23)cn1 nan
89554792 157176 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 5 2 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1 nan
CHEMBL3953648 157176 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 5 2 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1 nan
89554765 158242 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cncn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3962095 158242 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cncn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
22224729 102904 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(F)c3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260415 102904 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(F)c3)cc2N1 10.1016/j.bmcl.2008.02.076
156020940 184886 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 489 6 2 6 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4647980 184886 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 489 6 2 6 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554884 149986 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL3896344 149986 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
89554835 156301 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 4 2.9 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1 nan
CHEMBL3946509 156301 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 4 2.9 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1 nan
44309103 109650 0 None - 0 Rat 5.6 pIC50 = 5.6 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 323 4 0 4 4.5 Clc1ccc(/C(=C/n2cncn2)OC2CCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
CHEMBL305799 109650 0 None - 0 Rat 5.6 pIC50 = 5.6 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 323 4 0 4 4.5 Clc1ccc(/C(=C/n2cncn2)OC2CCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
9845873 167578 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL411440 167578 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
44434259 95429 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 336 1 1 2 4.5 O=C1CC(c2ccccc2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
CHEMBL235806 95429 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 336 1 1 2 4.5 O=C1CC(c2ccccc2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
22448890 96094 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 490 4 2 5 4.7 CC(C)(C)NC(=O)COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL236883 96094 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 490 4 2 5 4.7 CC(C)(C)NC(=O)COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
9845873 167578 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL411440 167578 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
9845873 167578 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL411440 167578 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
22317318 63198 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631875 63198 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
9845873 167578 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL411440 167578 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
89554791 166623 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 2 5 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cn[nH]c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4106552 166623 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 2 5 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cn[nH]c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
22224765 95534 0 None - 0 Rat 4.6 pIC50 = 4.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 343 1 2 4 3.1 CC(C)(O)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL236258 95534 0 None - 0 Rat 4.6 pIC50 = 4.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 343 1 2 4 3.1 CC(C)(O)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
71565962 156419 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 462 5 1 6 4.1 NC(=O)c1cc(-c2cnc(C3CC3)s2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3947299 156419 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 462 5 1 6 4.1 NC(=O)c1cc(-c2cnc(C3CC3)s2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
22224583 161382 0 None - 0 Rat 6.6 pIC50 = 6.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 404 1 1 2 5.6 O=C1CC(c2cccc(C(F)(F)F)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
CHEMBL399187 161382 0 None - 0 Rat 6.6 pIC50 = 6.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 404 1 1 2 5.6 O=C1CC(c2cccc(C(F)(F)F)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
44309086 210713 0 None - 0 Rat 5.6 pIC50 = 5.6 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 346 5 0 5 4.2 Clc1ccc(/C(=C/n2cnnn2)OCc2ccccc2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
CHEMBL69204 210713 0 None - 0 Rat 5.6 pIC50 = 5.6 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 346 5 0 5 4.2 Clc1ccc(/C(=C/n2cnnn2)OCc2ccccc2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
71566597 156651 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 1 4 3.4 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3949122 156651 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 1 4 3.4 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
89554867 156863 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 1 5 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1C nan
CHEMBL3950864 156863 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 1 5 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1C nan
71565671 157288 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 389 5 1 5 2.7 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1 nan
CHEMBL3954513 157288 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 389 5 1 5 2.7 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1 nan
89554775 160614 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 476 5 2 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(S(=O)(=O)O)nc4ccccc43)cc2n1 nan
CHEMBL3982636 160614 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 476 5 2 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(S(=O)(=O)O)nc4ccccc43)cc2n1 nan
18548766 102638 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 405 2 1 5 4.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259053 102638 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 405 2 1 5 4.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
156019727 184771 0 None - 0 Human 5.6 pIC50 = 5.6 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 497 7 2 6 4.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(C(C)C)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4646222 184771 0 None - 0 Human 5.6 pIC50 = 5.6 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 497 7 2 6 4.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(C(C)C)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554914 167393 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.2 Cc1c(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)cnn1C nan
CHEMBL4112966 167393 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.2 Cc1c(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)cnn1C nan
89554778 150131 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 408 5 3 5 1.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC(O)CC3C(N)=O)cc2n1 nan
CHEMBL3897537 150131 0 None - 0 Human 6.6 pIC50 = 6.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 408 5 3 5 1.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC(O)CC3C(N)=O)cc2n1 nan
53320742 63194 0 None - 0 Rat 6.6 pIC50 = 6.6 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 452 4 1 4 5.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CN(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631871 63194 0 None - 0 Rat 6.6 pIC50 = 6.6 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 452 4 1 4 5.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CN(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
9868835 155731 0 None - 0 Rat 6.6 pIC50 = 6.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 459 2 1 5 4.2 CN1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1 10.1016/j.bmcl.2007.10.026
CHEMBL394201 155731 0 None - 0 Rat 6.6 pIC50 = 6.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 459 2 1 5 4.2 CN1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1 10.1016/j.bmcl.2007.10.026
89554888 149387 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccc(C(F)(F)F)n4)ccc23)cn1 nan
CHEMBL3891468 149387 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccc(C(F)(F)F)n4)ccc23)cn1 nan
89554859 156806 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 4 1 5 3.9 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C(F)(F)F)nc4)ccc23)cn1 nan
CHEMBL3950438 156806 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 4 1 5 3.9 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C(F)(F)F)nc4)ccc23)cn1 nan
71565521 157263 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 4 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CC4(CCCC4)C3=O)cc2n1 nan
CHEMBL3954371 157263 0 None - 0 Human 7.6 pIC50 = 7.6 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 4 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CC4(CCCC4)C3=O)cc2n1 nan
22448614 96092 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 435 5 1 5 4.4 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL236881 96092 0 None - 0 Rat 7.6 pIC50 = 7.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 435 5 1 5 4.4 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
44434256 95380 0 None - 0 Rat 5.6 pIC50 = 5.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 284 1 1 2 4.1 Cc1ccc2c(c1)NC(=O)CC(c1cccc(Cl)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL235599 95380 0 None - 0 Rat 5.6 pIC50 = 5.6 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 284 1 1 2 4.1 Cc1ccc2c(c1)NC(=O)CC(c1cccc(Cl)c1)=N2 10.1016/j.bmcl.2007.10.026
71565526 158225 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(C2CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3961948 158225 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(C2CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
18548910 102709 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 401 3 1 6 3.8 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL259340 102709 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 401 3 1 6 3.8 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
22317258 63197 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 480 3 1 5 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(N4CCOCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631874 63197 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 480 3 1 5 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(N4CCOCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
11279365 74334 0 None 1 2 Rat 7.5 pIC50 = 7.5 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL189814 74334 0 None 1 2 Rat 7.5 pIC50 = 7.5 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
44434258 95381 0 None - 0 Rat 5.5 pIC50 = 5.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 275 1 1 3 3.3 Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL235600 95381 0 None - 0 Rat 5.5 pIC50 = 5.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 275 1 1 3 3.3 Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
11158623 10124 11 None -8 2 Human 6.5 pIC50 = 6.5 Binding
Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2012.04.112
6226 10124 11 None -8 2 Human 6.5 pIC50 = 6.5 Binding
Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2012.04.112
CHEMBL1629855 10124 11 None -8 2 Human 6.5 pIC50 = 6.5 Binding
Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2012.04.112
11158623 10124 11 None -8 2 Human 6.5 pIC50 = 6.5 Binding
Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1021/jm400439t
6226 10124 11 None -8 2 Human 6.5 pIC50 = 6.5 Binding
Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1021/jm400439t
CHEMBL1629855 10124 11 None -8 2 Human 6.5 pIC50 = 6.5 Binding
Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1021/jm400439t
89543886 155553 0 None - 0 Human 6.5 pIC50 = 6.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 363 3 1 3 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCC3)cc2n1 nan
CHEMBL3940628 155553 0 None - 0 Human 6.5 pIC50 = 6.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 363 3 1 3 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCC3)cc2n1 nan
44452714 166047 0 None - 0 Human 8.5 pIC50 = 8.5 Binding
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 N[C@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@]1(F)C(=O)O 10.1016/j.bmc.2008.02.066
CHEMBL409928 166047 0 None - 0 Human 8.5 pIC50 = 8.5 Binding
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 N[C@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@]1(F)C(=O)O 10.1016/j.bmc.2008.02.066
71566669 152262 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 5 1 4 3.8 CCC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3914560 152262 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 5 1 4 3.8 CCC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
89554938 153453 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C5CC5)nc4)ccc23)cn1 nan
CHEMBL3923798 153453 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C5CC5)nc4)ccc23)cn1 nan
89554823 155811 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)(F)C4)ccc23)cn1 nan
CHEMBL3942629 155811 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)(F)C4)ccc23)cn1 nan
22224615 96839 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 1 1 3 4.6 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL238167 96839 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 1 1 3 4.6 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
22224975 95532 0 None - 0 Rat 6.5 pIC50 = 6.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 368 1 1 5 3.9 N#Cc1cccc(C2=Nc3ccc(C#Cc4nccs4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236256 95532 0 None - 0 Rat 6.5 pIC50 = 6.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 368 1 1 5 3.9 N#Cc1cccc(C2=Nc3ccc(C#Cc4nccs4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
10359073 161753 1 None -2 2 Human 5.5 pIC50 = 5.5 Binding
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm980571q
CHEMBL40123 161753 1 None -2 2 Human 5.5 pIC50 = 5.5 Binding
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm980571q
89554903 159429 0 None - 0 Human 5.5 pIC50 = 5.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 345 3 0 3 4.0 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1 nan
CHEMBL3972456 159429 0 None - 0 Human 5.5 pIC50 = 5.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 345 3 0 3 4.0 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1 nan
71566274 153670 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 4 1 3 4.4 Cc1ccncc1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3925507 153670 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 4 1 3 4.4 Cc1ccncc1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
71565738 157043 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 6 1 5 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)C4CC4)cn3)cc2n1 nan
CHEMBL3952509 157043 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 6 1 5 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)C4CC4)cn3)cc2n1 nan
71565805 159097 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
CHEMBL3969686 159097 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
71566206 160426 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 1 4 4.1 COc1cncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
CHEMBL3981039 160426 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 1 4 4.1 COc1cncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
89554764 160734 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 4 4.5 CC(C)c1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3983614 160734 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 4 4.5 CC(C)c1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
22224825 165773 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL409638 165773 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
44309101 210343 0 None - 0 Rat 5.5 pIC50 = 5.5 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 278 6 0 5 3.1 CCCCO/C(=C\n1ncnn1)c1ccc(Cl)cc1 10.1016/s0960-894x(99)00346-7
CHEMBL66701 210343 0 None - 0 Rat 5.5 pIC50 = 5.5 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 278 6 0 5 3.1 CCCCO/C(=C\n1ncnn1)c1ccc(Cl)cc1 10.1016/s0960-894x(99)00346-7
22224682 96384 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 367 1 1 4 4.5 N#Cc1cccc(C2=Nc3ccc(C#Cc4cccs4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL237523 96384 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 367 1 1 4 4.5 N#Cc1cccc(C2=Nc3ccc(C#Cc4cccs4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554733 149318 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 5 1 7 3.2 COc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
CHEMBL3890866 149318 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 5 1 7 3.2 COc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
71566126 155561 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 2 5 4.5 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1 nan
CHEMBL3940665 155561 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 2 5 4.5 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1 nan
89554774 160655 0 None - 0 Human 6.5 pIC50 = 6.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 5 1 4 3.3 CN(C)C1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
CHEMBL3982968 160655 0 None - 0 Human 6.5 pIC50 = 6.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 5 1 4 3.3 CN(C)C1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
89543925 159204 0 None - 0 Human 6.5 pIC50 = 6.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 284 2 1 2 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2cccc(F)c2n1 nan
CHEMBL3970688 159204 0 None - 0 Human 6.5 pIC50 = 6.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 284 2 1 2 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2cccc(F)c2n1 nan
89554911 149772 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
CHEMBL3894556 149772 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
89554971 154062 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 6 2.8 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(Cl)nc4)ccc23)cn1 nan
CHEMBL3928860 154062 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 6 2.8 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(Cl)nc4)ccc23)cn1 nan
9820321 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
9820321 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2008.02.076
CHEMBL401446 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
CHEMBL401446 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2008.02.076
22224841 96838 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 1 1 3 4.6 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL238166 96838 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 1 1 3 4.6 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
9820321 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL401446 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
9820321 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
CHEMBL401446 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
9820321 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
CHEMBL401446 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
44285839 106928 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 353 4 3 4 2.9 CC1c2ccccc2Oc2cccc([C@@](N)(C(=O)O)[C@H]3C[C@@H]3C(=O)O)c21 10.1021/jm980571q
CHEMBL287831 106928 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 353 4 3 4 2.9 CC1c2ccccc2Oc2cccc([C@@](N)(C(=O)O)[C@H]3C[C@@H]3C(=O)O)c21 10.1021/jm980571q
9820321 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
CHEMBL401446 161787 0 None - 0 Rat 7.5 pIC50 = 7.5 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
117642059 150487 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 428 4 1 4 4.5 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccc(F)c(C(F)(F)F)c4)ccc23)cn1 nan
CHEMBL3900371 150487 0 None - 0 Human 7.5 pIC50 = 7.5 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 428 4 1 4 4.5 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccc(F)c(C(F)(F)F)c4)ccc23)cn1 nan
53318106 63178 0 None - 0 Rat 6.5 pIC50 = 6.5 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 4 5.1 Cc1nc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)co1 10.1016/j.bmcl.2010.09.125
CHEMBL1631855 63178 0 None - 0 Rat 6.5 pIC50 = 6.5 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 4 5.1 Cc1nc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)co1 10.1016/j.bmcl.2010.09.125
22224908 95526 0 None - 0 Rat 6.5 pIC50 = 6.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 2 2 3 3.6 NC(=O)c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236244 95526 0 None - 0 Rat 6.5 pIC50 = 6.5 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 2 2 3 3.6 NC(=O)c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
117642047 149312 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 6 2 6 3.9 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL3890814 149312 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 6 2 6 3.9 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
89554868 156121 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 402 5 1 6 3.1 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4cnc(C5CC5)nc4)ccc23)cn1 nan
CHEMBL3945166 156121 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 402 5 1 6 3.1 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4cnc(C5CC5)nc4)ccc23)cn1 nan
10204007 104293 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 446 3 1 6 4.2 CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL270402 104293 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 446 3 1 6 4.2 CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2007.12.005
89554759 166825 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4108213 166825 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
156015207 184352 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4640529 184352 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
22224803 96690 0 None - 0 Rat 6.4 pIC50 = 6.4 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 449 2 1 4 4.0 O=C1CC(c2cccc(C(=O)N3CCOCC3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
CHEMBL237938 96690 0 None - 0 Rat 6.4 pIC50 = 6.4 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 449 2 1 4 4.0 O=C1CC(c2cccc(C(=O)N3CCOCC3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
156013741 184045 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 282 1 1 4 2.3 O=c1[nH]nc2ccccccc(-c3ccc(F)cc3)nn12 10.1016/j.bmcl.2020.127066
CHEMBL4636186 184045 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 282 1 1 4 2.3 O=c1[nH]nc2ccccccc(-c3ccc(F)cc3)nn12 10.1016/j.bmcl.2020.127066
71566438 159640 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 2 1 2 4.0 Cc1cc(Cl)ccc1-c1cc(C(N)=O)nc2ccccc12 nan
CHEMBL3974279 159640 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 2 1 2 4.0 Cc1cc(Cl)ccc1-c1cc(C(N)=O)nc2ccccc12 nan
89554845 153187 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 2 1 2 4.0 Cc1ccc2c(-c3ccccc3Cl)cc(C(N)=O)nc2c1 nan
CHEMBL3921799 153187 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 2 1 2 4.0 Cc1ccc2c(-c3ccccc3Cl)cc(C(N)=O)nc2c1 nan
22448617 95825 0 None - 0 Rat 6.4 pIC50 = 6.4 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 446 2 1 5 4.3 N#Cc1cccc(C2=Nc3cc(N4CCOCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236467 95825 0 None - 0 Rat 6.4 pIC50 = 6.4 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 446 2 1 5 4.3 N#Cc1cccc(C2=Nc3cc(N4CCOCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
