Ligand source activities (1 row/activity)



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Ligands (move mouse cursor over ligand name to see structure) Receptor Assay information Chemical information
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10353365 83247 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 83247 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 142133 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 142133 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 142226 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 142226 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 142213 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 142213 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 2528 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 2528 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 2528 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 2528 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 2528 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 2528 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 123406 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 123406 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 123405 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 123405 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 156122 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 156122 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 2528 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 2528 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 2528 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 142237 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 142237 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 142312 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 142312 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 142159 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 142159 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 142200 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 142200 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 1539 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 1539 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 1539 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 1539 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 142223 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 142223 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 174547 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 174547 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 82648 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 82648 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 178028 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 178028 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 167397 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 167397 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 123397 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 123397 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 83901 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 83901 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 119304 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 119304 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 74588 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 74588 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 74608 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 74608 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 74612 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 74612 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 158045 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 158045 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 152069 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 152069 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 158293 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 158293 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 158293 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 192693 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 192693 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 67230 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 67230 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 114559 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 114559 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 82637 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 82637 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 165796 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 165796 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 3802 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 3802 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 3802 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 67259 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 67259 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 169839 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 169839 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 114557 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 114557 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 74606 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 74606 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 149158 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 149158 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 201362 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 201362 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 144885 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 144885 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 66314 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 66314 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 200045 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 200045 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 83910 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 83910 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 142198 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 142198 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 142222 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 142222 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 192372 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 192372 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 123403 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 123403 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 177238 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 177238 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 123399 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 123399 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 80809 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 80809 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 74587 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 74587 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 61975 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 61975 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 114499 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 114499 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 82635 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 82635 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 68027 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 68027 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 74581 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 74581 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 82639 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 82639 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 82642 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 82642 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 145682 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 145682 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 184262 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 184262 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 90061 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 90061 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 8699 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 8699 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 74583 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 74583 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 126808 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 126808 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 153891 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 153891 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 170835 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 170835 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 8846 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 8846 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 111866 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 111866 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 177238 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 177238 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 157111 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 157111 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 123402 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 123402 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 80808 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 80808 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 177434 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 177434 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 177687 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 177687 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 8690 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 8690 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 177687 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 177687 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 182669 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 182669 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 8548 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 8548 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 146085 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 146085 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 82633 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 82633 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 82647 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 82647 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 177434 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 177434 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 82654 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 82654 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 109538 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 109538 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 57724 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 57724 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 57743 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 57743 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 1872 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 1872 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 1872 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 173840 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 173840 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 109549 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 109549 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 74601 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 74601 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 123400 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 123400 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 142306 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 142306 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 142314 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 142314 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 172179 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 172179 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 61964 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 61964 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 166542 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 166542 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 123398 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 123398 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 180185 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 180185 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 201935 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 201935 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 8692 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 8692 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 101400 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 101400 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 124401 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 124401 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 149062 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 149062 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 8547 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 8547 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 166464 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 166464 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 67326 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 67326 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 190484 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 190484 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 183513 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 183513 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 74607 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 74607 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 8584 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 8584 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 183468 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 183468 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 175177 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 175177 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 166963 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 166963 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 144859 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 144859 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 173278 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 173278 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 174156 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 174156 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 114570 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 114570 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 170370 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 170370 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 199693 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 199693 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 184302 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 184302 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 148147 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 148147 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 61957 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 61957 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 123404 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 123404 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 2144 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 2144 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 2144 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 2144 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 158618 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 158618 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 74599 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 74599 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 171304 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 171304 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 82645 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 82645 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 172694 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 172694 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 171944 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 171944 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 176000 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 176000 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 158744 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 158744 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 80811 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 80811 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 64313 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 64313 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 2143 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 2143 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 2143 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 2143 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 114579 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 114579 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 156894 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 156894 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 114800 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 114800 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 64878 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 64878 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 114800 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 114800 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 177210 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 177210 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 177914 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 177914 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 171511 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 171511 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 82652 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 82652 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 192750 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 192750 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 188665 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 188665 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 178028 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 178028 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 57742 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 57742 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 199845 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 199845 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 171852 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 171852 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 173840 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 173840 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 109544 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 109544 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 157629 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 157629 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 57727 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 57727 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 61956 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 61956 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 167150 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 167150 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 155947 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 155947 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 142302 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 142302 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 2146 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 2146 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 2146 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 148600 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 148600 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 123401 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 123401 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 114499 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 114499 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 80810 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 80810 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 178028 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 178028 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 177210 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 177210 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 177914 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 177914 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 109713 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 109713 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2422 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 2422 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 2422 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 61958 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 61958 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 74610 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 74610 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 146992 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 146992 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 192742 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 192742 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 80802 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 80802 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 61961 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 61961 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 142283 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 142283 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 175885 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 175885 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 2145 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 2145 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 2145 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 158422 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 158422 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 156364 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 156364 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 156472 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 156472 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 152716 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 152716 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 147314 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 147314 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 114580 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 114580 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 181192 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 181192 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 122 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 122 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 122 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 118764 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 118764 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 66693 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 66693 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 74597 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 74597 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 192747 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 192747 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 8850 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 8850 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 146844 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 146844 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 173840 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 173840 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 114567 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 114567 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 82640 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 82640 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 142279 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 142279 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 170400 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 170400 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 175621 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 175621 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 158513 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 158513 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 83247 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 83247 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 2146 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 2146 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 2146 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 1539 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 1539 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 1539 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 1539 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 156225 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 156225 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 156908 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 156908 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 142324 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 142324 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 179423 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 179423 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 171248 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 171248 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 184644 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 184644 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 33 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 33 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 33 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 184240 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 184240 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 180121 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 180121 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 61973 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 61973 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 201635 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 201635 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 74589 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 74589 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 201635 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 201635 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 165901 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 165901 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 123409 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 123409 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 156124 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 156124 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 158961 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 158961 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 80804 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 80804 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 173268 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 173268 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 8504 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 8504 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 114582 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 114582 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 61962 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 61962 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 65008 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 65008 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 109541 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 109541 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 109550 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 109550 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 109551 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 109551 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 57741 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 57741 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 1871 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 1871 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 1871 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 199759 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 199759 