136152920 101988 0 None - 0 Rat 6.4 pIC50 = 6.4 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 467 3 3 7 3.5 O=C1CC(c2cccc(-n3nncc3CO)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL256008 101988 0 None - 0 Rat 6.4 pIC50 = 6.4 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 467 3 3 7 3.5 O=C1CC(c2cccc(-n3nncc3CO)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
71566600 152975 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CNC3=O)cc2n1 nan
CHEMBL3920092 152975 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CNC3=O)cc2n1 nan
89554814 159662 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 4 1 5 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCn4cc(C(F)(F)F)nc4C3)cc2n1 nan
CHEMBL3974523 159662 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 4 1 5 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCn4cc(C(F)(F)F)nc4C3)cc2n1 nan
18613455 102825 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 414 3 1 6 3.8 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL259924 102825 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 414 3 1 6 3.8 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
89554808 152002 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(N)CC3)cc2n1 nan
CHEMBL3912631 152002 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(N)CC3)cc2n1 nan
89554869 151444 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 389 4 1 5 3.5 Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1 nan
CHEMBL3908309 151444 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 389 4 1 5 3.5 Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1 nan
89554849 157734 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 1 6 2.9 COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cn1 nan
CHEMBL3958094 157734 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 1 6 2.9 COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cn1 nan
22224570 102690 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 378 3 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259269 102690 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 378 3 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1 10.1016/j.bmcl.2008.02.076
53316798 63179 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 384 2 1 4 4.6 Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
CHEMBL1631856 63179 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 384 2 1 4 4.6 Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
89554811 154640 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 2 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)CC3)cc2n1 nan
CHEMBL3933190 154640 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 2 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)CC3)cc2n1 nan
71566521 150105 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc2c(-c3ccccc3F)cc(C(N)=O)nc2c1 nan
CHEMBL3897268 150105 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc2c(-c3ccccc3F)cc(C(N)=O)nc2c1 nan
89554885 151081 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL3905282 151081 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
89554951 161052 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 361 3 0 5 3.4 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COC3=O)cc2n1 nan
CHEMBL3986465 161052 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 361 3 0 5 3.4 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COC3=O)cc2n1 nan
89554872 156177 0 None - 0 Human 8.4 pIC50 = 8.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F nan
CHEMBL3945590 156177 0 None - 0 Human 8.4 pIC50 = 8.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F nan
44450479 103038 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 398 3 1 4 4.9 CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL261050 103038 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 398 3 1 4 4.9 CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
11235624 63079 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629862 63079 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11304010 63081 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629864 63081 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
11474913 63181 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631858 63181 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11281280 63182 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631859 63182 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
22317431 63187 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631864 63187 0 None - 0 Rat 8.4 pIC50 = 8.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
11559750 102730 0 None - 0 Human 8.4 pIC50 = 8.4 Binding
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O 10.1016/j.bmc.2008.02.066
CHEMBL259435 102730 0 None - 0 Human 8.4 pIC50 = 8.4 Binding
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O 10.1016/j.bmc.2008.02.066
71565740 151347 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 418 6 1 6 3.6 CCOC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
CHEMBL3907527 151347 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 418 6 1 6 3.6 CCOC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
22448643 95826 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 2 1 5 5.0 N#Cc1cccc(C2=Nc3cc(N4CCSCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236468 95826 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 2 1 5 5.0 N#Cc1cccc(C2=Nc3cc(N4CCSCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
53324715 63193 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 453 3 2 4 5.8 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631870 63193 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 453 3 2 4 5.8 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
11382367 73711 0 None 1 2 Rat 7.4 pIC50 = 7.4 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186630 73711 0 None 1 2 Rat 7.4 pIC50 = 7.4 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
22224567 174190 0 None - 0 Rat 6.4 pIC50 = 6.4 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 325 1 1 3 3.9 C=C(C)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL429629 174190 0 None - 0 Rat 6.4 pIC50 = 6.4 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 325 1 1 3 3.9 C=C(C)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
6324634 154722 11 None -1 2 Human 6.4 pIC50 = 6.4 Binding
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm980571q
CHEMBL39338 154722 11 None -1 2 Human 6.4 pIC50 = 6.4 Binding
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm980571q
156009702 183950 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 277 1 1 1 3.9 O=C1NCc2c1cc(-c1ccc(F)cc1)c1ccccc21 10.1016/j.bmcl.2020.127066
CHEMBL4634600 183950 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 277 1 1 1 3.9 O=C1NCc2c1cc(-c1ccc(F)cc1)c1ccccc21 10.1016/j.bmcl.2020.127066
71566442 152025 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 276 2 1 2 3.6 Cc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1 nan
CHEMBL3912824 152025 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 276 2 1 2 3.6 Cc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1 nan
156017399 184493 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 455 5 1 6 4.7 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4642255 184493 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 455 5 1 6 4.7 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
117642070 157828 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 5 1 7 2.1 COc1ncc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3958736 157828 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 5 1 7 2.1 COc1ncc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 nan
71566668 151003 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 359 3 0 4 3.6 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3904529 151003 0 None - 0 Human 6.4 pIC50 = 6.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 359 3 0 4 3.6 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
89554730 149792 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 413 4 1 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCS3(=O)=O)cc2n1 nan
CHEMBL3894724 149792 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 413 4 1 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCS3(=O)=O)cc2n1 nan
89554897 152193 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccnc4C(F)(F)F)ccc23)cn1 nan
CHEMBL3914040 152193 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccnc4C(F)(F)F)ccc23)cn1 nan
89554771 156439 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 5 1 5 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4cccnc4)nc4ccccc43)cc2n1 nan
CHEMBL3947441 156439 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 5 1 5 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4cccnc4)nc4ccccc43)cc2n1 nan
89554802 159431 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.4 C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL3972468 159431 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.4 C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCO1 nan
18613373 102949 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 442 5 2 6 4.8 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL260643 102949 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 442 5 2 6 4.8 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
71565807 149609 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 424 4 1 4 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc(Br)c3)cc2n1 nan
CHEMBL3893078 149609 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 424 4 1 4 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc(Br)c3)cc2n1 nan
44450484 103455 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 370 2 1 4 4.4 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL263906 103455 0 None - 0 Rat 7.4 pIC50 = 7.4 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 370 2 1 4 4.4 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
89554879 160499 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccncc3)cc2n1 nan
CHEMBL3981623 160499 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccncc3)cc2n1 nan
22448569 95956 0 None - 0 Rat 6.4 pIC50 = 6.4 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 478 2 1 5 4.0 N#Cc1cccc(C2=Nc3cc(N4CC[S+]([O-])CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236668 95956 0 None - 0 Rat 6.4 pIC50 = 6.4 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 478 2 1 5 4.0 N#Cc1cccc(C2=Nc3cc(N4CC[S+]([O-])CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
71565669 149740 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL3894283 149740 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4515671 149740 0 None - 0 Human 7.4 pIC50 = 7.4 Binding
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 10.1021/acs.jmedchem.8b01266
71565522 149728 0 None - 0 Human 6.3 pIC50 = 6.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 495 4 1 6 5.8 CC(C)(C)OC(=O)N(Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(=O)OC(C)(C)C nan
CHEMBL3894156 149728 0 None - 0 Human 6.3 pIC50 = 6.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 495 4 1 6 5.8 CC(C)(C)OC(=O)N(Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(=O)OC(C)(C)C nan
89554819 155094 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 1 4 4.8 Cc1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3936939 155094 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 1 4 4.8 Cc1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554826 157264 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)(F)CC4)ccc23)cn1 nan
CHEMBL3954377 157264 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)(F)CC4)ccc23)cn1 nan
71566278 159021 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 396 4 1 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ccccc43)cc2n1 nan
CHEMBL3968939 159021 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 396 4 1 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ccccc43)cc2n1 nan
89554896 166741 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 C[C@@H]1COC[C@@H](C)N1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL4107449 166741 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 C[C@@H]1COC[C@@H](C)N1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
22448868 162076 0 None - 0 Rat 7.3 pIC50 = 7.3 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 480 5 2 6 4.2 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL402963 162076 0 None - 0 Rat 7.3 pIC50 = 7.3 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 480 5 2 6 4.2 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
44450455 174347 0 None - 0 Rat 6.3 pIC50 = 6.3 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 345 3 1 5 3.9 CC(C)c1ccc2c(c1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL430053 174347 0 None - 0 Rat 6.3 pIC50 = 6.3 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 345 3 1 5 3.9 CC(C)c1ccc2c(c1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
89554847 151699 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 357 4 1 3 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cccnc3)cc2n1 nan
CHEMBL3910265 151699 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 357 4 1 3 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cccnc3)cc2n1 nan
89554756 156495 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 3.7 CC1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C nan
CHEMBL3947898 156495 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 3.7 CC1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C nan
71565803 160085 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 486 6 1 6 4.6 CCOC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nc1C(F)(F)F nan
CHEMBL3978058 160085 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 486 6 1 6 4.6 CCOC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nc1C(F)(F)F nan
44309314 210756 0 None - 0 Rat 6.3 pIC50 = 6.3 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.3 Clc1ccc(/C(=C/n2cncn2)OC2CCCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
CHEMBL69461 210756 0 None - 0 Rat 6.3 pIC50 = 6.3 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.3 Clc1ccc(/C(=C/n2cncn2)OC2CCCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
89554962 159877 0 None - 0 Human 6.3 pIC50 = 6.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 3 0 4 4.6 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C(=O)C1 nan
CHEMBL3976206 159877 0 None - 0 Human 6.3 pIC50 = 6.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 3 0 4 4.6 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C(=O)C1 nan
10130658 73527 0 None 2 2 Rat 6.3 pIC50 = 6.3 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185822 73527 0 None 2 2 Rat 6.3 pIC50 = 6.3 Binding
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
89554743 157730 0 None - 0 Human 6.3 pIC50 = 6.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 4 1 4 3.6 N#C[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3958048 157730 0 None - 0 Human 6.3 pIC50 = 6.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 4 1 4 3.6 N#C[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554738 157738 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3958113 157738 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
89554921 160576 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 373 5 1 6 2.7 COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3982294 160576 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 373 5 1 6 2.7 COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 nan
22224756 154730 0 None - 0 Rat 6.3 pIC50 = 6.3 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 397 1 1 3 4.7 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL393385 154730 0 None - 0 Rat 6.3 pIC50 = 6.3 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 397 1 1 3 4.7 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554738 157738 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3958113 157738 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
89554866 153373 0 None - 0 Human 8.3 pIC50 = 8.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 434 6 1 5 4.2 COc1cc(F)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 nan
CHEMBL3923126 153373 0 None - 0 Human 8.3 pIC50 = 8.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 434 6 1 5 4.2 COc1cc(F)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 nan
89554768 156230 0 None - 0 Human 8.3 pIC50 = 8.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 6 1 4 4.8 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1 nan
CHEMBL3946016 156230 0 None - 0 Human 8.3 pIC50 = 8.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 6 1 4 4.8 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1 nan
89554800 158523 0 None - 0 Human 8.3 pIC50 = 8.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 2 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(O)Cc3cccnc3)cc2n1 nan
CHEMBL3964644 158523 0 None - 0 Human 8.3 pIC50 = 8.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 2 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(O)Cc3cccnc3)cc2n1 nan
71552551 159294 0 None - 0 Human 8.3 pIC50 = 8.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 373 4 1 4 3.0 Cc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1 nan
CHEMBL3971388 159294 0 None - 0 Human 8.3 pIC50 = 8.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 373 4 1 4 3.0 Cc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1 nan
22317744 63061 0 None - 0 Rat 8.3 pIC50 = 8.3 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 1 4 5.5 COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629844 63061 0 None - 0 Rat 8.3 pIC50 = 8.3 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 1 4 5.5 COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
18548795 63175 0 None - 0 Rat 8.3 pIC50 = 8.3 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 399 2 1 4 5.4 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1 10.1016/j.bmcl.2010.09.125
CHEMBL1631757 63175 0 None - 0 Rat 8.3 pIC50 = 8.3 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 399 2 1 4 5.4 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1 10.1016/j.bmcl.2010.09.125
69093928 90684 0 None - 0 Human 8.3 pIC50 = 8.3 Binding
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206447 90684 0 None - 0 Human 8.3 pIC50 = 8.3 Binding
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
89554792 157176 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 5 2 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1 nan
CHEMBL3953648 157176 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 5 2 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1 nan
10428048 10134 31 None - 1 Rat 6.3 pIC50 = 6.3 Binding
Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
3955 10134 31 None - 1 Rat 6.3 pIC50 = 6.3 Binding
Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
CHEMBL305406 10134 31 None - 1 Rat 6.3 pIC50 = 6.3 Binding
Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
71566525 155461 0 None - 0 Human 6.3 pIC50 = 6.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 314 3 1 4 3.2 NC(=O)c1cc(-c2cnn(-c3ccccc3)c2)c2ccccc2n1 nan
CHEMBL3939839 155461 0 None - 0 Human 6.3 pIC50 = 6.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 314 3 1 4 3.2 NC(=O)c1cc(-c2cnn(-c3ccccc3)c2)c2ccccc2n1 nan
89554842 166666 0 None - 0 Human 6.3 pIC50 = 6.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 2 5 2.5 NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1 nan
CHEMBL4106872 166666 0 None - 0 Human 6.3 pIC50 = 6.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 2 5 2.5 NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1 nan
89554876 154937 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 426 6 1 5 4.5 COc1cc(C)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(C)c1 nan
CHEMBL3935571 154937 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 426 6 1 5 4.5 COc1cc(C)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(C)c1 nan
89554795 160222 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 5 1 6 2.9 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(CC(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3979288 160222 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 5 1 6 2.9 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(CC(F)(F)F)C4)ccc23)cn1 nan
89554817 150889 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(n4cncn4)C3)cc2n1 nan
CHEMBL3903609 150889 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(n4cncn4)C3)cc2n1 nan
89554934 166947 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 486 5 1 6 4.5 C[C@@H]1CN(Cc2ccc3c(-c4cnc(C(F)F)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4109232 166947 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 486 5 1 6 4.5 C[C@@H]1CN(Cc2ccc3c(-c4cnc(C(F)F)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
71565808 158042 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 360 4 1 4 3.7 Cc1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3960284 158042 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 360 4 1 4 3.7 Cc1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554773 150468 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 4 1 5 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ncccc43)cc2n1 nan
CHEMBL3900236 150468 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 4 1 5 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ncccc43)cc2n1 nan
89554798 151982 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 5 1 6 2.3 CCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL3912490 151982 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 5 1 6 2.3 CCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
117644752 153229 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 4 1 4 3.7 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C)O1 nan
CHEMBL3922089 153229 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 4 1 4 3.7 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C)O1 nan
89544007 153824 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 358 4 1 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cncnc3)cc2n1 nan
CHEMBL3926904 153824 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 358 4 1 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cncnc3)cc2n1 nan
71566128 154348 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 1 4 4.8 COc1nccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1Cl nan
CHEMBL3930919 154348 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 1 4 4.8 COc1nccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1Cl nan
89554803 159028 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 413 4 1 5 2.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCS(=O)(=O)CC3)cc2n1 nan
CHEMBL3968972 159028 0 None - 0 Human 7.3 pIC50 = 7.3 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 413 4 1 5 2.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCS(=O)(=O)CC3)cc2n1 nan
89554805 155493 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.4 C[C@H]1COCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3940116 155493 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.4 C[C@H]1COCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
71566439 150854 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 300 2 1 2 3.8 NC(=O)c1cc(-c2ccc(Cl)cc2F)c2ccccc2n1 nan
CHEMBL3903327 150854 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 300 2 1 2 3.8 NC(=O)c1cc(-c2ccc(Cl)cc2F)c2ccccc2n1 nan
71565735 157164 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 377 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3953417 157164 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 377 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
44309315 109037 0 None - 0 Rat 6.2 pIC50 = 6.2 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 337 4 0 4 4.9 Clc1cccc(Cl)c1/C(=C/n1cncn1)OC1CCCCC1 10.1016/s0960-894x(99)00346-7
CHEMBL303193 109037 0 None - 0 Rat 6.2 pIC50 = 6.2 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 337 4 0 4 4.9 Clc1cccc(Cl)c1/C(=C/n1cncn1)OC1CCCCC1 10.1016/s0960-894x(99)00346-7