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 200048 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 200048 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 109545 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 109545 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 2421 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 2421 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 2421 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 2421 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 2421 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 2421 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 2421 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 2421 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 2421 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 159461 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 159461 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 83902 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 83902 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 142304 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 142304 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 172194 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 172194 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 148556 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 148556 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 214323 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 123407 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 123407 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 123396 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 123396 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 166542 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 166542 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 73 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 73 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 73 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 33 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 33 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 33 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 143637 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 143637 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 170374 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 170374 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 74598 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 74598 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 191606 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 191606 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 36473 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 36473 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 123396 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 123396 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 90057 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 90057 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 177834 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 177834 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 172829 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 172829 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 33 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 33 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 33 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 199696 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 199696 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 177834 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 177834 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 80801 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 80801 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 146549 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 146549 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 8543 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 8543 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 61977 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 61977 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 201935 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 201935 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 123396 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 123396 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 184924 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 184924 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 143931 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 143931 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 156050 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 156050 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 158290 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 158290 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 174909 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 174909 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 123644 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 123644 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 153548 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 153548 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 66805 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 66805 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 180654 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 180654 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 66338 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 66338 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 199717 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 199717 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 171638 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 171638 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 137600 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 137600 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 80803 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 80803 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 177238 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 177238 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 74613 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 74613 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 142325 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 142325 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 13129 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 13129 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 13129 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 177238 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 177238 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 201669 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 201669 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 192372 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 192372 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 188656 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 188656 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 82643 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 82643 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 8804 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 8804 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 182768 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 182768 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 13355 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 13355 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 13355 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 123408 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 123408 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 181251 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 181251 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 177250 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 177250 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 61971 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 61971 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 61970 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 61970 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 157338 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 157338 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 80813 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 80813 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 8696 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 8696 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 167150 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 167150 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 214857 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 215282 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 177250 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 177250 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 114581 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 114581 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 57745 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 57745 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 109539 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 109539 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 109540 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 109540 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 109543 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 109543 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 109552 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 109552 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 158741 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 158741 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 57728 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 57728 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 200046 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 200046 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 200174 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 200174 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 201462 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 201462 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 57722 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 57722 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 8693 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 8693 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 90059 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 90059 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 83906 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 83906 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 185041 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 185041 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 159284 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 159284 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 74585 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 74585 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 182369 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 182369 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 184805 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 184805 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 74609 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 74609 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 214300 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 114800 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 114800 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 145755 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 145755 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 170014 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 170014 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 664 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 664 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 664 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 2145 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 2145 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 2145 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 183526 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 183526 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 169594 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 169594 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 8736 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 8736 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 142174 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 142174 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 167397 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 167397 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 181503 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 181503 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 184915 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 184915 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 74605 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 74605 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 157655 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 157655 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 191475 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 191475 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 142310 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 142310 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 142310 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 142310 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 175429 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 175429 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 61976 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 61976 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 192732 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 192732 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 145276 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 145276 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 157189 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 157189 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 144580 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 144580 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 184301 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 184301 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 214219 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 114566 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 114566 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 61963 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 61963 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 142152 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 142152 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 171035 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 171035 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 114800 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 114800 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 155863 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 155863 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 156463 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 156463 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 158749 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 158749 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 167033 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 167033 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 177922 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 177922 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 74586 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 74586 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 170926 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 170926 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 215325 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 142766 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 142766 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 177922 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 177922 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 114556 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 114556 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 82653 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 82653 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 61979 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 61979 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 158568 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 158568 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 206508 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 206508 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 206508 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 206508 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 184259 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 184259 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 74614 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 74614 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 182022 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 182022 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 175638 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 175638 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 182022 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 182022 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 215006 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 158140 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 158140 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 42 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 42 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 42 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 42 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 177031 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 177031 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 1340 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 1340 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 1340 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 2290 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 2290 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 2290 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 34972 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 34972 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 73 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 73 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 73 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 67334 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 67334 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 177031 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 177031 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 192553 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 192553 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 149429 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 149429 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 114563 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 114563 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 83900 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 83900 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 114578 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 114578 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 61981 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 61981 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 214591 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 166464 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 166464 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 1105 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 1105 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 1105 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 57739 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 57739 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 57740 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 57740 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 109547 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 109547 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 177761 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 177761 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 57729 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 57729 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 201615 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 201615 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 114561 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 114561 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 74582 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 74582 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 67479 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 67479 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 146050 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 146050 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 191467 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 191467 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 142171 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 142171 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 80807 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 80807 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 182968 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 182968 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 177687 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 177687 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 177761 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 177761 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 148600 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 148600 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 177521 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 177521 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 177687 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 177687 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 64799 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 64799 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 171732 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 171732 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 61975 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 61975 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 157093 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 157093 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 80806 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 80806 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 167033 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 167033 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 177521 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 177521 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 8512 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 8512 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 13651 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 13651 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 13651 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 61955 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 61955 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 114560 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 114560 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 149349 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 149349 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 139163 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 139163 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 155894 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 155894 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 114499 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 114499 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 1539 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 1539 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 1539 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 1539 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 65603 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 65603 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 179791 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 179791 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 184643 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 184643 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 184022 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 184022 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 8993 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 8993 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 74604 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 74604 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 3224 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 3224 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 3224 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 3224 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 3224 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 3224 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 184300 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 184300 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 114575 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 114575 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 61981 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 61981 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 61982 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 61982 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 1539 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 1539 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 1539 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 1539 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 83902 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 83902 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 8803 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 8803 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 181512 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 181512 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 214452 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 8694 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 8694 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 206570 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 206570 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 206570 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 13284 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 13284 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 13284 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 67511 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 67511 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 114568 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 114568 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 150298 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 150298 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 67093 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 67093 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 8582 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 8582 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 8802 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 8802 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 8996 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 8996 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 114555 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 114555 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 35874 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 35874 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 74584 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 74584 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 83905 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 83905 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 83902 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 83902 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 175075 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 175075 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 13378 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 13378 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 13378 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 148556 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 148556 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 74617 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 74617 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 156461 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 156461 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 