71565523 160105 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 3 0 4 3.3 CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C1=O nan
CHEMBL3978239 160105 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 3 0 4 3.3 CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C1=O nan
71566671 157148 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 4 2 4 3.0 CC1(C)NC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3953282 157148 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 4 2 4 3.0 CC1(C)NC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
71565735 157164 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1 nan
CHEMBL3953417 157164 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1 nan
89554738 157738 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3958113 157738 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
53324292 63196 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 460 3 1 4 6.3 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-n4cccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631873 63196 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 460 3 1 4 6.3 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-n4cccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
89554993 155707 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 427 6 1 6 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)c(F)c1 nan
CHEMBL3941863 155707 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 427 6 1 6 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)c(F)c1 nan
89554892 157380 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 nan
CHEMBL3955188 157380 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 nan
89554749 158784 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
CHEMBL3966866 158784 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
71565966 159579 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 1 5 4.6 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1 nan
CHEMBL3973721 159579 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 1 5 4.6 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1 nan
89554893 160760 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1 nan
CHEMBL3983863 160760 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1 nan
22224854 102159 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL256812 102159 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
22317728 63063 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629846 63063 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
53320632 63069 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629852 63069 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
11442010 63083 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629866 63083 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
44450453 162677 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 337 2 1 5 3.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL406061 162677 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 337 2 1 5 3.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2008.02.076
18613404 95824 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 404 2 1 4 4.5 CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL236466 95824 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 404 2 1 4 4.5 CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
22448865 96093 0 None - 0 Rat 6.2 pIC50 = 6.2 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 435 4 2 5 3.9 N#Cc1cccc(C2=Nc3cc(OCC(=O)O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236882 96093 0 None - 0 Rat 6.2 pIC50 = 6.2 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 435 4 2 5 3.9 N#Cc1cccc(C2=Nc3cc(OCC(=O)O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
44450444 102908 0 None - 0 Rat 6.2 pIC50 = 6.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 353 3 1 5 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260455 102908 0 None - 0 Rat 6.2 pIC50 = 6.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 353 3 1 5 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
89554779 152871 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 3 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1 nan
CHEMBL3919306 152871 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 3 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1 nan
89554779 152871 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 385 4 1 3 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3919306 152871 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 385 4 1 3 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1 10.1016/j.bmcl.2020.127066
71565737 150750 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 2 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CC4)cn3)cc2n1 nan
CHEMBL3902679 150750 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 2 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CC4)cn3)cc2n1 nan
89554831 154282 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 1 4 3.8 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F nan
CHEMBL3930529 154282 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 1 4 3.8 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F nan
71566670 153686 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 1 4 3.3 CN1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C nan
CHEMBL3925652 153686 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 1 4 3.3 CN1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C nan
89554761 157346 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 346 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3)cc2n1 nan
CHEMBL3954993 157346 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 346 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3)cc2n1 nan
22224809 160766 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 375 1 1 3 4.7 Cc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1 10.1016/j.bmcl.2007.10.026
CHEMBL398392 160766 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 375 1 1 3 4.7 Cc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1 10.1016/j.bmcl.2007.10.026
9847181 101826 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 462 5 2 6 4.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL255151 101826 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 462 5 2 6 4.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
10089411 14299 0 None - 1 Human 5.2 pIC50 = 5.2 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.7 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
CHEMBL108735 14299 0 None - 1 Human 5.2 pIC50 = 5.2 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.7 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
353213 155837 16 None - 0 Rat 5.2 pIC50 = 5.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2007.12.005
353213 155837 16 None - 0 Rat 5.2 pIC50 = 5.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL394287 155837 16 None - 0 Rat 5.2 pIC50 = 5.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL394287 155837 16 None - 0 Rat 5.2 pIC50 = 5.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2008.02.076
353213 155837 16 None - 0 Rat 5.2 pIC50 = 5.2 Binding
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL394287 155837 16 None - 0 Rat 5.2 pIC50 = 5.2 Binding
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2010.09.125
71566437 154254 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 268 2 1 3 3.4 Cc1cscc1-c1cc(C(N)=O)nc2ccccc12 nan
CHEMBL3930346 154254 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 268 2 1 3 3.4 Cc1cscc1-c1cc(C(N)=O)nc2ccccc12 nan
44434255 95379 0 None - 0 Rat 5.2 pIC50 = 5.2 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 280 2 1 3 3.5 COc1cccc(C2=Nc3ccc(C)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL235598 95379 0 None - 0 Rat 5.2 pIC50 = 5.2 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 280 2 1 3 3.5 COc1cccc(C2=Nc3ccc(C)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554731 158890 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 438 5 1 4 5.7 CC(C)c1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3967755 158890 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 438 5 1 4 5.7 CC(C)c1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554972 160964 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 460 5 1 4 4.2 CCN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F nan
CHEMBL3985765 160964 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 460 5 1 4 4.2 CCN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F nan
22317369 63185 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 463 2 1 3 6.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(F)(F)F)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631862 63185 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 463 2 1 3 6.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(F)(F)F)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
71566346 156266 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 314 4 1 3 3.6 NC(=O)c1cc(-c2ccc(OC(F)F)cc2)c2ccccc2n1 nan
CHEMBL3946344 156266 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 314 4 1 3 3.6 NC(=O)c1cc(-c2ccc(OC(F)F)cc2)c2ccccc2n1 nan
71566348 157718 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 328 3 1 4 3.5 Cc1c(-c2cc(C(N)=O)nc3ccccc23)cnn1-c1ccccc1 nan
CHEMBL3957842 157718 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 328 3 1 4 3.5 Cc1c(-c2cc(C(N)=O)nc3ccccc23)cnn1-c1ccccc1 nan
89554750 149306 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 498 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(C)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3890746 149306 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 498 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(C)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
71566347 155476 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 252 2 1 4 1.7 Cn1cc(-c2cc(C(N)=O)nc3ccccc23)cn1 nan
CHEMBL3939979 155476 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 252 2 1 4 1.7 Cn1cc(-c2cc(C(N)=O)nc3ccccc23)cn1 nan
25195461 8925 48 None - 1 Human 7.2 pIC50 = 7.2 Binding
Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
8946 8925 48 None - 1 Human 7.2 pIC50 = 7.2 Binding
Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
CHEMBL3337527 8925 48 None - 1 Human 7.2 pIC50 = 7.2 Binding
Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
DB12059 8925 48 None - 1 Human 7.2 pIC50 = 7.2 Binding
Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
22224822 96691 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 391 2 1 4 4.4 COc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1 10.1016/j.bmcl.2007.10.026
CHEMBL237944 96691 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 391 2 1 4 4.4 COc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1 10.1016/j.bmcl.2007.10.026
89545189 159674 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3974648 159674 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1 10.1016/j.bmcl.2020.127066
156011740 184203 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 455 6 2 6 3.8 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4638570 184203 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 455 6 2 6 3.8 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554955 151959 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 326 2 1 2 3.8 NC(=O)c1cc(-c2ccccc2Br)c2ccccc2n1 nan
CHEMBL3912345 151959 0 None - 0 Human 6.2 pIC50 = 6.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 326 2 1 2 3.8 NC(=O)c1cc(-c2ccccc2Br)c2ccccc2n1 nan
89554762 159292 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 4 1 5 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4cccnc43)cc2n1 nan
CHEMBL3971379 159292 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 4 1 5 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4cccnc43)cc2n1 nan
1393 8321 64 None -2 6 Human 8.2 pIC50 = 8.2 Binding
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.6b01119
1396 8321 64 None -2 6 Human 8.2 pIC50 = 8.2 Binding
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.6b01119
213056 8321 64 None -2 6 Human 8.2 pIC50 = 8.2 Binding
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL8759 8321 64 None -2 6 Human 8.2 pIC50 = 8.2 Binding
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.6b01119
89554982 153630 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 6 2 6 3.2 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cncnc4N)ccc23)cc1 nan
CHEMBL3925177 153630 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 6 2 6 3.2 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cncnc4N)ccc23)cc1 nan
89554981 155237 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 409 6 1 6 3.5 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)cc1 nan
CHEMBL3937970 155237 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 409 6 1 6 3.5 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)cc1 nan
89554880 156823 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 372 5 1 4 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 nan
CHEMBL3950572 156823 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 372 5 1 4 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 nan
71565593 157740 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 4 3.2 CC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 nan
CHEMBL3958138 157740 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 4 3.2 CC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 nan
89554910 158173 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 445 4 1 5 4.4 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(Cl)nc(C(F)(F)F)c4)ccc23)cn1 nan
CHEMBL3961599 158173 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 445 4 1 5 4.4 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(Cl)nc(C(F)(F)F)c4)ccc23)cn1 nan
71565966 159579 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 1 5 4.6 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1 nan
CHEMBL3973721 159579 0 None - 0 Human 8.2 pIC50 = 8.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 1 5 4.6 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1 nan
18548862 164718 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 415 4 1 6 4.1 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL408455 164718 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 415 4 1 6 4.1 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
44450391 175614 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 414 3 1 4 5.3 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL437835 175614 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 414 3 1 4 5.3 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
22317892 63077 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 477 2 1 3 6.9 Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629860 63077 0 None - 0 Rat 8.2 pIC50 = 8.2 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 477 2 1 3 6.9 Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
69093344 90683 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206446 90683 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
44450434 174476 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 401 4 1 6 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(OCC(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL430231 174476 0 None - 0 Rat 7.2 pIC50 = 7.2 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 401 4 1 6 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(OCC(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
44431050 149122 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Antagonist activity at human mGlur2Antagonist activity at human mGlur2
ChEMBL 363 2 3 2 3.6 O=C1NCCc2c1[nH]c1ccc(NC(=O)C34CC5CC(CC(C5)C3)C4)cc21 10.1021/acs.jmedchem.0c01887
CHEMBL388669 149122 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Antagonist activity at human mGlur2Antagonist activity at human mGlur2
ChEMBL 363 2 3 2 3.6 O=C1NCCc2c1[nH]c1ccc(NC(=O)C34CC5CC(CC(C5)C3)C4)cc21 10.1021/acs.jmedchem.0c01887
71566601 157003 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 467 5 1 4 4.4 CC1(c2ccccc2)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3952222 157003 0 None - 0 Human 7.2 pIC50 = 7.2 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 467 5 1 4 4.4 CC1(c2ccccc2)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
44450483 175585 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 380 2 1 4 4.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(Br)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL437646 175585 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 380 2 1 4 4.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(Br)cc2N1 10.1016/j.bmcl.2008.02.076
9845127 174557 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 422 2 1 6 3.7 O=C1CC(c2cccc(-n3cnnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL430408 174557 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 422 2 1 6 3.7 O=C1CC(c2cccc(-n3cnnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
71565886 150826 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 6 1 6 3.0 CC(C)CC1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL3903111 150826 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 6 1 6 3.0 CC(C)CC1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
89554822 151420 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 436 5 1 4 5.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CC4)nc4ccccc43)cc2n1 nan
CHEMBL3908110 151420 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 436 5 1 4 5.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CC4)nc4ccccc43)cc2n1 nan
44453878 102452 0 None - 0 Rat 6.1 pIC50 = 6.1 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 416 2 1 4 5.0 Cn1ccnc1-c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
CHEMBL258113 102452 0 None - 0 Rat 6.1 pIC50 = 6.1 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 416 2 1 4 5.0 Cn1ccnc1-c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
89554929 157116 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 1 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2c(F)cc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3953060 157116 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 1 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2c(F)cc(CN3C(=O)CCC3=O)cc2n1 nan
89554907 167381 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)nc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL4112899 167381 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)nc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
44309080 210820 0 None - 0 Rat 4.1 pIC50 = 4.1 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 265 4 0 4 2.9 CC(C)O/C(=C\n1cncn1)c1ccc(F)cc1F 10.1016/s0960-894x(99)00346-7
CHEMBL69869 210820 0 None - 0 Rat 4.1 pIC50 = 4.1 Binding
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 265 4 0 4 2.9 CC(C)O/C(=C\n1cncn1)c1ccc(F)cc1F 10.1016/s0960-894x(99)00346-7
89554959 150117 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 362 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(F)nc4)ccc23)cn1 nan
CHEMBL3897362 150117 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 362 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(F)nc4)ccc23)cn1 nan
71566205 159075 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 386 5 1 3 4.7 COc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cc1 nan
CHEMBL3969476 159075 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 386 5 1 3 4.7 COc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cc1 nan
89554739 166685 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 4 1 6 3.9 Cc1cnc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)s1 nan
CHEMBL4107013 166685 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 4 1 6 3.9 Cc1cnc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)s1 nan
22224639 168549 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 395 1 1 3 5.1 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4Cl)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL413979 168549 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 395 1 1 3 5.1 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4Cl)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
1439 9247 15 None - 2 Rat 4.1 pIC50 = 4.1 Binding
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm980571q
5311457 9247 15 None - 2 Rat 4.1 pIC50 = 4.1 Binding
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm980571q
CHEMBL41013 9247 15 None - 2 Rat 4.1 pIC50 = 4.1 Binding
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm980571q
89554782 156813 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 5 2 4 2.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC[C@H]3C(N)=O)cc2n1 nan
CHEMBL3950507 156813 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 5 2 4 2.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC[C@H]3C(N)=O)cc2n1 nan
122539788 169324 15 None - 0 Human 7.1 pIC50 = 7.1 Binding
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 326 5 1 5 2.3 Cn1ccc(COc2cnc(C(N)=O)cc2-c2ccc(F)cc2)n1 10.1021/acs.jmedchem.8b01266
CHEMBL4168094 169324 15 None - 0 Human 7.1 pIC50 = 7.1 Binding
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 326 5 1 5 2.3 Cn1ccc(COc2cnc(C(N)=O)cc2-c2ccc(F)cc2)n1 10.1021/acs.jmedchem.8b01266
71565669 149740 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 nan
CHEMBL3894283 149740 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 nan
CHEMBL4515671 149740 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 nan
71565964 151028 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 7 1 4 5.2 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1 nan
CHEMBL3904730 151028 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 7 1 4 5.2 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1 nan
89554964 152001 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL3912615 152001 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
89554887 155110 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 2 4 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccnc(CO)c3)cc2n1 nan
CHEMBL3937038 155110 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 2 4 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccnc(CO)c3)cc2n1 nan
71566127 155416 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 415 6 1 4 4.9 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1 nan
CHEMBL3939455 155416 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 415 6 1 4 4.9 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1 nan
89554858 157878 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 520 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
CHEMBL3959134 157878 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 520 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
89554984 159300 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 423 6 1 6 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C#N)nc4)ccc23)cc1 nan
CHEMBL3971450 159300 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 423 6 1 6 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C#N)nc4)ccc23)cc1 nan
89554790 166646 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OCC4(C)C)ccc23)cn1 nan
CHEMBL4106729 166646 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OCC4(C)C)ccc23)cn1 nan
89554915 166880 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.2 Cc1nn(C)cc1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12 nan
CHEMBL4108673 166880 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.2 Cc1nn(C)cc1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12 nan
89554961 167063 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL4110317 167063 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
53317987 63075 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 453 4 1 4 6.0 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629859 63075 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 453 4 1 4 6.0 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
11484819 63080 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629863 63080 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
18548737 63177 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631854 63177 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
11362246 63183 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 3 1 3 6.1 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631860 63183 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 3 1 3 6.1 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
70052526 96827 2 None - 1 Human 8.1 pIC50 = 8.1 Binding
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL2381642 96827 2 None - 1 Human 8.1 pIC50 = 8.1 Binding
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
71566598 149468 15 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Negative allosteric modulation of rat mGluR2 by FLIPR assayNegative allosteric modulation of rat mGluR2 by FLIPR assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3892073 149468 15 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Negative allosteric modulation of rat mGluR2 by FLIPR assayNegative allosteric modulation of rat mGluR2 by FLIPR assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
89554908 149244 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 396 5 2 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(CF)C3)cc2n1 nan
CHEMBL3890277 149244 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 396 5 2 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(CF)C3)cc2n1 nan
9864190 95430 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 370 1 1 2 5.2 O=C1CC(c2cccc(Cl)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
CHEMBL235807 95430 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 370 1 1 2 5.2 O=C1CC(c2cccc(Cl)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
89554895 157013 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 5 1 4 5.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCC4)nc4ccccc43)cc2n1 nan
CHEMBL3952287 157013 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 5 1 4 5.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCC4)nc4ccccc43)cc2n1 nan
89554978 157484 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 5 1 6 3.5 CC(C)n1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3956019 157484 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 5 1 6 3.5 CC(C)n1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1 nan
89555003 152003 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 339 5 1 4 3.1 CON(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3912634 152003 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 339 5 1 4 3.1 CON(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554744 155117 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(=O)C3)cc2n1 nan
CHEMBL3937068 155117 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(=O)C3)cc2n1 nan
22448756 161380 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 474 3 1 5 5.0 COC1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1 10.1016/j.bmcl.2007.10.026
CHEMBL399185 161380 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 474 3 1 5 5.0 COC1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1 10.1016/j.bmcl.2007.10.026
89554949 154960 0 None - 0 Human 6.1 pIC50 = 6.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 238 2 1 2 2.9 NC(=O)c1cc(C2=CCCC2)c2ccccc2n1 nan
CHEMBL3935751 154960 0 None - 0 Human 6.1 pIC50 = 6.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 238 2 1 2 2.9 NC(=O)c1cc(C2=CCCC2)c2ccccc2n1 nan
89554741 153985 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 366 6 2 4 2.1 CN(CC(N)=O)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3928211 153985 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 366 6 2 4 2.1 CN(CC(N)=O)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554957 157156 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 2 6 2.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)O)nn3)cc2n1 nan
CHEMBL3953345 157156 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 2 6 2.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)O)nn3)cc2n1 nan
117642124 154119 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 6 2 6 4.1 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4C)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL3929304 154119 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 6 2 6 4.1 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4C)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
89554862 150762 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccccn3)cc2n1 nan
CHEMBL3902752 150762 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccccn3)cc2n1 nan
89554838 167714 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 461 4 1 6 3.5 Cc1nn(C)c(C)c1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12 nan
CHEMBL4115433 167714 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 461 4 1 6 3.5 Cc1nn(C)c(C)c1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12 nan
22318000 63066 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 438 3 1 4 5.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629849 63066 0 None - 0 Rat 7.1 pIC50 = 7.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 438 3 1 4 5.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
22224608 95533 0 None - 0 Rat 6.1 pIC50 = 6.1 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 362 1 1 4 3.8 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccn4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236257 95533 0 None - 0 Rat 6.1 pIC50 = 6.1 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 362 1 1 4 3.8 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccn4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554735 153406 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C)(C)C4)ccc23)cn1 nan
CHEMBL3923360 153406 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C)(C)C4)ccc23)cn1 nan
1408 7053 31 None - 0 Rat 4.1 pIC50 = 4.1 Binding
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 217 3 4 4 -1.0 OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O 10.1021/jm980571q
6604820 7053 31 None - 0 Rat 4.1 pIC50 = 4.1 Binding
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 217 3 4 4 -1.0 OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O 10.1021/jm980571q
CHEMBL285043 7053 31 None - 0 Rat 4.1 pIC50 = 4.1 Binding
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 217 3 4 4 -1.0 OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O 10.1021/jm980571q
CHEMBL288635 7053 31 None - 0 Rat 4.1 pIC50 = 4.1 Binding
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 217 3 4 4 -1.0 OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O 10.1021/jm980571q
89554810 158094 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 464 5 1 4 6.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCCC4)nc4ccccc43)cc2n1 nan
CHEMBL3960845 158094 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 464 5 1 4 6.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCCC4)nc4ccccc43)cc2n1 nan
71566598 149468 15 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3892073 149468 15 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
89554770 150869 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3903459 150869 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
71565965 155063 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 7 1 4 5.4 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1 nan
CHEMBL3936681 155063 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 7 1 4 5.4 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1 nan
89554985 157218 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 2 5 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)c(F)c1 nan
CHEMBL3954035 157218 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 2 5 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)c(F)c1 nan
89554980 160756 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 398 6 2 5 3.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)cc1 nan
CHEMBL3983820 160756 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 398 6 2 5 3.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)cc1 nan
89554809 160977 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 436 4 1 6 3.5 Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
CHEMBL3985872 160977 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 436 4 1 6 3.5 Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
89554789 166981 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1 nan
CHEMBL4109555 166981 0 None - 0 Human 8.1 pIC50 = 8.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1 nan
10201802 103422 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 413 3 1 5 4.4 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL263649 103422 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 413 3 1 5 4.4 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
18548824 164515 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL408229 164515 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
9888376 101990 1 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL256011 101990 1 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
71566598 149468 15 None - 0 Human 8.1 pIC50 = 8.1 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3892073 149468 15 None - 0 Human 8.1 pIC50 = 8.1 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
53316736 63058 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 3 1 3 6.1 CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629715 63058 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 3 1 3 6.1 CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
18548824 164515 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL408229 164515 0 None - 0 Rat 8.1 pIC50 = 8.1 Binding
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
71461395 90682 1 None - 0 Human 8.0 pIC50 = 8.0 Binding
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206445 90682 1 None - 0 Human 8.0 pIC50 = 8.0 Binding
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
89554912 152752 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 2 4 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C4CC4)C3)cc2n1 nan
CHEMBL3918313 152752 0 None - 0 Human 7.1 pIC50 = 7.1 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 2 4 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C4CC4)C3)cc2n1 nan
89554815 151924 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 5 1 6 3.8 CCc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
CHEMBL3912111 151924 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 5 1 6 3.8 CCc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
71565670 183999 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 363 4 1 3 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL4635528 183999 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 363 4 1 3 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
44450445 103051 0 None - 0 Rat 7.0 pIC50 = 7.0 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 371 2 1 5 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261128 103051 0 None - 0 Rat 7.0 pIC50 = 7.0 Binding
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 371 2 1 5 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
9886745 95958 0 None - 0 Rat 7.0 pIC50 = 7.0 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 391 2 1 4 4.4 COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL236670 95958 0 None - 0 Rat 7.0 pIC50 = 7.0 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 391 2 1 4 4.4 COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
117641966 153322 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC4(CCOC4)CC3)cc2n1 nan
CHEMBL3922743 153322 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC4(CCOC4)CC3)cc2n1 nan
89554924 149486 0 None - 0 Human 6.0 pIC50 = 6.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 2 6 1.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC[C@H](O)C4)ccc23)cn1 nan
CHEMBL3892213 149486 0 None - 0 Human 6.0 pIC50 = 6.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 2 6 1.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC[C@H](O)C4)ccc23)cn1 nan
117642073 155754 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 428 7 1 6 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1OC nan
CHEMBL3942209 155754 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 428 7 1 6 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1OC nan
22224730 161523 0 None - 0 Rat 6.0 pIC50 = 6.0 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 366 2 1 3 4.6 COc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL400018 161523 0 None - 0 Rat 6.0 pIC50 = 6.0 Binding
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 366 2 1 3 4.6 COc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554920 152341 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 439 5 1 7 1.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCS(=O)(=O)C(C5CC5)C4)ccc23)cn1 nan
CHEMBL3915181 152341 0 None - 0 Human 7.0 pIC50 = 7.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 439 5 1 7 1.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCS(=O)(=O)C(C5CC5)C4)ccc23)cn1 nan
9931956 101862 0 None - 0 Rat 7.0 pIC50 = 7.0 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3cncn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL255356 101862 0 None - 0 Rat 7.0 pIC50 = 7.0 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3cncn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
22224761 173394 0 None - 0 Rat 7.0 pIC50 = 7.0 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 434 2 1 4 5.2 Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccc(F)cc5)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2007.12.005
CHEMBL428066 173394 0 None - 0 Rat 7.0 pIC50 = 7.0 Binding
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 434 2 1 4 5.2 Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccc(F)cc5)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2007.12.005
71566203 155414 0 None - 0 Human 6.0 pIC50 = 6.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 3 1 4 2.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCOCC3)cc2n1 nan
CHEMBL3939409 155414 0 None - 0 Human 6.0 pIC50 = 6.0 Binding
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 3 1 4 2.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCOCC3)cc2n1 nan
3335 9789 4 None - 1 Rat 5.0 pIC50 = 5 Binding
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm980571q
5311344 9789 4 None - 1 Rat 5.0 pIC50 = 5 Binding
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm980571q
CHEMBL39573 9789 4 None - 1 Rat 5.0 pIC50 = 5 Binding
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm980571q
68109335 163890 0 None - 1 Human 9.0 pKd = 9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4074664 163890 0 None - 1 Human 9.0 pKd = 9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
66785087 164919 0 None - 1 Human 9.0 pKd = 9.0 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4087196 164919 0 None - 1 Human 9.0 pKd = 9.0 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
49801370 163814 0 None - 1 Human 8.9 pKd = 8.9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4073628 163814 0 None - 1 Human 8.9 pKd = 8.9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
68109941 162901 0 None - 1 Human 8.8 pKd = 8.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4063313 162901 0 None - 1 Human 8.8 pKd = 8.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66786131 163945 0 None - 1 Human 8.0 pKd = 8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075417 163945 0 None - 1 Human 8.0 pKd = 8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
66786493 164039 0 None - 1 Human 8.0 pKd = 8.0 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4076639 164039 0 None - 1 Human 8.0 pKd = 8.0 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
137652500 163968 0 None - 1 Human 8.0 pKd = 8.0 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075697 163968 0 None - 1 Human 8.0 pKd = 8.0 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
68109677 163972 0 None - 1 Human 8.0 pKd = 8.0 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4075762 163972 0 None - 1 Human 8.0 pKd = 8.0 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
44595851 10574 4 None - 1 Human 7.0 pKd = 7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
6259 10574 4 None - 1 Human 7.0 pKd = 7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
CHEMBL4092105 10574 4 None - 1 Human 7.0 pKd = 7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
68109605 165169 0 None - 1 Human 7.9 pKd = 7.9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4089955 165169 0 None - 1 Human 7.9 pKd = 7.9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
66786069 163240 0 None - 1 Human 7.9 pKd = 7.9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4067290 163240 0 None - 1 Human 7.9 pKd = 7.9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
66784529 163872 0 None - 1 Human 7.9 pKd = 7.9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4074421 163872 0 None - 1 Human 7.9 pKd = 7.9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66785027 165117 0 None - 1 Human 7.9 pKd = 7.9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4089416 165117 0 None - 1 Human 7.9 pKd = 7.9 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
66785551 163932 0 None - 1 Human 7.8 pKd = 7.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075258 163932 0 None - 1 Human 7.8 pKd = 7.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
66785393 163673 0 None - 1 Human 7.8 pKd = 7.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4072134 163673 0 None - 1 Human 7.8 pKd = 7.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
66784675 163953 0 None - 1 Human 7.8 pKd = 7.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4075537 163953 0 None - 1 Human 7.8 pKd = 7.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
68109333 164408 0 None - 1 Human 7.8 pKd = 7.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4081244 164408 0 None - 1 Human 7.8 pKd = 7.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66784246 163143 0 None - 1 Human 7.8 pKd = 7.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4066051 163143 0 None - 1 Human 7.8 pKd = 7.8 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
68109272 165397 0 None - 1 Human 7.7 pKd = 7.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4092275 165397 0 None - 1 Human 7.7 pKd = 7.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
3954 7451 60 None - 1 Human 6.7 pKd = 6.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
9868580 7451 60 None - 1 Human 6.7 pKd = 6.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
CHEMBL593013 7451 60 None - 1 Human 6.7 pKd = 6.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
66785780 165523 0 None - 1 Human 8.7 pKd = 8.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093657 165523 0 None - 1 Human 8.7 pKd = 8.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
66787433 163242 0 None - 1 Human 8.7 pKd = 8.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4067298 163242 0 None - 1 Human 8.7 pKd = 8.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
66784262 165010 0 None - 1 Human 8.7 pKd = 8.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4088239 165010 0 None - 1 Human 8.7 pKd = 8.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
70209638 164388 0 None - 1 Human 8.6 pKd = 8.6 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4080973 164388 0 None - 1 Human 8.6 pKd = 8.6 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
68109580 165304 0 None - 1 Human 8.5 pKd = 8.5 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4091370 165304 0 None - 1 Human 8.5 pKd = 8.5 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
66784890 162829 0 None - 1 Human 7.7 pKd = 7.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4062535 162829 0 None - 1 Human 7.7 pKd = 7.7 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
66785101 164824 0 None - 1 Human 7.6 pKd = 7.6 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4085882 164824 0 None - 1 Human 7.6 pKd = 7.6 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
66786816 165135 0 None - 1 Human 7.6 pKd = 7.6 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4089612 165135 0 None - 1 Human 7.6 pKd = 7.6 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
68109425 165069 0 None - 1 Human 7.6 pKd = 7.6 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4088960 165069 0 None - 1 Human 7.6 pKd = 7.6 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
68108857 164117 0 None - 1 Human 8.5 pKd = 8.5 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4077609 164117 0 None - 1 Human 8.5 pKd = 8.5 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66786493 166458 0 None - 1 Human 8.5 pKd = 8.5 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4104081 166458 0 None - 1 Human 8.5 pKd = 8.5 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
49801369 165528 0 None - 1 Human 8.5 pKd = 8.5 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4093792 165528 0 None - 1 Human 8.5 pKd = 8.5 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
66785300 163251 0 None - 1 Human 8.5 pKd = 8.5 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
CHEMBL4067421 163251 0 None - 1 Human 8.5 pKd = 8.5 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
66787355 163004 0 None - 1 Human 8.4 pKd = 8.4 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4064589 163004 0 None - 1 Human 8.4 pKd = 8.4 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
49801371 165520 0 None - 1 Human 7.4 pKd = 7.4 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093620 165520 0 None - 1 Human 7.4 pKd = 7.4 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
66785182 163957 0 None - 1 Human 7.4 pKd = 7.4 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4075593 163957 0 None - 1 Human 7.4 pKd = 7.4 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
59234231 8924 4 None -2 2 Human 7.3 pKd = 7.3 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6330 8924 4 None -2 2 Human 7.3 pKd = 7.3 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6331 8924 4 None -2 2 Human 7.3 pKd = 7.3 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
CHEMBL3337510 8924 4 None -2 2 Human 7.3 pKd = 7.3 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
68109379 164004 0 None - 1 Human 7.3 pKd = 7.3 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4076286 164004 0 None - 1 Human 7.3 pKd = 7.3 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
66785010 162642 0 None - 1 Human 8.2 pKd = 8.2 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4060306 162642 0 None - 1 Human 8.2 pKd = 8.2 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
25125217 7343 25 None - 1 Human 6.2 pKd = 6.2 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
7678 7343 25 None - 1 Human 6.2 pKd = 6.2 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
CHEMBL3937907 7343 25 None - 1 Human 6.2 pKd = 6.2 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
DB16073 7343 25 None - 1 Human 6.2 pKd = 6.2 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
66786902 166240 0 None - 1 Human 8.1 pKd = 8.1 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4101354 166240 0 None - 1 Human 8.1 pKd = 8.1 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
68109333 166171 0 None - 1 Human 8.1 pKd = 8.1 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4100691 166171 0 None - 1 Human 8.1 pKd = 8.1 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66784572 163687 0 None - 1 Human 8.1 pKd = 8.1 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4072262 163687 0 None - 1 Human 8.1 pKd = 8.1 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