184641 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 184641 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 8684 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 8684 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 184807 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 184807 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 65202 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 65202 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 66336 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 66336 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 82638 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 82638 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 8910 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 8910 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 82644 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 82644 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 148303 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 148303 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 123397 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 123397 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 74616 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 74616 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 214851 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 142687 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 142687 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 2422 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 2422 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 2422 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 74602 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 74602 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 57736 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 57736 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 57744 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 57744 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 109542 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 109542 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 57726 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 57726 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 201935 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 201935 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 201987 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 201987 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 31341 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 31341 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 142255 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 142255 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 83911 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 83911 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 123400 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 123400 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 180652 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 180652 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 183331 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 183331 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 214842 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 157153 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 157153 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 157174 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 157174 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 181737 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 181737 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 174598 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 174598 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 82646 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 82646 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 13459 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 13459 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 13459 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 142539 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 142539 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 192344 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 192344 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 157193 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 157193 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 157260 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 157260 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 8542 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 8542 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 74590 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 74590 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 159236 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 159236 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 179598 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 179598 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 66080 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 66080 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 61960 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 61960 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 147669 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 147669 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 184352 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 184352 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 123404 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 123404 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 178011 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 178011 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 664 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 664 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 664 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 8849 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 8849 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 178011 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 178011 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 199963 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 199963 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 200092 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 200092 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 74600 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 74600 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 36386 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 36386 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 1340 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 1340 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 1340 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 126776 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 126776 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 8584 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 8584 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 66722 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 66722 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 61972 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 61972 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 66081 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 66081 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 114574 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 114574 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 123402 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 123402 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 123396 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 123396 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 74596 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 74596 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 114564 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 114564 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 82634 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 82634 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 157655 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 157655 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 145315 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 145315 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 13033 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 13033 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 13033 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 179629 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 179629 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 177250 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 177250 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 74592 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 74592 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 192093 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 192093 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 61953 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 61953 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 114573 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 114573 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 61960 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 61960 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 123396 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 123396 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 148772 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 148772 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 73 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 73 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 73 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 177250 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 177250 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 101382 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 101382 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 2081 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 2081 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 2081 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 192681 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 192681 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 114572 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 114572 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 193050 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 193050 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 193050 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 1073 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 1073 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 1073 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 5582 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 5582 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 184336 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 184336 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 31341 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 31341 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 123409 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 123409 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 83902 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 83902 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 83902 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 83902 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 142268 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 142268 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 123396 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 123396 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 158525 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 158525 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 180050 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 180050 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 182053 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 182053 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 169704 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 169704 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 172496 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 172496 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 214351 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 215319 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 35817 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 35817 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 33 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 33 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 33 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 80805 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 80805 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 82650 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 82650 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 57737 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 57737 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 109537 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 109537 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 109548 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 109548 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 109554 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 109554 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 57722 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 57722 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 57723 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 57723 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 57732 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 57732 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 199758 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 199758 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 109553 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 109553 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 156588 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 156588 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 177210 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 177210 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 177914 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 177914 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 149275 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 149275 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 177210 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 177210 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 177914 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 177914 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 82649 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 82649 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 182837 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 182837 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 8314 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 8314 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 8314 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 184916 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 184916 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 123399 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 123399 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 177434 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 177434 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 177434 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 177434 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 123398 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 123398 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 179609 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 179609 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 181932 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 181932 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 215240 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 177521 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 177521 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 114552 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 114552 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 82636 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 82636 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 177521 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 177521 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 74595 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 74595 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 182736 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 182736 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 64768 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 64768 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 66800 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 66800 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 123429 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 123429 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 82655 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 82655 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 147449 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 147449 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 82655 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 82655 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 159658 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 159658 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 146264 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 146264 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 555 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 555 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 555 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 555 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 144706 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 144706 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 157274 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 157274 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 7868 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 7868 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 144706 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 144706 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 65234 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 65234 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 65269 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 65269 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 8875 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 8875 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 214742 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 8546 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 8546 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 189023 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 189023 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 8655 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 8655 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 8848 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 8848 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 8873 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 8873 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 145853 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 145853 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 192440 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 192440 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 67343 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 67343 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 83904 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 83904 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 175934 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 175934 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 151811 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 151811 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 142285 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 142285 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 123406 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 123406 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 156787 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 156787 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 123407 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 123407 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 142167 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 142167 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 83909 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 83909 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 158921 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 158921 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 142209 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 142209 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 174895 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 174895 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 175971 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 175971 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 215041 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 215179 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 215452 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 170701 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 170701 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 83899 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 83899 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 80569 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 80569 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 80569 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 214326 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 14186 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 14186 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 14186 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 80799 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 80799 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 214654 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 174859 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 174859 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 158338 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 158338 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 214431 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 57725 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 57725 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 57731 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 57731 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 57738 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 57738 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 199675 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 199675 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 202613 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 202613 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 157225 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 157225 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 199696 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 199696 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 199977 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 199977 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 200047 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 200047 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 200134 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 200134 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 201362 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 201362 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 184659 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 184659 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 67107 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 67107 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 74615 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 74615 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 174142 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 174142 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 143621 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 143621 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 158390 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 158390 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 114800 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 114800 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 8508 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 8508 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 8698 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 8698 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 8759 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 8759 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 200091 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 200091 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 74591 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 74591 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 182108 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 182108 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 68232 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 68232 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 8994 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 8994 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 114562 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 114562 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 8218 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 8218 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 66654 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 66654 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 143147 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 143147 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 65601 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 65601 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 114577 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 114577 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 175120 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 175120 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 145045 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 145045 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 123403 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 123403 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 82651 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 82651 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 192074 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 192074 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 156545 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 156545 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 83907 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 83907 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 61959 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 61959 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 157035 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 157035 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 123405 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 123405 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 184494 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 184494 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 177031 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 177031 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 177031 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 177031 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 184260 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 184260 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 182011 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 182011 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 183415 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 183415 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 173659 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 173659 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 175620 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 175620 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 176049 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 176049 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 173797 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 173797 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 80800 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 80800 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 8507 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 8507 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 