137652320 164053 0 None - 1 Human 8.1 pKd = 8.1 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4076786 164053 0 None - 1 Human 8.1 pKd = 8.1 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
49801368 166437 0 None - 1 Human 8.0 pKd = 8.0 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4103808 166437 0 None - 1 Human 8.0 pKd = 8.0 Binding
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
68109941 162901 0 None - 1 Human 9.1 pKi = 9.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4063313 162901 0 None - 1 Human 9.1 pKi = 9.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
117972250 149090 3 None - 1 Human 9.0 pKi = 9 Binding
Displacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting methodDisplacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting method
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885379 149090 3 None - 1 Human 9.0 pKi = 9 Binding
Displacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting methodDisplacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting method
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
11325656 133547 0 None - 1 Rat 9.0 pKi = 9.0 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 6 4 5 0.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(=O)O)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL365305 133547 0 None - 1 Rat 9.0 pKi = 9.0 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 6 4 5 0.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(=O)O)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11211507 72221 0 None - 1 Rat 8.8 pKi = 8.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 391 5 3 4 2.7 C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL182972 72221 0 None - 1 Rat 8.8 pKi = 8.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 391 5 3 4 2.7 C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
11339150 133931 0 None - 1 Rat 8.8 pKi = 8.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 419 7 3 4 3.4 CCC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL365680 133931 0 None - 1 Rat 8.8 pKi = 8.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 419 7 3 4 3.4 CCC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
66786902 166240 0 None - 1 Human 8.8 pKi = 8.8 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4101354 166240 0 None - 1 Human 8.8 pKi = 8.8 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
11177216 73097 0 None - 1 Rat 8.8 pKi = 8.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 405 6 3 4 3.1 CC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL184983 73097 0 None - 1 Rat 8.8 pKi = 8.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 405 6 3 4 3.1 CC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
11383191 103379 0 None - 1 Rat 8.8 pKi = 8.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 373 5 3 4 2.5 C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1 10.1021/jm0400294
CHEMBL263312 103379 0 None - 1 Rat 8.8 pKi = 8.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 373 5 3 4 2.5 C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1 10.1021/jm0400294
68108857 164117 0 None - 1 Human 8.7 pKi = 8.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4077609 164117 0 None - 1 Human 8.7 pKi = 8.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66785551 163932 0 None - 1 Human 8.7 pKi = 8.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075258 163932 0 None - 1 Human 8.7 pKi = 8.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
68109605 165169 0 None - 1 Human 8.0 pKi = 8 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4089955 165169 0 None - 1 Human 8.0 pKi = 8 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
66785027 165117 0 None - 1 Human 8.0 pKi = 8.0 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4089416 165117 0 None - 1 Human 8.0 pKi = 8.0 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
67637138 190397 0 None -1 2 Human 8.0 pKi = 8.0 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4776989 190397 0 None -1 2 Human 8.0 pKi = 8.0 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802329 190397 0 None -1 2 Human 8.0 pKi = 8.0 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
49836087 7847 0 None - 1 Human 6.0 pKi = 6 Binding
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
6222 7847 0 None - 1 Human 6.0 pKi = 6 Binding
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
CHEMBL1630805 7847 0 None - 1 Human 6.0 pKi = 6 Binding
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
15461589 107205 0 None - 1 Rat 6.0 pKi = 6 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL290416 107205 0 None - 1 Rat 6.0 pKi = 6 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
11756841 168097 0 None - 1 Rat 6.0 pKi = 6 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 CCC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
CHEMBL41242 168097 0 None - 1 Rat 6.0 pKi = 6 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 CCC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
11768848 122030 11 None - 1 Human 5.0 pKi = 5.0 Binding
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@H]1CC(=O)O 10.1039/C1MD00186H
CHEMBL3347671 122030 11 None - 1 Human 5.0 pKi = 5.0 Binding
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@H]1CC(=O)O 10.1039/C1MD00186H
11195342 130812 0 None - 1 Rat 7.0 pKi = 7.0 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363034 130812 0 None - 1 Rat 7.0 pKi = 7.0 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
68109333 164408 0 None - 1 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4081244 164408 0 None - 1 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66787433 163242 0 None - 1 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4067298 163242 0 None - 1 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
66784675 163953 0 None - 1 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4075537 163953 0 None - 1 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
11188098 129875 0 None - 1 Rat 7.9 pKi = 7.9 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL361024 129875 0 None - 1 Rat 7.9 pKi = 7.9 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
1377 8122 26 None -2 6 Human 7.0 pKi = 7.0 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm010323l
5310979 8122 26 None -2 6 Human 7.0 pKi = 7.0 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm010323l
CHEMBL284193 8122 26 None -2 6 Human 7.0 pKi = 7.0 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm010323l
1310 9095 110 None -22 18 Human 5.0 pKi = 5.0 Binding
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
1369 9095 110 None -22 18 Human 5.0 pKi = 5.0 Binding
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
33032 9095 110 None -22 18 Human 5.0 pKi = 5.0 Binding
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
44272391 9095 110 None -22 18 Human 5.0 pKi = 5.0 Binding
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
88747398 9095 110 None -22 18 Human 5.0 pKi = 5.0 Binding
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
CHEMBL575060 9095 110 None -22 18 Human 5.0 pKi = 5.0 Binding
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
DB00142 9095 110 None -22 18 Human 5.0 pKi = 5.0 Binding
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
71476419 130187 0 None -1 2 Human 7.0 pKi = 7.0 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616860 130187 0 None -1 2 Human 7.0 pKi = 7.0 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
155533313 178631 0 None - 1 Human 7.0 pKi = 7.0 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4468977 178631 0 None - 1 Human 7.0 pKi = 7.0 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
60096194 163367 0 None -10 2 Human 5.0 pKi = 5.0 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 290 5 4 4 0.3 N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4068679 163367 0 None -10 2 Human 5.0 pKi = 5.0 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 290 5 4 4 0.3 N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
11462089 74116 0 None - 1 Rat 7.9 pKi = 7.9 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(F)cc(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL188532 74116 0 None - 1 Rat 7.9 pKi = 7.9 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(F)cc(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
1310 9095 110 None -22 18 Human 5.9 pKi = 5.9 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
1369 9095 110 None -22 18 Human 5.9 pKi = 5.9 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
33032 9095 110 None -22 18 Human 5.9 pKi = 5.9 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
44272391 9095 110 None -22 18 Human 5.9 pKi = 5.9 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
88747398 9095 110 None -22 18 Human 5.9 pKi = 5.9 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
CHEMBL575060 9095 110 None -22 18 Human 5.9 pKi = 5.9 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
DB00142 9095 110 None -22 18 Human 5.9 pKi = 5.9 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
162652146 186992 0 None -1 2 Human 5.9 pKi = 5.9 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 289 5 4 5 -0.2 CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4749728 186992 0 None -1 2 Human 5.9 pKi = 5.9 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 289 5 4 5 -0.2 CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O 10.1021/acs.jmedchem.6b01119
71135411 130175 0 None -1 2 Human 6.9 pKi = 6.9 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616848 130175 0 None -1 2 Human 6.9 pKi = 6.9 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
71681826 96836 0 None -4 2 Human 5.9 pKi = 5.9 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL2381651 96836 0 None -4 2 Human 5.9 pKi = 5.9 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
1393 8321 64 None -2 6 Human 7.9 pKi = 7.9 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm010323l
1396 8321 64 None -2 6 Human 7.9 pKi = 7.9 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm010323l
213056 8321 64 None -2 6 Human 7.9 pKi = 7.9 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm010323l
CHEMBL8759 8321 64 None -2 6 Human 7.9 pKi = 7.9 Binding
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm010323l
71131322 130184 0 None 4 2 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616857 130184 0 None 4 2 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
60096250 165700 0 None -60 2 Human 6.9 pKi = 6.9 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4095567 165700 0 None -60 2 Human 6.9 pKi = 6.9 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
10197984 9199 44 None 2 5 Human 7.9 pKi = 7.9 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
1394 9199 44 None 2 5 Human 7.9 pKi = 7.9 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
CHEMBL275079 9199 44 None 2 5 Human 7.9 pKi = 7.9 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
10197984 9199 44 None 2 5 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
1394 9199 44 None 2 5 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
CHEMBL275079 9199 44 None 2 5 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
69669646 190458 0 None 1 2 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
CHEMBL4757159 190458 0 None 1 2 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
CHEMBL4802990 190458 0 None 1 2 Human 7.9 pKi = 7.9 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
11348518 133072 0 None - 1 Rat 7.8 pKi = 7.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(F)ccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL365018 133072 0 None - 1 Rat 7.8 pKi = 7.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(F)ccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
66784246 163143 0 None - 1 Human 7.8 pKi = 7.8 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4066051 163143 0 None - 1 Human 7.8 pKi = 7.8 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
71136640 130180 0 None 1 2 Human 6.9 pKi = 6.9 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616853 130180 0 None 1 2 Human 6.9 pKi = 6.9 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
53240406 130174 17 None 1 2 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 130174 17 None 1 2 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
9834591 144378 69 None -1 2 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 235 2 3 5 -2.1 N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL375611 144378 69 None -1 2 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 235 2 3 5 -2.1 N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
49765871 8926 45 None - 1 Human 7.8 pKi = 7.8 Binding
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 8926 45 None - 1 Human 7.8 pKi = 7.8 Binding
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 8926 45 None - 1 Human 7.8 pKi = 7.8 Binding
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
11393152 73769 0 None - 1 Rat 7.8 pKi = 7.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 324 5 4 5 0.4 Nc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
CHEMBL186891 73769 0 None - 1 Rat 7.8 pKi = 7.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 324 5 4 5 0.4 Nc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
49822116 153770 13 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 153770 13 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
9914583 148743 0 None - 1 Rat 5.8 pKi = 5.8 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL38729 148743 0 None - 1 Rat 5.8 pKi = 5.8 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
60096183 166063 0 None -6 2 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL4099470 166063 0 None -6 2 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
137635882 162673 0 None -1 2 Human 5.8 pKi = 5.8 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4060567 162673 0 None -1 2 Human 5.8 pKi = 5.8 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
11310142 9200 19 None 1 2 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
11614 9200 19 None 1 2 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
CHEMBL192051 9200 19 None 1 2 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
155533313 178631 0 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4468977 178631 0 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
70052526 96827 2 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL2381642 96827 2 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
11164815 129129 0 None - 1 Rat 7.8 pKi = 7.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@@H](OCc2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL359973 129129 0 None - 1 Rat 7.8 pKi = 7.8 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@@H](OCc2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
71137008 130182 0 None -2 2 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616855 130182 0 None -2 2 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
155548817 180619 0 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 180619 0 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
66785101 164824 0 None - 1 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4085882 164824 0 None - 1 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
25195461 8925 48 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 8925 48 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 8925 48 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 8925 48 None - 1 Human 6.8 pKi = 6.8 Binding
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
1310 9095 110 None -22 18 Human 5.7 pKi = 5.7 Binding
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
1369 9095 110 None -22 18 Human 5.7 pKi = 5.7 Binding
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
33032 9095 110 None -22 18 Human 5.7 pKi = 5.7 Binding
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
44272391 9095 110 None -22 18 Human 5.7 pKi = 5.7 Binding
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
88747398 9095 110 None -22 18 Human 5.7 pKi = 5.7 Binding
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
CHEMBL575060 9095 110 None -22 18 Human 5.7 pKi = 5.7 Binding
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
DB00142 9095 110 None -22 18 Human 5.7 pKi = 5.7 Binding
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
60096246 162726 0 None -40 2 Human 6.7 pKi = 6.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1 10.1021/acs.jmedchem.7b01481
CHEMBL4061162 162726 0 None -40 2 Human 6.7 pKi = 6.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1 10.1021/acs.jmedchem.7b01481
11172339 73130 0 None - 1 Rat 6.7 pKi = 6.7 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 233 3 3 4 -0.8 CO[C@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185135 73130 0 None - 1 Rat 6.7 pKi = 6.7 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 233 3 3 4 -0.8 CO[C@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
11326253 72090 0 None - 1 Rat 8.7 pKi = 8.7 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 373 5 3 4 2.5 C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1 10.1021/jm0400294
CHEMBL182899 72090 0 None - 1 Rat 8.7 pKi = 8.7 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 373 5 3 4 2.5 C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1 10.1021/jm0400294
68109580 165304 0 None - 1 Human 8.7 pKi = 8.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4091370 165304 0 None - 1 Human 8.7 pKi = 8.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
66786493 166458 0 None - 1 Human 8.7 pKi = 8.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4104081 166458 0 None - 1 Human 8.7 pKi = 8.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
1397 9307 15 None 1 5 Human 8.7 pKi = 8.7 Binding
Binding affinity to mGLUR2Binding affinity to mGLUR2
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
9886034 9307 15 None 1 5 Human 8.7 pKi = 8.7 Binding
Binding affinity to mGLUR2Binding affinity to mGLUR2
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
CHEMBL186453 9307 15 None 1 5 Human 8.7 pKi = 8.7 Binding
Binding affinity to mGLUR2Binding affinity to mGLUR2
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
49801370 163814 0 None - 1 Human 8.7 pKi = 8.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4073628 163814 0 None - 1 Human 8.7 pKi = 8.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
11382367 73711 0 None 1 2 Rat 8.6 pKi = 8.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186630 73711 0 None 1 2 Rat 8.6 pKi = 8.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
1397 9307 15 None -1 5 Rat 8.6 pKi = 8.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
9886034 9307 15 None -1 5 Rat 8.6 pKi = 8.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186453 9307 15 None -1 5 Rat 8.6 pKi = 8.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11405687 73231 0 None 2 2 Rat 8.6 pKi = 8.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185210 73231 0 None 2 2 Rat 8.6 pKi = 8.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
70209638 164388 0 None - 1 Human 8.6 pKi = 8.6 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4080973 164388 0 None - 1 Human 8.6 pKi = 8.6 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
11257636 175151 0 None 1 2 Rat 8.6 pKi = 8.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.4 N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL434536 175151 0 None 1 2 Rat 8.6 pKi = 8.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.4 N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11375886 131134 0 None - 1 Rat 8.6 pKi = 8.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 521 6 3 4 5.0 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)c(Cl)c2)c2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363724 131134 0 None - 1 Rat 8.6 pKi = 8.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 521 6 3 4 5.0 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)c(Cl)c2)c2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11198402 133863 0 None - 1 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 334 5 3 5 0.7 N#Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
CHEMBL365647 133863 0 None - 1 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 334 5 3 5 0.7 N#Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
57338826 156406 0 None - 1 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3947221 156406 0 None - 1 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
11259548 73461 0 None - 1 Rat 7.7 pKi = 7.7 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 453 6 3 4 3.7 N[C@@]1(C(=O)O)[C@@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185456 73461 0 None - 1 Rat 7.7 pKi = 7.7 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 453 6 3 4 3.7 N[C@@]1(C(=O)O)[C@@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
162658340 190465 0 None -1 2 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4760856 190465 0 None -1 2 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803084 190465 0 None -1 2 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
10197984 9199 44 None 2 5 Human 5.7 pKi = 5.7 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
1394 9199 44 None 2 5 Human 5.7 pKi = 5.7 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
CHEMBL275079 9199 44 None 2 5 Human 5.7 pKi = 5.7 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
15518713 107044 0 None - 1 Rat 5.7 pKi = 5.7 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1cccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)c1 10.1016/s0960-894x(99)00227-9
CHEMBL288902 107044 0 None - 1 Rat 5.7 pKi = 5.7 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1cccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)c1 10.1016/s0960-894x(99)00227-9
15461591 168676 0 None - 1 Rat 5.7 pKi = 5.7 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 521 6 0 6 6.5 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2Cl)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
CHEMBL41513 168676 0 None - 1 Rat 5.7 pKi = 5.7 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 521 6 0 6 6.5 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2Cl)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
15461594 169950 0 None - 1 Rat 5.7 pKi = 5.7 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 545 8 0 7 6.6 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC(C)C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
CHEMBL41808 169950 0 None - 1 Rat 5.7 pKi = 5.7 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 545 8 0 7 6.6 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC(C)C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
162658781 190470 0 None -1 2 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4759209 190470 0 None -1 2 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803105 190470 0 None -1 2 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
66786131 163945 0 None - 1 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075417 163945 0 None - 1 Human 7.7 pKi = 7.7 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
60096190 165292 0 None -102 2 Human 6.7 pKi = 6.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4091203 165292 0 None -102 2 Human 6.7 pKi = 6.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
60096236 165201 0 None -38 2 Human 6.7 pKi = 6.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4090293 165201 0 None -38 2 Human 6.7 pKi = 6.7 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
9815617 121277 7 None 1 2 Rat 7.7 pKi = 7.7 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
CHEMBL333519 121277 7 None 1 2 Rat 7.7 pKi = 7.7 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
68109425 165069 0 None - 1 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4088960 165069 0 None - 1 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
45082292 122029 2 None -3 3 Human 4.7 pKi = 4.7 Binding
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O 10.1039/C1MD00186H
CHEMBL3347670 122029 2 None -3 3 Human 4.7 pKi = 4.7 Binding
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O 10.1039/C1MD00186H
44361401 38115 0 None -7 2 Human 7.6 pKi = 7.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 was determinedBinding affinity towards metabotropic glutamate receptor 2 was determined
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
CHEMBL140197 38115 0 None -7 2 Human 7.6 pKi = 7.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 was determinedBinding affinity towards metabotropic glutamate receptor 2 was determined
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
1393 8321 64 None 1 6 Rat 7.6 pKi = 7.6 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
1396 8321 64 None 1 6 Rat 7.6 pKi = 7.6 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
213056 8321 64 None 1 6 Rat 7.6 pKi = 7.6 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
CHEMBL8759 8321 64 None 1 6 Rat 7.6 pKi = 7.6 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
11084869 96828 2 None - 1 Human 6.6 pKi = 6.6 Binding
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL2381643 96828 2 None - 1 Human 6.6 pKi = 6.6 Binding
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
155548817 180619 0 None - 1 Human 6.6 pKi = 6.6 Binding
Irreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting methodIrreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 180619 0 None - 1 Human 6.6 pKi = 6.6 Binding
Irreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting methodIrreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
69669702 190454 0 None 1 2 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4756556 190454 0 None 1 2 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4802948 190454 0 None 1 2 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
15518714 107100 0 None - 1 Rat 5.6 pKi = 5.6 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 COc1ccccc1C1C(C(=O)OCCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL289394 107100 0 None - 1 Rat 5.6 pKi = 5.6 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 COc1ccccc1C1C(C(=O)OCCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
137652500 163968 0 None - 1 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075697 163968 0 None - 1 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
11361140 131096 0 None - 1 Rat 7.6 pKi = 7.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(-c3ccccc3)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363526 131096 0 None - 1 Rat 7.6 pKi = 7.6 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(-c3ccccc3)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
59234231 8924 4 None -2 2 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6330 8924 4 None -2 2 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6331 8924 4 None -2 2 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
CHEMBL3337510 8924 4 None -2 2 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
71136655 130179 0 None -1 2 Human 6.6 pKi = 6.6 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616852 130179 0 None -1 2 Human 6.6 pKi = 6.6 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
162644419 190401 0 None -1 2 Human 6.6 pKi = 6.6 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4778355 190401 0 None -1 2 Human 6.6 pKi = 6.6 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4802356 190401 0 None -1 2 Human 6.6 pKi = 6.6 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
71137011 130185 0 None 2 2 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616858 130185 0 None 2 2 Human 7.6 pKi = 7.6 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
10089411 14299 0 None - 1 Human 5.6 pKi = 5.6 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.7 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
CHEMBL108735 14299 0 None - 1 Human 5.6 pKi = 5.6 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.7 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
162663798 190498 0 None -1 2 Human 6.6 pKi = 6.6 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4779554 190498 0 None -1 2 Human 6.6 pKi = 6.6 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4803378 190498 0 None -1 2 Human 6.6 pKi = 6.6 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
11220424 165740 0 None -43 2 Human 6.5 pKi = 6.5 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 304 4 4 4 -0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4095995 165740 0 None -43 2 Human 6.5 pKi = 6.5 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 304 4 4 4 -0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
66784529 163872 0 None - 1 Human 8.5 pKi = 8.5 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4074421 163872 0 None - 1 Human 8.5 pKi = 8.5 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
11200955 71381 0 None - 1 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 419 7 3 4 3.4 CCC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL181710 71381 0 None - 1 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 419 7 3 4 3.4 CCC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
11177217 73450 0 None - 1 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 405 6 3 4 3.1 CC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL185423 73450 0 None - 1 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 405 6 3 4 3.1 CC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
1378 9195 54 None -1 10 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
1399 9195 54 None -1 10 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
9819927 9195 54 None -1 10 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
CHEMBL432038 9195 54 None -1 10 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
66785780 165523 0 None - 1 Human 8.5 pKi = 8.5 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093657 165523 0 None - 1 Human 8.5 pKi = 8.5 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
11279365 74334 0 None 1 2 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL189814 74334 0 None 1 2 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11221617 74165 0 None - 1 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL188787 74165 0 None - 1 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
1395 9306 15 None 2 2 Rat 8.5 pKi = 8.5 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
9837317 9306 15 None 2 2 Rat 8.5 pKi = 8.5 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
CHEMBL121053 9306 15 None 2 2 Rat 8.5 pKi = 8.5 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
11314439 128804 0 None - 1 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 361 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL359491 128804 0 None - 1 Rat 8.5 pKi = 8.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 361 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
66784572 163687 0 None - 1 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4072262 163687 0 None - 1 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
66785087 164919 0 None - 1 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4087196 164919 0 None - 1 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
11418500 129113 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 411 5 3 4 2.8 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)c(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL359905 129113 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 411 5 3 4 2.8 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)c(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
10807972 42591 1 None 1 2 Rat 8.4 pKi = 8.4 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm000346k
CHEMBL144151 42591 1 None 1 2 Rat 8.4 pKi = 8.4 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm000346k
11248009 133329 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 453 6 3 4 3.7 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL365244 133329 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 453 6 3 4 3.7 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11153780 130609 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 399 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2c(F)c(F)c(F)c(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL362459 130609 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 399 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2c(F)c(F)c(F)c(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11212336 131130 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 421 6 3 4 2.7 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(F)cc2)c2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363696 131130 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 421 6 3 4 2.7 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(F)cc2)c2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11485742 176253 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL442967 176253 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
66785300 163251 0 None - 1 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
CHEMBL4067421 163251 0 None - 1 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
162665071 190507 0 None -1 2 Human 7.5 pKi = 7.5 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4781638 190507 0 None -1 2 Human 7.5 pKi = 7.5 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803454 190507 0 None -1 2 Human 7.5 pKi = 7.5 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
15518719 175259 0 None - 1 Rat 5.5 pKi = 5.5 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 CCOc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL435174 175259 0 None - 1 Rat 5.5 pKi = 5.5 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 CCOc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
60096201 165347 0 None -13 2 Human 7.5 pKi = 7.5 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4091735 165347 0 None -13 2 Human 7.5 pKi = 7.5 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
68109333 166171 0 None - 1 Human 7.5 pKi = 7.5 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4100691 166171 0 None - 1 Human 7.5 pKi = 7.5 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
10130658 73527 0 None 2 2 Rat 7.5 pKi = 7.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185822 73527 0 None 2 2 Rat 7.5 pKi = 7.5 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
15518717 170152 0 None - 1 Rat 5.5 pKi = 5.5 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 505 6 0 6 6.0 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2F)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
CHEMBL41932 170152 0 None - 1 Rat 5.5 pKi = 5.5 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 505 6 0 6 6.0 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2F)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
60096204 162903 0 None -75 2 Human 6.5 pKi = 6.5 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4063336 162903 0 None -75 2 Human 6.5 pKi = 6.5 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
71136654 130186 0 None -4 2 Human 6.5 pKi = 6.5 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616859 130186 0 None -4 2 Human 6.5 pKi = 6.5 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
10197984 9199 44 None 2 5 Human 7.4 pKi = 7.4 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
1394 9199 44 None 2 5 Human 7.4 pKi = 7.4 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
CHEMBL275079 9199 44 None 2 5 Human 7.4 pKi = 7.4 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
25125217 7343 25 None - 1 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
7678 7343 25 None - 1 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
CHEMBL3937907 7343 25 None - 1 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
DB16073 7343 25 None - 1 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
68109272 165397 0 None - 1 Human 7.4 pKi = 7.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4092275 165397 0 None - 1 Human 7.4 pKi = 7.4 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
10192719 72888 0 None 2 2 Rat 7.4 pKi = 7.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 233 3 3 4 -0.8 CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL183956 72888 0 None 2 2 Rat 7.4 pKi = 7.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 233 3 3 4 -0.8 CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
137659992 166015 0 None -14 2 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4098939 166015 0 None -14 2 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
11360426 130581 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 361 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL362325 130581 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 361 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11749464 131814 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2-c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL364320 131814 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2-c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
155567633 182779 0 None - 1 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4589377 182779 0 None - 1 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
11484738 173056 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cccc(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL426983 173056 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cccc(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11268934 73901 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2c(Cl)cccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL187482 73901 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2c(Cl)cccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
1378 9195 54 None -2 10 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
1399 9195 54 None -2 10 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
9819927 9195 54 None -2 10 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
CHEMBL432038 9195 54 None -2 10 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
11188099 73601 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186107 73601 0 None - 1 Rat 8.4 pKi = 8.4 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
10353365 90022 1 None -5 2 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL218710 90022 1 None -5 2 Human 8.4 pKi = 8.4 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
11255753 129053 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 323 5 3 4 1.1 Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
CHEMBL359805 129053 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 323 5 3 4 1.1 Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
11290903 74112 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL188511 74112 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11188380 74240 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 387 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Br)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL189186 74240 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 387 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Br)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11163717 130448 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL362092 130448 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
10198133 213287 12 None -6 2 Human 7.4 pKi = 7.4 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
CHEMBL8839 213287 12 None -6 2 Human 7.4 pKi = 7.4 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
10198133 213287 12 None -6 2 Human 7.4 pKi = 7.4 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL8839 213287 12 None -6 2 Human 7.4 pKi = 7.4 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
15518715 107097 0 None - 1 Rat 5.4 pKi = 5.4 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 545 8 0 7 6.5 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C(C)C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL289388 107097 0 None - 1 Rat 5.4 pKi = 5.4 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 545 8 0 7 6.5 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C(C)C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
15518712 107270 0 None - 1 Rat 5.4 pKi = 5.4 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 483 7 0 7 5.2 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL291017 107270 0 None - 1 Rat 5.4 pKi = 5.4 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 483 7 0 7 5.2 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3)=CN21 10.1016/s0960-894x(99)00227-9
15392100 175874 0 None - 1 Rat 5.4 pKi = 5.4 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 474 5 0 6 6.3 CCOC(=O)C1=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN2C1c1ccccc1OC 10.1016/s0960-894x(99)00227-9
CHEMBL439925 175874 0 None - 1 Rat 5.4 pKi = 5.4 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 474 5 0 6 6.3 CCOC(=O)C1=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN2C1c1ccccc1OC 10.1016/s0960-894x(99)00227-9
11310142 9200 19 None 1 2 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
11614 9200 19 None 1 2 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
CHEMBL192051 9200 19 None 1 2 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
60096231 164434 15 None -446 2 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
CHEMBL4081453 164434 15 None -446 2 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
10979251 96835 0 None -3 2 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL2381650 96835 0 None -3 2 Human 6.4 pKi = 6.4 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
162666357 190510 0 None -1 2 Human 7.4 pKi = 7.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4784701 190510 0 None -1 2 Human 7.4 pKi = 7.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803523 190510 0 None -1 2 Human 7.4 pKi = 7.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
11275666 96832 1 None -15 2 Human 5.4 pKi = 5.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL2381647 96832 1 None -15 2 Human 5.4 pKi = 5.4 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
9815616 121578 6 None 1 2 Rat 7.3 pKi = 7.3 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
CHEMBL334014 121578 6 None 1 2 Rat 7.3 pKi = 7.3 Binding
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
66787355 163004 0 None - 1 Human 8.3 pKi = 8.3 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4064589 163004 0 None - 1 Human 8.3 pKi = 8.3 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
11196276 175119 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 261 5 3 4 0.0 CCCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL434338 175119 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 261 5 3 4 0.0 CCCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
67637415 190466 0 None -1 2 Human 8.3 pKi = 8.3 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4759992 190466 0 None -1 2 Human 8.3 pKi = 8.3 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4803099 190466 0 None -1 2 Human 8.3 pKi = 8.3 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
66786069 163240 0 None - 1 Human 8.3 pKi = 8.3 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4067290 163240 0 None - 1 Human 8.3 pKi = 8.3 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
69669747 190432 11 None -2 2 Human 8.3 pKi = 8.3 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4751065 190432 11 None -2 2 Human 8.3 pKi = 8.3 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802733 190432 11 None -2 2 Human 8.3 pKi = 8.3 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
11268363 131517 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2cccc3ccccc23)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL364201 131517 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2cccc3ccccc23)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11450243 74232 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 327 5 3 4 0.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL189139 74232 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 327 5 3 4 0.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11451742 131223 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)cc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363980 131223 0 None - 1 Rat 8.3 pKi = 8.3 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)cc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11349412 74318 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 1.8 N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(F)(F)F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL189710 74318 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 1.8 N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(F)(F)F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
155567633 182779 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4589377 182779 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
11338331 72308 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 391 5 3 4 2.7 C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL183073 72308 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 391 5 3 4 2.7 C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
11313770 130653 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 339 6 3 5 0.8 COc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
CHEMBL362708 130653 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 339 6 3 5 0.8 COc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
10353365 90022 1 None -5 2 Human 6.3 pKi = 6.3 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL218710 90022 1 None -5 2 Human 6.3 pKi = 6.3 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
66785182 163957 0 None - 1 Human 7.3 pKi = 7.3 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4075593 163957 0 None - 1 Human 7.3 pKi = 7.3 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
60096228 163566 0 None -5 2 Human 7.3 pKi = 7.3 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4070866 163566 0 None -5 2 Human 7.3 pKi = 7.3 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
60096224 163324 0 None -32 2 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4068189 163324 0 None -32 2 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL5076351 221209 0 None - 1 Human 7.2 pKi = 7.2 Binding
Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay
ChEMBL None None None CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1 10.1021/acs.jmedchem.1c02004
CHEMBL5076351 221209 0 None - 1 Human 7.2 pKi = 7.2 Binding
Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay
ChEMBL None None None CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1 10.1021/acs.jmedchem.1c02004
137634033 163420 0 None -2 2 Human 6.2 pKi = 6.2 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4069251 163420 0 None -2 2 Human 6.2 pKi = 6.2 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
68109335 163890 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4074664 163890 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
68109677 163972 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4075762 163972 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
155548817 180619 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 180619 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
66786816 165135 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4089612 165135 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
44396480 73611 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 275 5 3 4 0.4 CCC(C)O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186145 73611 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 275 5 3 4 0.4 CCC(C)O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
66785010 162642 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4060306 162642 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
3954 7451 60 None - 1 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
9868580 7451 60 None - 1 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
CHEMBL593013 7451 60 None - 1 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