142191 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 142191 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 143147 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 143147 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 192484 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 192484 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 172015 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 172015 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 123408 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 123408 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 82632 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 82632 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 158356 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 158356 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 183296 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 183296 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 61974 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 61974 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 189008 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 189008 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 181669 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 181669 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 124319 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 124319 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 193370 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 193370 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 192739 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 192739 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 184913 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 184913 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 61977 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 61977 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 8697 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 8697 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 133922 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 133922 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 157166 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 157166 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 66228 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 66228 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 67530 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 67530 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 199759 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 199759 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 8999 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 8999 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 8752 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 8752 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 61978 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 61978 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 67434 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 67434 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 170359 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 170359 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 215405 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 178011 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 178011 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 2143 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 2143 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 2143 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 2143 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 178011 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 178011 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 166777 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 166777 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 8691 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 8691 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 8727 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 8727 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 57730 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 57730 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 57733 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 57733 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 57735 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 57735 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 57746 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 57746 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 114827 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 114827 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 83903 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 83903 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 192484 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 192484 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 156881 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 156881 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 177922 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 177922 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 157609 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 157609 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 177922 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 177922 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 175737 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 175737 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 181106 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 181106 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 181106 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 181106 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 114569 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 114569 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 61982 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 61982 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 66667 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 66667 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 146992 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 146992 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 1073 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 1073 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 1073 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 96086 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 96086 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 74603 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 74603 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 192074 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 192074 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 172686 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 172686 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 8944 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 8944 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 96086 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 96086 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 80812 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 80812 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 199851 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 199851 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 74580 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 74580 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 74580 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 74580 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 174104 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 174104 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 61954 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 61954 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 192754 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 192754 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 157178 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 157178 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 147159 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 147159 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 123401 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 123401 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 61954 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 61954 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 114558 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 114558 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 67484 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 67484 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 184312 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 184312 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 114571 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 114571 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 65244 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 65244 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 61952 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 61952 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 156641 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 156641 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 61979 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 61979 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 177834 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 177834 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 177834 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 177834 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 83908 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 83908 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 159679 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 159679 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 178028 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 178028 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 202688 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 202688 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 181311 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 181311 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 181409 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 181409 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 182052 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 182052 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 170305 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 170305 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 177761 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 177761 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 177761 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 177761 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 190484 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 190484 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 664 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 664 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 664 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 158231 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 158231 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 74611 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 74611 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 165901 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 165901 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 2528 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 2528 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 2528 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 82641 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 82641 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 114565 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 114565 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 151107 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 151107 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 192318 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 192318 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 159392 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 159392 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 180065 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 180065 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 201917 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 201917 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 114576 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 114576 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 67295 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 67295 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 150431 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 150431 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 61980 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 61980 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 160045 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 160045 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 160169 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 160169 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 160546 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 160546 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 160106 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 160106 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 160310 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 160310 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 160180 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 160180 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 160570 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 160570 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 56306 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 56306 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 96263 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 96263 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 155282 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 155282 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 56287 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 56287 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 56290 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 56290 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 56305 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 56305 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 56413 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 56413 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 160253 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 160253 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 160657 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 160657 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 159878 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 159878 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 160743 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 160743 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 151373 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 151373 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 142893 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 142893 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 106103 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 106103 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 160424 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 160424 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 78739 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 78739 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 78742 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 78742 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 16781 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 16781 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 1110 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 1110 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 1110 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 56304 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 56304 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 174297 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 174297 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 174297 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 174297 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 160688 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 160688 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 174855 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 174855 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 175877 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 175877 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 174855 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 174855 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 175877 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 175877 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 159885 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 159885 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 160799 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 160799 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 160799 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 160799 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 96172 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 96172 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 96308 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 96308 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 56407 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 56407 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 160799 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 160799 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 145681 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 145681 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 160399 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 160399 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 160611 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 160611 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 160511 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 160511 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 78731 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 78731 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 66192 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 66192 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 112001 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 112001 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 147500 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 147500 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 183691 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 183691 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 183691 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 95863 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 95863 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 160729 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 160729 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 95384 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 95384 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 150497 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 150497 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 160936 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 160936 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 160023 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 160023 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 152255 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 152255 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 160083 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 160083 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 160744 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 160744 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 155894 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 155894 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 183622 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 183622 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 183622 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 97555 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 97555 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 56408 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 56408 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 159942 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 159942 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 148107 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 148107 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 159892 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 159892 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 160581 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 160581 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 160854 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 160854 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 160008 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 160008 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 160240 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 160240 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 160129 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 160129 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 144725 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 144725 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 106100 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 106100 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 207754 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 207754 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 106101 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 106101 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 207980 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 207980 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 111993 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 111993 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 3351 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 3351 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 3351 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 96173 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 96173 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 56419 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 56419 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 160034 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 160034 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 160506 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 160506 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 159866 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 159866 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 160916 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 160916 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 78738 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 78738 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 171135 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 171135 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 171468 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 171468 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 171135 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 171135 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 171468 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 171468 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 183670 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 183670 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 183670 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 175108 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 175108 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 175108 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 175108 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 145959 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 145959 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 56309 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 56309 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 96264 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 96264 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 155586 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 155586 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 56300 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 56300 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 160587 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 160587 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 160828 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 160828 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 160359 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 160359 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 160926 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 160926 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 160792 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 160792 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 1089 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 1089 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 1089 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 175860 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 175860 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 175860 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 175860 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 90061 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 90061 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 111992 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 111992 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 155492 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 155492 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 56297 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 56297 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 56421 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 56421 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 159895 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 159895 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 160575 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 160575 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 183653 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 183653 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 183653 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 159864 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 159864 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 153248 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 153248 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 145232 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 145232 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 159877 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 159877 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 160529 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 160529 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 56291 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 56291 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 113350 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 113350 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 107879 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 107879 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 144789 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 144789 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 168835 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 168835 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 155008 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 155008 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 155665 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 155665 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 155008 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 155008 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 183721 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 183721 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 183721 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 159846 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 159846 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 160001 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 160001 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 152675 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 152675 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 160395 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 160395 