71136653 130181 0 None 2 2 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616854 130181 0 None 2 2 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
49858117 7875 4 None - 1 Human 6.2 pKi = 6.2 Binding
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
6223 7875 4 None - 1 Human 6.2 pKi = 6.2 Binding
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
CHEMBL1630806 7875 4 None - 1 Human 6.2 pKi = 6.2 Binding
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
66784890 162829 0 None - 1 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4062535 162829 0 None - 1 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
68109379 164004 0 None - 1 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4076286 164004 0 None - 1 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
155548817 180619 0 None - 1 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 180619 0 None - 1 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
137656301 165461 0 None -1 2 Human 6.2 pKi = 6.2 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 324 5 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4093017 165461 0 None -1 2 Human 6.2 pKi = 6.2 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 324 5 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL5089623 221996 2 None - 1 Human 7.2 pKi = 7.2 Binding
Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay
ChEMBL None None None COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1 10.1021/acs.jmedchem.1c02004
CHEMBL5089623 221996 2 None - 1 Human 7.2 pKi = 7.2 Binding
Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay
ChEMBL None None None COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1 10.1021/acs.jmedchem.1c02004
49801371 165520 0 None - 1 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093620 165520 0 None - 1 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
11344646 133554 1 None -1 2 Human 6.2 pKi = 6.2 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm040222y
CHEMBL365368 133554 1 None -1 2 Human 6.2 pKi = 6.2 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm040222y
1310 9095 110 None -22 18 Human 5.2 pKi = 5.2 Binding
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
1369 9095 110 None -22 18 Human 5.2 pKi = 5.2 Binding
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
33032 9095 110 None -22 18 Human 5.2 pKi = 5.2 Binding
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
44272391 9095 110 None -22 18 Human 5.2 pKi = 5.2 Binding
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
88747398 9095 110 None -22 18 Human 5.2 pKi = 5.2 Binding
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
CHEMBL575060 9095 110 None -22 18 Human 5.2 pKi = 5.2 Binding
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
DB00142 9095 110 None -22 18 Human 5.2 pKi = 5.2 Binding
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
49858116 63122 0 None - 1 Human 5.2 pKi = 5.2 Binding
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 312 2 2 4 2.8 O=C(Nc1ccc(F)cc1)C12CC1/C(=N\O)c1ccccc1O2 10.1021/jm101069m
CHEMBL1630804 63122 0 None - 1 Human 5.2 pKi = 5.2 Binding
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 312 2 2 4 2.8 O=C(Nc1ccc(F)cc1)C12CC1/C(=N\O)c1ccccc1O2 10.1021/jm101069m
71137012 130178 0 None -1 2 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616851 130178 0 None -1 2 Human 7.2 pKi = 7.2 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
10198133 213287 12 None -6 2 Human 7.2 pKi = 7.2 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
CHEMBL8839 213287 12 None -6 2 Human 7.2 pKi = 7.2 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
11484739 129880 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2c(F)cccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL361051 129880 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2c(F)cccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11817779 72982 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 259 5 3 4 -0.2 C=CCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL184441 72982 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 259 5 3 4 -0.2 C=CCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
49801368 166437 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4103808 166437 0 None - 1 Human 8.2 pKi = 8.2 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
11347391 73626 0 None 2 2 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 309 5 3 4 0.8 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186214 73626 0 None 2 2 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 309 5 3 4 0.8 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11258119 74094 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 401 7 3 5 2.6 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Oc3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL188425 74094 0 None - 1 Rat 8.2 pKi = 8.2 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 401 7 3 5 2.6 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Oc3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
66785393 163673 0 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4072134 163673 0 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
67705089 159034 0 None -2 2 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 458 7 4 7 1.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
CHEMBL3969063 159034 0 None -2 2 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 458 7 4 7 1.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
49822115 8927 21 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
8947 8927 21 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
CHEMBL3947764 8927 21 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
49822115 8927 21 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
8947 8927 21 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
CHEMBL3947764 8927 21 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
11772601 134286 0 None - 1 Rat 8.1 pKi = 8.1 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 354 6 3 6 0.7 N[C@@]1(C(=O)O)[C@H](OCc2cccc([N+](=O)[O-])c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL366152 134286 0 None - 1 Rat 8.1 pKi = 8.1 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 354 6 3 6 0.7 N[C@@]1(C(=O)O)[C@H](OCc2cccc([N+](=O)[O-])c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
49801369 165528 0 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4093792 165528 0 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
15392101 107215 0 None - 1 Rat 5.2 pKi = 5.2 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1 10.1016/s0960-894x(99)00227-9
CHEMBL290509 107215 0 None - 1 Rat 5.2 pKi = 5.2 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1 10.1016/s0960-894x(99)00227-9
1393 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
1396 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
213056 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
CHEMBL8759 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
1393 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
1396 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
213056 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
CHEMBL8759 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
162654849 190449 0 None -1 2 Human 6.1 pKi = 6.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4755204 190449 0 None -1 2 Human 6.1 pKi = 6.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802906 190449 0 None -1 2 Human 6.1 pKi = 6.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
1393 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
1396 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
213056 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
CHEMBL8759 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
1393 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
1396 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
213056 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
CHEMBL8759 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
1393 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
1396 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
213056 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
CHEMBL8759 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
134132133 151567 0 None - 1 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3909237 151567 0 None - 1 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
44595851 10574 4 None - 1 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
6259 10574 4 None - 1 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
CHEMBL4092105 10574 4 None - 1 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
67633284 190426 0 None 1 2 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4748699 190426 0 None 1 2 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802655 190426 0 None 1 2 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
90098428 130183 0 None 5 2 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616856 130183 0 None 5 2 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
11449064 131172 0 None - 1 Rat 8.1 pKi = 8.1 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 287 4 3 4 0.5 N[C@@]1(C(=O)O)[C@H](OC2CCCC2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363940 131172 0 None - 1 Rat 8.1 pKi = 8.1 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 287 4 3 4 0.5 N[C@@]1(C(=O)O)[C@H](OC2CCCC2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
137652320 164053 0 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4076786 164053 0 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
11267024 73433 0 None - 1 Rat 8.1 pKi = 8.1 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 315 5 3 5 0.9 N[C@@]1(C(=O)O)[C@H](OCc2cccs2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185335 73433 0 None - 1 Rat 8.1 pKi = 8.1 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 315 5 3 5 0.9 N[C@@]1(C(=O)O)[C@H](OCc2cccs2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
67633340 190500 0 None -1 2 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4780402 190500 0 None -1 2 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4803381 190500 0 None -1 2 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
66784262 165010 0 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4088239 165010 0 None - 1 Human 8.1 pKi = 8.1 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
49858118 7894 0 None - 1 Human 6.1 pKi = 6.1 Binding
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
6224 7894 0 None - 1 Human 6.1 pKi = 6.1 Binding
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
CHEMBL1630807 7894 0 None - 1 Human 6.1 pKi = 6.1 Binding
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
15518718 106999 0 None - 1 Rat 5.1 pKi = 5.1 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 501 6 0 6 6.1 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
CHEMBL288472 106999 0 None - 1 Rat 5.1 pKi = 5.1 Binding
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 501 6 0 6 6.1 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
10198133 213287 12 None -6 2 Human 6.1 pKi = 6.1 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
CHEMBL8839 213287 12 None -6 2 Human 6.1 pKi = 6.1 Binding
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
71137010 130176 0 None -1 2 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616849 130176 0 None -1 2 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
1393 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm050235r
1396 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm050235r
213056 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm050235r
CHEMBL8759 8321 64 None -2 6 Human 7.1 pKi = 7.1 Binding
Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm050235r
9885546 117315 0 None - 1 Human 7.1 pKi = 7.1 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
CHEMBL325140 117315 0 None - 1 Human 7.1 pKi = 7.1 Binding
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
60096178 163660 0 None -181 2 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4071962 163660 0 None -181 2 Human 7.1 pKi = 7.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
60096211 96834 0 None -5 2 Human 6.1 pKi = 6.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL2381649 96834 0 None -5 2 Human 6.1 pKi = 6.1 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
69669820 190419 0 None -1 2 Human 8.0 pKi = 8.0 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
CHEMBL4746125 190419 0 None -1 2 Human 8.0 pKi = 8.0 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
CHEMBL4802570 190419 0 None -1 2 Human 8.0 pKi = 8.0 Binding
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
66786493 164039 0 None - 1 Human 8.0 pKi = 8.0 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4076639 164039 0 None - 1 Human 8.0 pKi = 8.0 Binding
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
11749463 72996 0 None - 1 Rat 8.0 pKi = 8.0 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(-c3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL184504 72996 0 None - 1 Rat 8.0 pKi = 8.0 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(-c3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11209918 73627 0 None - 1 Rat 8.0 pKi = 8.0 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 337 7 3 4 1.2 N[C@@]1(C(=O)O)[C@H](OCCCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186215 73627 0 None - 1 Rat 8.0 pKi = 8.0 Binding
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 337 7 3 4 1.2 N[C@@]1(C(=O)O)[C@H](OCCCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
71137034 130177 0 None -1 2 Human 7.0 pKi = 7.0 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616850 130177 0 None -1 2 Human 7.0 pKi = 7.0 Binding
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
11298568 76150 1 None -6 2 Human 6.0 pKi = 6.0 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O 10.1021/jm040222y
CHEMBL192977 76150 1 None -6 2 Human 6.0 pKi = 6.0 Binding
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O 10.1021/jm040222y
49822115 8927 21 None - 1 Human 8.8 pKd = 8.8 Binding
Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
8947 8927 21 None - 1 Human 8.8 pKd = 8.8 Binding
Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
CHEMBL3947764 8927 21 None - 1 Human 8.8 pKd = 8.8 Binding
Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
59234231 8924 4 None -2 2 Human 7.9 pKd = 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6330 8924 4 None -2 2 Human 7.9 pKd = 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6331 8924 4 None -2 2 Human 7.9 pKd = 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
CHEMBL3337510 8924 4 None -2 2 Human 7.9 pKd = 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
59234231 8924 4 None 2 2 Rat 8.0 pKd = 8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6330 8924 4 None 2 2 Rat 8.0 pKd = 8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6331 8924 4 None 2 2 Rat 8.0 pKd = 8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
CHEMBL3337510 8924 4 None 2 2 Rat 8.0 pKd = 8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
11362035 6831 1 None - 1 Rat 8.4 pKd = 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 21470207
6328 6831 1 None - 1 Rat 8.4 pKd = 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 21470207
6329 6831 1 None - 1 Rat 8.4 pKd = 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 21470207
CHEMBL105296 6831 1 None - 1 Rat 8.4 pKd = 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 21470207
1393 8321 64 None 1 6 Rat 7.7 pKd None 7.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
1396 8321 64 None 1 6 Rat 7.7 pKd None 7.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
213056 8321 64 None 1 6 Rat 7.7 pKd None 7.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
CHEMBL8759 8321 64 None 1 6 Rat 7.7 pKd None 7.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
1378 9195 54 None -2 10 Human 8.8 pKd None 8.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
1399 9195 54 None -2 10 Human 8.8 pKd None 8.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
9819927 9195 54 None -2 10 Human 8.8 pKd None 8.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
CHEMBL432038 9195 54 None -2 10 Human 8.8 pKd None 8.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
None 223112 0 3H-LY354740 - 1 Rat 8.0 pKi = 8 Binding
NoneNone
PDSP KiDatabase 323 5 5 9 -1.3 C1C(C1C(CN2C=NC3=C2N=C(N=C3O)O)(C(=O)O)N)C(=O)O None
12310764 8751 64 Functional -14 8 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
12310764 8751 64 3H-LY354740 -14 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
12310764 8751 64 Functional -14 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1233 8751 64 Functional -14 8 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1233 8751 64 3H-LY354740 -14 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1233 8751 64 Functional -14 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1371 8751 64 Functional -14 8 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1371 8751 64 3H-LY354740 -14 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1371 8751 64 Functional -14 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
CHEMBL284895 8751 64 Functional -14 8 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
CHEMBL284895 8751 64 3H-LY354740 -14 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
CHEMBL284895 8751 64 Functional -14 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1310 9095 110 Functional -13 18 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 9095 110 Functional -13 18 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 9095 110 Functional -13 18 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 9095 110 Functional -13 18 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 9095 110 Functional -13 18 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 9095 110 Functional -13 18 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 9095 110 Functional -13 18 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
134 9292 24 Functional -8511 67 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 353 4 2 4 1.9 CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO None
1775 9292 24 Functional -8511 67 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 353 4 2 4 1.9 CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO None
9681 9292 24 Functional -8511 67 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 353 4 2 4 1.9 CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO None
CHEMBL1065 9292 24 Functional -8511 67 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 353 4 2 4 1.9 CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO None
DB00247 9292 24 Functional -8511 67 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 353 4 2 4 1.9 CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO None
15897 9637 0 Functional -354 36 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 203 2 1 1 2.6 CC(Cc1cccc(c1)C(F)(F)F)N None
215 9637 0 Functional -354 36 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 203 2 1 1 2.6 CC(Cc1cccc(c1)C(F)(F)F)N None
CHEMBL1979333 9637 0 Functional -354 36 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 203 2 1 1 2.6 CC(Cc1cccc(c1)C(F)(F)F)N None
1370 10037 67 Functional -602 8 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
1370 10037 67 3H-LY354740 -602 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
1372 10037 67 Functional -602 8 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
1372 10037 67 3H-LY354740 -602 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
40539 10037 67 Functional -602 8 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
40539 10037 67 3H-LY354740 -602 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
6971145 10037 67 Functional -602 8 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
6971145 10037 67 3H-LY354740 -602 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
CHEMBL279956 10037 67 Functional -602 8 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
CHEMBL279956 10037 67 3H-LY354740 -602 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
DB02999 10037 67 Functional -602 8 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
DB02999 10037 67 3H-LY354740 -602 8 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
128563 10237 33 Functional -2398 42 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 432 3 0 8 3.0 COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1 None
1666 10237 33 Functional -2398 42 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 432 3 0 8 3.0 COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1 None
CHEMBL445332 10237 33 Functional -2398 42 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 432 3 0 8 3.0 COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1 None
DB12327 10237 33 Functional -2398 42 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 432 3 0 8 3.0 COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1 None
10297 33885 30 Functional -38 43 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 C[C@H](N)[C@H](O)c1ccccc1 None
CHEMBL136560 33885 30 Functional -38 43 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 C[C@H](N)[C@H](O)c1ccccc1 None
2207 106641 63 3H-LY354740 -25 7 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 183 4 4 3 -1.0 NC(CCP(=O)(O)O)C(=O)O None
CHEMBL285843 106641 63 3H-LY354740 -25 7 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 183 4 4 3 -1.0 NC(CCP(=O)(O)O)C(=O)O None
1222 108514 63 Functional 5 3 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 None
CHEMBL299683 108514 63 Functional 5 3 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 None
5115 118824 47 Functional 1 5 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
5115 118824 47 3H-GLUTAMATE -1 5 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
5115 118824 47 Functional -1 5 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
CHEMBL328984 118824 47 Functional 1 5 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
CHEMBL328984 118824 47 3H-GLUTAMATE -1 5 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
CHEMBL328984 118824 47 Functional -1 5 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
446220 140299 14 Functional -1778 45 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 303 3 0 5 1.9 COC(=O)[C@H]1[C@@H](OC(=O)c2ccccc2)C[C@@H]2CC[C@H]1N2C None
CHEMBL370805 140299 14 Functional -1778 45 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 303 3 0 5 1.9 COC(=O)[C@H]1[C@@H](OC(=O)c2ccccc2)C[C@@H]2CC[C@H]1N2C None
19702198 168101 16 Functional 1 2 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
19702198 168101 16 3H-LY354740 -1 2 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
19702198 168101 16 Functional -1 2 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
CHEMBL412445 168101 16 Functional 1 2 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
CHEMBL412445 168101 16 3H-LY354740 -1 2 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
CHEMBL412445 168101 16 Functional -1 2 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
1615 174570 24 Functional -26 44 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 193 3 1 3 1.6 CNC(C)Cc1ccc2c(c1)OCO2 None
CHEMBL43048 174570 24 Functional -26 44 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 193 3 1 3 1.6 CNC(C)Cc1ccc2c(c1)OCO2 None
1297 177031 36 Functional -1 4 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 None
1297 177031 36 Functional -1 4 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 None
CHEMBL444589 177031 36 Functional -1 4 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 None
CHEMBL444589 177031 36 Functional -1 4 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 None
162265 209053 22 Functional -239 44 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 CC(N)C(O)c1ccccc1 None
4786 209053 22 Functional -239 44 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 CC(N)C(O)c1ccccc1 None
CHEMBL61006 209053 22 Functional -239 44 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 CC(N)C(O)c1ccccc1 None