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 2400 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 2400 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 2400 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 172367 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 172367 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 172835 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 172835 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 175824 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 175824 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 172835 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 172835 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 175824 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 175824 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 172367 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 172367 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 69375 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 69375 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 112003 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 112003 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 111995 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 111995 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 96267 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 96267 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 56284 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 56284 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 56410 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 56410 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 56417 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 56417 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 160638 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 160638 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 159858 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 159858 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 159983 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 159983 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 150248 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 150248 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 160681 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 160681 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 148642 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 148642 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 160210 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 160210 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 160270 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 160270 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 16785 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 16785 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 114585 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 114585 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 116882 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 116882 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 78765 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 78765 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 154974 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 154974 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 96050 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 96050 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 108274 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 108274 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 160365 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 160365 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 160365 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 160365 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 154188 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 154188 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 160136 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 160136 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 160488 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 160488 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 160502 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 160502 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 159858 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 159858 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 160103 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 160103 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 160760 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 160760 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 144637 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 144637 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 160504 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 160504 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 160646 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 160646 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 160376 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 160376 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 160249 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 160249 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 149765 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 149765 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 56405 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 56405 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 117012 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 117012 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 117012 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 111990 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 111990 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 170908 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 170908 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 170908 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 170908 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 56307 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 56307 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 160005 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 160005 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 160010 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 160010 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 160042 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 160042 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 160124 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 160124 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 160447 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 160447 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 160679 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 160679 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 160731 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 160731 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 160525 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 160525 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 160564 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 160564 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 160404 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 160404 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 160479 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 160479 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 2529 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 2529 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 2529 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 56289 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 56289 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 142690 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 142690 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 183618 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 183618 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 183618 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 159995 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 159995 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 160579 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 160579 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 160461 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 160461 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 144900 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 144900 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 159982 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 159982 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 160476 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 160476 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 35817 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 35817 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 2417 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 2417 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 2417 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 2417 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 102126 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 102126 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 183719 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 183719 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 183719 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 2417 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 2417 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 2417 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 2417 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 148390 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 148390 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 160674 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 160674 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 160784 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 160784 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 159965 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 159965 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 160499 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 160499 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 160066 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 160066 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 160947 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 160947 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 152510 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 152510 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 147068 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 147068 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 163521 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 163521 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 96308 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 96308 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 145948 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 145948 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 160041 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 160041 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 160540 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 160540 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 152500 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 152500 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 160817 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 160817 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 145907 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 145907 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 144081 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 144081 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 16566 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 16566 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 16604 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 16604 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 173586 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 173586 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 173586 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 173586 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 142446 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 142446 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 180213 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 180213 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 2417 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 2417 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 2417 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 2417 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 95864 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 95864 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 160799 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 160799 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 160799 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 160799 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 160407 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 160407 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 160241 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 160241 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 160436 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 160436 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 78741 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 78741 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 78744 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 78744 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 160702 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 160702 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 112004 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 112004 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 112004 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 112004 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 56308 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 56308 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 148664 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 148664 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 152648 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 152648 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 160559 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 160559 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 148061 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 148061 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 160128 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 160128 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 160693 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 160693 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 172782 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 172782 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 172782 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 172782 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 169898 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 169898 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 169898 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 169898 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 56304 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 56304 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 148745 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 148745 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 160350 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 160350 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 145339 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 145339 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 183640 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 183640 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 183640 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 160100 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 160100 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 160539 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 160539 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 2417 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 2417 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 2417 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 2417 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 160072 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 160072 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 160951 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 160951 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 96174 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 96174 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 96172 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 96172 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 96308 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 96308 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 147982 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 147982 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 150290 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 150290 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 183679 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 183679 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 183679 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 146637 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 146637 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 160705 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 160705 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 159863 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 159863 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 159896 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 159896 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 154062 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 154062 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 150394 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 150394 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 169083 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 169083 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 174318 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 174318 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 174318 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 174318 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 160133 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 160133 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 160716 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 160716 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 160304 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 160304 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 95864 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 95864 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 3351 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 3351 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 3351 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 56306 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 56306 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 56425 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 56425 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 160656 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 160656 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 160932 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 160932 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 160112 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 160112 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 160462 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 160462 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 160458 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 160458 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 160466 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 160466 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 160895 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 160895 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 160017 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 160017 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 160085 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 160085 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 160342 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 160342 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 160942 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 160942 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 160542 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 160542 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 56424 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 56424 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 159868 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 159868 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 160185 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 160185 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 151262 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 151262 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 100439 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 100439 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 98739 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 98739 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 150637 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 150637 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 160805 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 160805 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 160139 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 160139 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 144871 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 144871 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 149682 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 149682 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 16564 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 16564 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 150823 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 150823 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 111994 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 111994 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 172345 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 172345 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 172345 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 172345 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 172345 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 172345 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 160866 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 160866 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 147951 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 147951 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 160772 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 160772 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 183728 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 183728 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 183728 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 157939 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 157939 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 147948 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 147948 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 150700 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 150700 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 174269 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 174269 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 174269 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 174269 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 155778 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 155778 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 160021 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 160021 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 158994 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 158994 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 56308 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 56308 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 143011 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 143011 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 160549 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 160549 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 160962 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 160962 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 149006 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 149006 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 100846 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 100846 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 171673 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 171673 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 171673 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 171673 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 96308 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 96308 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 160286 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 160286 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 102731 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 102731 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 56305 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 56305 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 160578 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 160578 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 160244 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 160244 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 153463 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 153463 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 173091 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 173091 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 173091 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 173091 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 157736 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 157736 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 157736 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 157736 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 111998 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 111998 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 56298 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 56298 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 56299 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 56299 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 56408 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 56408 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 160485 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 160485 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 160742 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 160742 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 183653 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 183653 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 183653 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 159920 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 159920 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 160746 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 160746 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 160082 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 160082 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 160297 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 160297 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 160703 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 160703 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 159970 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 159970 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 160601 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 160601 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 160769 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 160769 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 159862 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 159862 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 160108 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 160108 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 160287 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 160287 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 160600 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 160600 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 160903 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 160903 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 160928 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 160928 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 160264 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 160264 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 159901 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 159901 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 143725 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 143725 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 144114 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 144114 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 150823 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 150823 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 56408 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 56408 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 160510 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 160510 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 160503 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 160503 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 200916 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 200916 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 172899 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 172899 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 111999 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 111999 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 172899 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 172899 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 160318 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 160318 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 118494 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 118494 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 2475 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 2475 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 2475 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 2475 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 2475 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 98861 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 98861 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 86122 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 86122 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 160718 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 160718 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 172345 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 172345 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 172345 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 172345 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 172345 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 172345 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 144638 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 144638 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 183675 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 183675 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 183675 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 160087 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 160087 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 78743 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 78743 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 13032 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 13032 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 13032 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 13013 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 13013 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 13013 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 149627 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 149627 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 160855 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 160855 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 163270 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 163270 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 112002 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 112002 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 95915 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 95915 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 148314 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 148314 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 160012 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 160012 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 56296 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 56296 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 144006 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 144006 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 170252 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 170252 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 183686 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 183686 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 183686 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 149365 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 149365 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 90058 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 90058 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 56288 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 56288 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 56301 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 56301 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 56409 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 56409 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 56416 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 56416 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 160090 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 160090 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 160569 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 160569 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 160801 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 160801 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 160944 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 160944 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 160720 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 160720 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 159914 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 159914 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 160305 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 160305 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 160356 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 160356 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 159937 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 159937 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 160315 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 160315 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 1539 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 1539 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 1539 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 1539 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 160302 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 160302 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 160040 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 160040 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 160220 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 160220 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 160137 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 160137 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 56295 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 56295 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 159963 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 159963 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 101737 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 101737 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 147944 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 147944 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 202633 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 202633 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 147944 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 147944 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 160861 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 160861 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 12951 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 12951 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 12951 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 56304 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 56304 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 96647 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 96647 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 3361 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 3361 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 3361 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 142690 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 142690 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 151291 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 151291 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 173381 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 173381 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 173381 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 173381 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 156641 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 156641 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 111996 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 111996 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 153562 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 153562 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 174603 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 174603 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 174603 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 174603 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 145393 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 145393 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 56412 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 56412 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 56418 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 56418 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 214430 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 159930 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 159930 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 160905 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 160905 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 159933 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 159933 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 183687 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 183687 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 183687 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 159893 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 159893 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 118818 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 118818 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 151224 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 151224 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 102631 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 102631 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 144764 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 144764 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 100714 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 100714 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 16947 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 16947 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 161322 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 161322 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 153269 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 153269 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 147467 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 147467 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 78736 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 78736 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 151361 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 151361 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 174179 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 174179 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 174179 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 174179 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 173982 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 173982 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 174858 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 174858 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 173982 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 173982 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 174858 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 174858 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 56307 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 56307 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 56303 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 56303 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 56414 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 56414 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 160802 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 160802 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 160819 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 160819 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 159911 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 159911 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 160339 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 160339 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 160091 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 160091 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 160642 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 160642 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 2417 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 2417 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 2417 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 2417 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 160684 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 160684 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 160362 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 160362 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 160914 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 160914 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 90060 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 90060 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 90060 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 90060 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 56293 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 56293 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 144577 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 144577 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 96304 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 96304 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 151654 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 151654 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 95934 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 95934 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 175570 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 175570 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 175570 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 175570 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 56403 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 56403 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 163236 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 163236 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 175552 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 175552 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 175552 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 175552 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 183731 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 183731 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 183731 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 158682 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 158682 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 13659 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 13659 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 13659 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 160526 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 160526 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 153828 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 153828 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 118817 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 118817 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 169539 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 169539 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 169539 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 169539 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 56305 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 56305 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 56309 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 56309 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 214966 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 214966 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 143822 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 143822 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 118816 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 118816 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 1061 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 1061 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 1061 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 3015 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 3015 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 3015 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 160418 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 160418 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 112000 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 112000 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 78740 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 78740 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 78740 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 78740 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 111991 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 111991 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 175418 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 175418 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 175418 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 175418 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 170550 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 170550 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 170550 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 170550 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 106099 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 106099 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 106104 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 106104 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 170008 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 170008 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 170008 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 170008 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 95215 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 95215 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 56401 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 56401 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 160254 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 160254 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 150155 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 150155 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 160435 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 160435 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 160920 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 160920 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 160140 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 160140 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 160670 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 160670 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 183647 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 183647 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 183647 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 142861 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 142861 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 106102 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 106102 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 148468 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 148468 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 215217 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 215217 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 143594 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 143594 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 160824 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 160824 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 148245 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 148245 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 206653 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 206653 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 1539 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 1539 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 1539 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 1539 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 3361 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 3361 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 3361 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 112571 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 112571 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 2614 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 2614 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 2614 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 154974 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 154974 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 2421 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 2421 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 2421 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 161292 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 161292 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 170252 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 170252 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 2417 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 2417 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 2417 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 2417 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 141584 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 141584 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 18062 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 18062 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 206603 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 206603 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 98739 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 98739 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 92176 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 92176 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 92176 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 92176 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 206837 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 206837 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 206570 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 206570 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 206570 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 106166 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 106166 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 73 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 73 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 73 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 101382 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 101382 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 2290 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 2290 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 2290 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 33 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 33 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 33 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 147944 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 147944 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 101737 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 101737 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 73958 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 73958 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 168750 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 168750 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 168750 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 168750 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 206866 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 206866 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 2469 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 2469 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 2469 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2144 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 2144 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 2144 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 2144 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 113 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 113 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 1105 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 1105 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 1105 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 555 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 555 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 555 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 555 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 989 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 989 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 989 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 1872 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 1872 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 1872 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 664 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 664 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 664 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 813 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 813 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 813 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 1073 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 1073 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 1073 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 1871 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 1871 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 1871 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 1009 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 1009 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 2143 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 2143 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 2143 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 2143 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 2143 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 2143 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 2143 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 2143 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 987 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 987 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 985 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 985 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 1300 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 1300 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 1300 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 3802 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 3802 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 3802 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 2145 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 2145 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 2145 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 42 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 42 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 42 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 42 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 3802 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 3802 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 3802 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 3015 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 3015 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 3015 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 122 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 122 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 122 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 122 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 122 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 122 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 122 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 122 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 122 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 122 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 122 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 122 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 1089 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 1089 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 1089 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 1110 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 1110 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 1110 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 1061 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 1061 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 1061 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 3361 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 3361 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 3361 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 2585 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 2585 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 2587 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 2587 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 3351 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 3351 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 3351 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 3351 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 3351 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 3351 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 2585 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 2585 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 2586 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 2586 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 2586 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 2586 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 3351 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 3351 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 3351 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 2587 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 2587 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 3353 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 3353 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 3224 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 3224 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 3224 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 107 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 107 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 107 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 107 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 107 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 107 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