139054390 211702 106 Functional 1 5 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
139054390 211702 106 3H-LY354740 -1 5 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
139054390 211702 106 Functional -1 5 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
23327 211702 106 Functional 1 5 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
23327 211702 106 3H-LY354740 -1 5 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
23327 211702 106 Functional -1 5 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
CHEMBL76232 211702 106 Functional 1 5 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
CHEMBL76232 211702 106 3H-LY354740 -1 5 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
CHEMBL76232 211702 106 Functional -1 5 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
3337 213146 27 Functional -1513 40 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
65801 213146 27 Functional -1513 40 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
66264 213146 27 Functional -1513 40 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
91452 213146 27 Functional -1513 40 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
CHEMBL87493 213146 27 Functional -1513 40 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
11954224 222732 0 Functional -141253 59 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 581 4 3 6 2.0 CC1(C(=O)N2C(C(=O)N3CCCC3C2(O1)O)CC4=CC=CC=C4)NC(=O)C5CN(C6CC7=CNC8=CC=CC(=C78)C6=C5)C None
6971132 222788 0 3H-LY341495 -2570 14 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 268 1 2 2 2.1 CN1CC(C=C2C1CC3=CNC4=CC=CC2=C34)C(=O)O None
None 222951 0 Functional -2 7 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 173 2 3 3 -0.3 C1CC(CC1C(=O)O)(C(=O)O)N None
None 222951 0 Functional 1 7 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 173 2 3 3 -0.3 C1CC(CC1C(=O)O)(C(=O)O)N None
25137849 222958 0 Functional -4 40 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 165 3 2 2 1.3 CC(C(C1=CC=CC=C1)O)NC None
71290 222958 0 Functional -4 40 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 165 3 2 2 1.3 CC(C(C1=CC=CC=C1)O)NC None
None 223095 0 Functional -1 40 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 153 3 3 3 -1.4 C(C(C(=O)O)N)S(=O)O None
None 223096 0 Functional -1 39 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 169 3 3 4 -1.7 C(C(C(=O)O)N)S(=O)(=O)O None
None 223104 0 Functional -13 40 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 149 2 1 2 1.2 CC(C(=O)C1=CC=CC=C1)N None
1576 223105 0 Functional -16 40 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 163 3 1 2 1.5 CC(C(=O)C1=CC=CC=C1)NC None
177120 223115 0 3H-LY354740 - 1 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 169 3 4 3 -1.4 C(C(C(=O)O)N)P(=O)(O)O None
194385 223124 0 Functional 1 2 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 172 3 3 4 -1.1 C1=C(ONC1=O)CC(C(=O)O)N None
194385 223124 0 Functional -1 2 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 172 3 3 4 -1.1 C1=C(ONC1=O)CC(C(=O)O)N None
6604769 223141 0 Functional 1 2 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 145 2 3 3 -1.1 C1C(NC1C(=O)O)C(=O)O None
6604769 223141 0 Functional -1 2 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 145 2 3 3 -1.1 C1C(NC1C(=O)O)C(=O)O None
None 223142 0 Functional 1 3 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 245 3 3 4 0.2 CC(C1=CC=C(C=C1)S(=O)(=O)O)(C(=O)O)N None
None 223142 0 Functional -1 3 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 245 3 3 4 0.2 CC(C1=CC=C(C=C1)S(=O)(=O)O)(C(=O)O)N None
None 223143 0 Functional 1 2 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 233 3 2 6 -0.1 CC(C1=CC=C(C=C1)N2C=NN=N2)(C(=O)O)N None
None 223143 0 Functional -1 2 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 233 3 2 6 -0.1 CC(C1=CC=C(C=C1)N2C=NN=N2)(C(=O)O)N None
None 223144 0 Functional 1 3 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 197 4 4 3 -0.6 CC(CCP(=O)(O)O)(C(=O)O)N None
None 223144 0 Functional -1 3 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 197 4 4 3 -0.6 CC(CCP(=O)(O)O)(C(=O)O)N None
None 223179 0 Functional - 1 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 396 2 0 4 4.7 CC(=O)C1(C(=C)CC2C1(CCC3C2CC(=C)C4=CC(=O)CCC34C)C)OC(=O)C None
None 223188 0 Functional 1 2 Human 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 250 3 3 4 -0.3 C(C1=C(C(=O)NO1)Br)C(C(=O)O)N None
None 223188 0 Functional -1 2 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 250 3 3 4 -0.3 C(C1=C(C(=O)NO1)Br)C(C(=O)O)N None
None 223269 0 Functional 1 2 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 144 2 2 2 -0.7 CC(C(=O)NC)NC(=O)C None
None 223270 0 Functional 1 2 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 161 5 3 3 -0.3 C(CC(C(=O)O)N)CC(=O)O None
1376 7109 55 3H-M-MPEP 91 2 Rat 6.0 pKi = 6.0 Binding
NoneNone
PDSP KiDatabase 221 2 3 3 0.6 OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O None
2071 7109 55 3H-M-MPEP 91 2 Rat 6.0 pKi = 6.0 Binding
NoneNone
PDSP KiDatabase 221 2 3 3 0.6 OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O None
CHEMBL313938 7109 55 3H-M-MPEP 91 2 Rat 6.0 pKi = 6.0 Binding
NoneNone
PDSP KiDatabase 221 2 3 3 0.6 OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O None
1310 9095 110 3H-LY354740 -13 18 Rat 6.0 pKi = 6.0 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 9095 110 3H-LY354740 -13 18 Rat 6.0 pKi = 6.0 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 9095 110 3H-LY354740 -13 18 Rat 6.0 pKi = 6.0 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 9095 110 3H-LY354740 -13 18 Rat 6.0 pKi = 6.0 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 9095 110 3H-LY354740 -13 18 Rat 6.0 pKi = 6.0 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 9095 110 3H-LY354740 -13 18 Rat 6.0 pKi = 6.0 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 9095 110 3H-LY354740 -13 18 Rat 6.0 pKi = 6.0 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1310 9095 110 Functional -13 18 Rat 5.9 pKi = 5.9 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 9095 110 Functional -13 18 Rat 5.9 pKi = 5.9 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 9095 110 Functional -13 18 Rat 5.9 pKi = 5.9 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 9095 110 Functional -13 18 Rat 5.9 pKi = 5.9 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 9095 110 Functional -13 18 Rat 5.9 pKi = 5.9 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 9095 110 Functional -13 18 Rat 5.9 pKi = 5.9 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 9095 110 Functional -13 18 Rat 5.9 pKi = 5.9 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
None 222951 0 3H-LY354740 1 7 Rat 5.7 pKi = 5.7 Binding
NoneNone
PDSP KiDatabase 173 2 3 3 -0.3 C1CC(CC1C(=O)O)(C(=O)O)N None
None 222951 0 Functional 1 7 Rat 5.7 pKi = 5.7 Binding
NoneNone
PDSP KiDatabase 173 2 3 3 -0.3 C1CC(CC1C(=O)O)(C(=O)O)N None
None 223113 0 Functional -5 3 Human 6.5 pKi = 6.5 Binding
NoneNone
PDSP KiDatabase 203 4 4 4 -1.6 C1(C(C1C(=O)O)C(=O)O)C(C(=O)O)N None
None 223178 0 Functional - 1 Human 5.5 pKi = 5.5 Binding
NoneNone
PDSP KiDatabase 174 2 4 4 -1.8 C1C(NCC1(C(=O)O)N)C(=O)O None
1310 9095 110 Functional -22 18 Human 5.4 pKi = 5.4 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 9095 110 Functional -22 18 Human 5.4 pKi = 5.4 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 9095 110 Functional -22 18 Human 5.4 pKi = 5.4 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 9095 110 Functional -22 18 Human 5.4 pKi = 5.4 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 9095 110 Functional -22 18 Human 5.4 pKi = 5.4 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 9095 110 Functional -22 18 Human 5.4 pKi = 5.4 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 9095 110 Functional -22 18 Human 5.4 pKi = 5.4 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
None 223113 0 3H-LY354740 3 3 Rat 7.2 pKi = 7.2 Binding
NoneNone
PDSP KiDatabase 203 4 4 4 -1.6 C1(C(C1C(=O)O)C(=O)O)C(C(=O)O)N None
None 223114 0 3H-LY354740 - 1 Rat 7.2 pKi = 7.2 Binding
NoneNone
PDSP KiDatabase 159 3 3 3 -0.9 C1C(C1C(=O)O)C(C(=O)O)N None
114827 223111 0 3H-LY341495 3 3 Rat 7.1 pKi = 7.1 Binding
NoneNone
PDSP KiDatabase 185 2 3 3 -0.5 C1CC(C2C1C2C(=O)O)(C(=O)O)N None
114827 223111 0 3H-LY341495 -3 3 Human 7.1 pKi = 7.1 Binding
NoneNone
PDSP KiDatabase 185 2 3 3 -0.5 C1CC(C2C1C2C(=O)O)(C(=O)O)N None
1310 9095 110 Functional -13 18 Rat 5.1 pKi = 5.1 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 9095 110 Functional -13 18 Rat 5.1 pKi = 5.1 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 9095 110 Functional -13 18 Rat 5.1 pKi = 5.1 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 9095 110 Functional -13 18 Rat 5.1 pKi = 5.1 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 9095 110 Functional -13 18 Rat 5.1 pKi = 5.1 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 9095 110 Functional -13 18 Rat 5.1 pKi = 5.1 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 9095 110 Functional -13 18 Rat 5.1 pKi = 5.1 Binding
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
114827 223111 0 3H-LY354740 3 3 Rat 8.1 pKi = 8.1 Binding
NoneNone
PDSP KiDatabase 185 2 3 3 -0.5 C1CC(C2C1C2C(=O)O)(C(=O)O)N None
49822115 8927 21 None - 1 Human 8.3 pKi = 8.3 Binding
Homologous displacement assay.Homologous displacement assay.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
8947 8927 21 None - 1 Human 8.3 pKi = 8.3 Binding
Homologous displacement assay.Homologous displacement assay.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
CHEMBL3947764 8927 21 None - 1 Human 8.3 pKi = 8.3 Binding
Homologous displacement assay.Homologous displacement assay.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
49836087 7847 0 None - 1 Human 6.0 pKi = 6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
6222 7847 0 None - 1 Human 6.0 pKi = 6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
CHEMBL1630805 7847 0 None - 1 Human 6.0 pKi = 6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
49858118 7894 0 None - 1 Human 6.1 pKi = 6.1 Binding
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
6224 7894 0 None - 1 Human 6.1 pKi = 6.1 Binding
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
CHEMBL1630807 7894 0 None - 1 Human 6.1 pKi = 6.1 Binding
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
49858117 7875 4 None - 1 Human 6.2 pKi = 6.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
6223 7875 4 None - 1 Human 6.2 pKi = 6.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
CHEMBL1630806 7875 4 None - 1 Human 6.2 pKi = 6.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
11310142 9200 19 None 1 2 Human 6.8 pKi = 6.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 26341392
11614 9200 19 None 1 2 Human 6.8 pKi = 6.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 26341392
CHEMBL192051 9200 19 None 1 2 Human 6.8 pKi = 6.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 26341392
11158623 10124 11 None -8 2 Human 7.3 pKi = 7.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
6226 10124 11 None -8 2 Human 7.3 pKi = 7.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
CHEMBL1629855 10124 11 None -8 2 Human 7.3 pKi = 7.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
49765871 8926 45 None - 1 Human 7.8 pKi = 7.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
6317 8926 45 None - 1 Human 7.8 pKi = 7.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
CHEMBL2179319 8926 45 None - 1 Human 7.8 pKi = 7.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
11158623 10124 11 None 8 2 Rat 8.3 pKi = 8.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
6226 10124 11 None 8 2 Rat 8.3 pKi = 8.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
CHEMBL1629855 10124 11 None 8 2 Rat 8.3 pKi = 8.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
6325 10131 0 None - 1 Rat 8.3 pKi = 8.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 474 3 2 4 5.4 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cccc(c1)S(=O)(=O)O 21470207
73755206 10131 0 None - 1 Rat 8.3 pKi = 8.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 474 3 2 4 5.4 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cccc(c1)S(=O)(=O)O 21470207
6324 10126 0 None - 1 Rat 8.6 pKi = 8.6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 512 2 1 6 4.5 FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F 21470207
73755205 10126 0 None - 1 Rat 8.6 pKi = 8.6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 512 2 1 6 4.5 FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F 21470207
1373 9253 51 None -6 5 Human 3.8 pKi None 3.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10530814
139055582 9253 51 None -6 5 Human 3.8 pKi None 3.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10530814
446355 9253 51 None -6 5 Human 3.8 pKi None 3.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10530814
CHEMBL257626 9253 51 None -6 5 Human 3.8 pKi None 3.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10530814
DB04256 9253 51 None -6 5 Human 3.8 pKi None 3.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10530814
104766 6822 42 None -11 11 Human 4.2 pKi None 4.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10530814
1365 6822 42 None -11 11 Human 4.2 pKi None 4.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10530814
CHEMBL34453 6822 42 None -11 11 Human 4.2 pKi None 4.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10530814
1400 8320 0 None -7 2 Rat 4.5 pKi None 4.5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 10884552
1400 8320 0 None -7 2 Rat 4.5 pKi None 4.5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 9504391
5311079 8320 0 None -7 2 Rat 4.5 pKi None 4.5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 10884552
5311079 8320 0 None -7 2 Rat 4.5 pKi None 4.5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 9504391
CHEMBL1450466 8320 0 None -7 2 Rat 4.5 pKi None 4.5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 10884552
CHEMBL1450466 8320 0 None -7 2 Rat 4.5 pKi None 4.5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 9504391
1373 9253 51 None 6 5 Rat 4.6 pKi None 4.6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 9504391
139055582 9253 51 None 6 5 Rat 4.6 pKi None 4.6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 9504391
446355 9253 51 None 6 5 Rat 4.6 pKi None 4.6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 9504391
CHEMBL257626 9253 51 None 6 5 Rat 4.6 pKi None 4.6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 9504391
DB04256 9253 51 None 6 5 Rat 4.6 pKi None 4.6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 9504391
1374 8862 35 None -12 2 Rat 4.8 pKi None 4.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 9504391
5311455 8862 35 None -12 2 Rat 4.8 pKi None 4.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 9504391
CHEMBL39372 8862 35 None -12 2 Rat 4.8 pKi None 4.8 Binding
UnclassifiedUnclassified
Guide to Pharmacology 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 9504391
1310 9095 110 None -22 18 Human 4.9 pKi None 4.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
1369 9095 110 None -22 18 Human 4.9 pKi None 4.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
33032 9095 110 None -22 18 Human 4.9 pKi None 4.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
44272391 9095 110 None -22 18 Human 4.9 pKi None 4.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
88747398 9095 110 None -22 18 Human 4.9 pKi None 4.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
CHEMBL575060 9095 110 None -22 18 Human 4.9 pKi None 4.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
DB00142 9095 110 None -22 18 Human 4.9 pKi None 4.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
1392 6861 48 None -1 2 Human 5.0 pKi None 5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10530814
5310984 6861 48 None -1 2 Human 5.0 pKi None 5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10530814
CHEMBL40086 6861 48 None -1 2 Human 5.0 pKi None 5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10530814
104766 6822 42 None -3 11 Rat 5.2 pKi None 5.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10884552
104766 6822 42 None -3 11 Rat 5.2 pKi None 5.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 9504391
1365 6822 42 None -3 11 Rat 5.2 pKi None 5.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10884552
1365 6822 42 None -3 11 Rat 5.2 pKi None 5.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 9504391
CHEMBL34453 6822 42 None -3 11 Rat 5.2 pKi None 5.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10884552
CHEMBL34453 6822 42 None -3 11 Rat 5.2 pKi None 5.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 9504391
1398 7153 0 None 7 2 Rat 5.3 pKi None 5.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 199 4 4 4 -1.1 OC(=O)C(COP(=O)(O)O)(N)C 9504391
3964633 7153 0 None 7 2 Rat 5.3 pKi None 5.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 199 4 4 4 -1.1 OC(=O)C(COP(=O)(O)O)(N)C 9504391
CHEMBL1437137 7153 0 None 7 2 Rat 5.3 pKi None 5.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 199 4 4 4 -1.1 OC(=O)C(COP(=O)(O)O)(N)C 9504391
1310 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
1310 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
1369 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
1369 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
33032 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
33032 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
44272391 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
44272391 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
88747398 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
88747398 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
CHEMBL575060 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
CHEMBL575060 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
DB00142 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
DB00142 9095 110 None -13 18 Rat 5.7 pKi None 5.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
1368 9070 37 None -3 11 Human 6.3 pKi None 6.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10530814
5310956 9070 37 None -3 11 Human 6.3 pKi None 6.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10530814
CHEMBL280563 9070 37 None -3 11 Human 6.3 pKi None 6.3 Binding
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10530814
1377 8122 26 None -2 6 Human 6.5 pKi None 6.5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10530814
5310979 8122 26 None -2 6 Human 6.5 pKi None 6.5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10530814
CHEMBL284193 8122 26 None -2 6 Human 6.5 pKi None 6.5 Binding
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10530814
1368 9070 37 None 1 11 Rat 6.9 pKi None 6.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10884552
1368 9070 37 None 1 11 Rat 6.9 pKi None 6.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 9504391
5310956 9070 37 None 1 11 Rat 6.9 pKi None 6.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10884552
5310956 9070 37 None 1 11 Rat 6.9 pKi None 6.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 9504391
CHEMBL280563 9070 37 None 1 11 Rat 6.9 pKi None 6.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10884552
CHEMBL280563 9070 37 None 1 11 Rat 6.9 pKi None 6.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 9504391
1393 8321 64 None -2 6 Human 6.9 pKi None 6.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10530814
1396 8321 64 None -2 6 Human 6.9 pKi None 6.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10530814
213056 8321 64 None -2 6 Human 6.9 pKi None 6.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10530814
CHEMBL8759 8321 64 None -2 6 Human 6.9 pKi None 6.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10530814
1377 8122 26 None -1 6 Rat 7.0 pKi None 7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10884552
1377 8122 26 None -1 6 Rat 7.0 pKi None 7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 9504391
5310979 8122 26 None -1 6 Rat 7.0 pKi None 7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10884552
5310979 8122 26 None -1 6 Rat 7.0 pKi None 7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 9504391
CHEMBL284193 8122 26 None -1 6 Rat 7.0 pKi None 7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10884552
CHEMBL284193 8122 26 None -1 6 Rat 7.0 pKi None 7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 9504391
1393 8321 64 None 1 6 Rat 7.9 pKi None 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
1393 8321 64 None 1 6 Rat 7.9 pKi None 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 9504391
1396 8321 64 None 1 6 Rat 7.9 pKi None 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
1396 8321 64 None 1 6 Rat 7.9 pKi None 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 9504391
213056 8321 64 None 1 6 Rat 7.9 pKi None 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
213056 8321 64 None 1 6 Rat 7.9 pKi None 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 9504391
CHEMBL8759 8321 64 None 1 6 Rat 7.9 pKi None 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
CHEMBL8759 8321 64 None 1 6 Rat 7.9 pKi None 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 9504391
10197984 9199 44 None 2 5 Human 7.9 pKi None 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10090786
1394 9199 44 None 2 5 Human 7.9 pKi None 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10090786
CHEMBL275079 9199 44 None 2 5 Human 7.9 pKi None 7.9 Binding
UnclassifiedUnclassified
Guide to Pharmacology 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10090786
1378 9195 54 None -1 10 Rat 8.4 pKi None 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10884552
1378 9195 54 None -1 10 Rat 8.4 pKi None 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 9504391
1399 9195 54 None -1 10 Rat 8.4 pKi None 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10884552
1399 9195 54 None -1 10 Rat 8.4 pKi None 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 9504391
9819927 9195 54 None -1 10 Rat 8.4 pKi None 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10884552
9819927 9195 54 None -1 10 Rat 8.4 pKi None 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 9504391
CHEMBL432038 9195 54 None -1 10 Rat 8.4 pKi None 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10884552
CHEMBL432038 9195 54 None -1 10 Rat 8.4 pKi None 8.4 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 9504391
1378 9195 54 None -2 10 Human 8.6 pKi None 8.6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
1399 9195 54 None -2 10 Human 8.6 pKi None 8.6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
9819927 9195 54 None -2 10 Human 8.6 pKi None 8.6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
CHEMBL432038 9195 54 None -2 10 Human 8.6 pKi None 8.6 Binding
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
1397 9307 15 None -1 5 Rat 8.7 pKi None 8.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 14975669
1397 9307 15 None -1 5 Rat 8.7 pKi None 8.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 15317467
9886034 9307 15 None -1 5 Rat 8.7 pKi None 8.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 14975669
9886034 9307 15 None -1 5 Rat 8.7 pKi None 8.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 15317467
CHEMBL186453 9307 15 None -1 5 Rat 8.7 pKi None 8.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 14975669
CHEMBL186453 9307 15 None -1 5 Rat 8.7 pKi None 8.7 Binding
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 15317467
1395 9306 15 None 2 2 Rat 9.2 pKi None 9.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 11123999
9837317 9306 15 None 2 2 Rat 9.2 pKi None 9.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 11123999
CHEMBL121053 9306 15 None 2 2 Rat 9.2 pKi None 9.2 Binding
UnclassifiedUnclassified
Guide to Pharmacology 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 11123999