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

 Reference
ligand		 Fold
selectivity		 # Tested
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 p-value
(-log)		 Activity
Type		 Activity
Relation		 Activity
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Type		 Assay
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 DOI
9794208 90050 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 90050 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 90062 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 90062 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 90062 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 90051 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 90051 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 109657 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 109657 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 57331 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 57331 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 199759 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 199759 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 201462 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 201462 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 201987 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 201987 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 115252 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 115252 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 73958 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 73958 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 111864 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 111864 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 184952 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 184952 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 111890 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 111890 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 137997 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 137997 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 111893 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 111893 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 66073 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 66073 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 123311 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 123311 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 111875 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 111875 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 156122 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 156122 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 82694 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 82694 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 82695 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 82695 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 4843 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 4843 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 137897 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 137897 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 184754 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 184754 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 186381 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 186381 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 181569 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 181569 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 111884 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 111884 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 111879 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 111879 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 147449 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 147449 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 140288 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 140288 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 111885 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 111885 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 63043 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 63043 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 90061 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 90061 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 183644 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 183644 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 183644 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 90055 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 90055 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 33 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 33 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 33 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 63490 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 63490 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 183637 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 183637 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 183637 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 111847 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 111847 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 111882 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 111882 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 140201 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 140201 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 1872 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 1872 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 1872 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 199737 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 199737 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 199829 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 199829 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 200046 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 200046 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 201862 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 201862 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 201935 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 201935 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 199897 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 199897 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 200097 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 200097 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 140319 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 140319 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 137943 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 137943 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 111861 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 111861 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 184467 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 184467 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 149679 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 149679 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 82688 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 82688 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 82696 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 82696 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 101400 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 101400 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 146182 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 146182 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 183683 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 183683 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 183683 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 2144 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 2144 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 2144 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 2144 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 111896 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 111896 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 185184 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 185184 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 42 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 42 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 42 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 42 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 4846 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 4846 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 109769 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 109769 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 146992 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 146992 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 66300 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 66300 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 185532 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 185532 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 2144 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 2144 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 2144 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 2144 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 2145 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 2145 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 2145 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 111866 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 111866 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 111886 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 111886 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 140209 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 140209 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 146154 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 146154 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 148556 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 148556 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 137965 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 137965 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 4851 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 4851 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 4851 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 4851 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 111856 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 111856 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 111858 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 111858 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 111872 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 111872 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 109537 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 109537 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 199823 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 199823 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 201365 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 201365 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 201615 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 201615 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 117346 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 117346 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 109223 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 109223 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 140223 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 140223 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 4825 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 4825 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 4902 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 4902 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 4951 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 4951 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 70554 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 70554 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 111874 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 111874 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 111880 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 111880 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 184022 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 184022 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 2144 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 2144 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 2144 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 2144 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 184948 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 184948 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 63469 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 63469 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 184022 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 184022 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 5036 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 5036 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 2145 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 2145 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 2145 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 150871 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 150871 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 143931 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 143931 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 989 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 989 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 989 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 82697 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 82697 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 989 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 989 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 989 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 122 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 122 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 122 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 111887 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 111887 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 111870 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 111870 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 109674 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 109674 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 156225 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 156225 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 108546 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 108546 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 57326 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 57326 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 137994 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 137994 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 66675 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 66675 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 111894 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 111894 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 138044 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 138044 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 64465 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 64465 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 138053 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 138053 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 111862 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 111862 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 138036 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 138036 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 184616 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 184616 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 65390 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 65390 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 555 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 555 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 555 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 555 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 199696 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 199696 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 200047 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 200047 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 200174 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 200174 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 201874 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 201874 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 199763 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 199763 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 143911 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 143911 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 182467 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 182467 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 82691 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 82691 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 82703 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 82703 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 107454 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 107454 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 82700 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 82700 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 111876 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 111876 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 33 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 33 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 33 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 2144 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 2144 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 2144 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 2144 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 166026 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 166026 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 111897 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 111897 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 2146 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 2146 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 2146 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 90057 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 90057 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 186384 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 186384 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 5122 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 5122 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 109760 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 109760 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 184349 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 184349 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 138081 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 138081 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 143621 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 143621 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 154216 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 154216 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 57332 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 57332 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 140284 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 140284 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 111849 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 111849 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 184579 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 184579 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 63786 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 63786 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 123603 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 123603 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 111867 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 111867 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 66338 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 66338 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 2145 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 2145 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 2145 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 5287 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 5287 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 115251 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 115251 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 111888 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 111888 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 146992 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 146992 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 111869 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 111869 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 181622 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 181622 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 1300 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 1300 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 1300 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 82701 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 82701 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 66925 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 66925 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 111855 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 111855 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 70076 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 70076 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 146085 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 146085 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 82685 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 82685 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 138081 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 138081 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 4802 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 4802 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 191788 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 191788 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 201363 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 201363 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 201873 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 201873 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 90059 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 90059 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 185529 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 185529 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 2144 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 2144 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 2144 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 2144 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 111852 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 111852 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 111877 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 111877 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 181602 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 181602 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 181603 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 181603 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 189537 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 189537 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 147287 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 147287 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 153753 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 153753 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 137950 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 137950 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 144580 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 144580 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 57333 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 57333 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 186200 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 186200 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 2144 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 2144 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 2144 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 2144 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 5882 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 5882 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 2145 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 2145 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 2145 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 66101 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 66101 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 122 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 122 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 122 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 57334 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 57334 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 130175 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 130175 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 184925 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 184925 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 185565 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 185565 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 126776 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 126776 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 183648 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 183648 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 183648 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 65860 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 65860 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 145755 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 145755 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 5394 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 5394 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 140227 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 140227 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 140308 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 140308 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 64182 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 64182 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 186211 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 186211 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 152069 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 152069 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 189639 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 189639 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 1340 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 1340 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 1340 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 57338 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 57338 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 181585 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 181585 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 66781 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 66781 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 185114 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 185114 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 137958 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 137958 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 4963 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 4963 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 57337 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 57337 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 138026 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 138026 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 200048 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 200048 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 201183 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 201183 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 201362 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 201362 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 4824 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 4824 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 101231 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 101231 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 64590 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 64590 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 140313 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 140313 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 111854 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 111854 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 67138 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 67138 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 111889 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 111889 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 3224 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 3224 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 3224 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 1340 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 1340 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 1340 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 57335 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 57335 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 206570 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 206570 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 206570 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 102201 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 102201 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 102201 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 206570 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 206570 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 206570 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 5027 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 5027 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 140272 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 140272 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 164465 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 164465 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 70554 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 70554 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 140195 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 140195 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 115265 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 115265 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 115265 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 115265 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 64694 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 64694 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 186029 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 186029 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 137887 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 137887 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 142795 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 142795 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 2290 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 2290 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 2290 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 66713 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 66713 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 664 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 664 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 664 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 664 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 664 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 664 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 164517 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 164517 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 184902 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 184902 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 2145 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 2145 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 2145 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 199675 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 199675 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 2145 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 2145 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 2145 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 111866 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 111866 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 144859 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 144859 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 204923 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 204923 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 204923 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 21785 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 21785 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 21785 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 21785 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 111853 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 111853 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 184242 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 184242 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 5700 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 5700 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 67029 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 67029 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 111873 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 111873 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 140199 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 140199 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 147669 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 147669 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 5355 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 5355 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 63891 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 63891 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 185444 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 185444 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 146992 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 146992 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 111850 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 111850 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 111860 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 111860 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 2145 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 2145 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 2145 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 138063 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 138063 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 111895 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 111895 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 90056 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 90056 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 82687 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 82687 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 185485 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 185485 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 86271 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 86271 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 137928 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 137928 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 185251 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 185251 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 86271 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 86271 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 123157 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 123157 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 57327 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 57327 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 57327 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 57327 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 111878 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 111878 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 185769 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 185769 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 199762 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 199762 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 64868 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 64868 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 33 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 33 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 33 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 199824 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 199824 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 199977 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 199977 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 199705 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 199705 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 185462 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 185462 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 149062 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 149062 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 111857 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 111857 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 181586 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 181586 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 185742 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 185742 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 131965 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 131965 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 111891 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 111891 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 142312 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 142312 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 140208 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 140208 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 183793 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 183793 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 183793 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 147314 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 147314 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 178365 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 178365 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 63476 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 63476 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 111871 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 111871 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 147404 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 147404 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 151543 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 151543 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 137945 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 137945 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 150759 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 150759 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 82686 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 82686 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 65590 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 65590 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 122336 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 122336 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 57336 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 57336 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 123238 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 123238 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 138081 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 138081 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 111863 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 111863 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 138081 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 138081 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 181900 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 181900 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 183706 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 183706 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 183706 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 111881 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 111881 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 108573 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 108573 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 123327 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 123327 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 138081 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 138081 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 185065 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 185065 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 199797 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 199797 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 2422 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 2422 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 2422 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 140227 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 140227 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 111865 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 111865 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 184243 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 184243 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 169140 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 169140 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 82684 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 82684 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 147427 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 147427 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 2144 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 2144 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 2144 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 2144 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 82689 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 82689 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 146992 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 146992 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 140308 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 140308 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 180420 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 180420 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 145276 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 145276 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 111859 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 111859 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 181588 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 181588 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 90053 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 90053 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 90052 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 90052 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 57328 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 57328 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 137902 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 137902 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 5011 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 5011 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 111892 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 111892 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 82699 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 82699 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 140308 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 140308 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 185130 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 185130 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 2290 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 2290 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 2290 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 66139 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 66139 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 65598 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 65598 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 2144 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 2144 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 2144 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 2144 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 33 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 33 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 33 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 146992 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 146992 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 190359 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 190359 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 185391 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 185391 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 4806 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 4806 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 63897 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 63897 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 1871 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 1871 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 1871 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 199758 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 199758 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 199854 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 199854 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 200134 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 200134 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 200135 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 200135 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 181621 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 181621 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 90054 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 90054 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 82690 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 82690 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 82692 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 82692 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 57329 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 57329 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 138023 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 138023 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 185873 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 185873 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 137948 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 137948 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 111883 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 111883 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 111848 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 111848 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 148735 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 148735 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 184890 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 184890 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 63268 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 63268 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 181256 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 181256 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 181543 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 181543 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 184388 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 184388 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 138074 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 138074 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 184441 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 184441 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 66700 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 66700 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 110066 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 110066 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 148772 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 148772 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 156461 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 156461 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 47471 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 47471 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 148600 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 148600 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 144991 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 144991 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 82693 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 82693 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 57330 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 57330 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 67050 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 67050 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 183619 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 183619 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 183619 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 125037 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 125037 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 67237 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 67237 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 183632 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 183632 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 183632 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 111868 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 111868 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 181568 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 181568 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 181566 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 181566 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 111851 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 111851 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 146992 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 146992 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 183733 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 183733 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 183733 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 82702 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 82702 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 142801 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 142801 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 144250 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 144250 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 146562 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 146562 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 146882 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 146882 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 147050 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 147050 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 148098 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 148098 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 148284 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 148284 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 148637 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 148637 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 149451 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 149451 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 150354 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 150354 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 153471 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 153471 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 160711 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 160711 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 177357 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 177357 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 56290 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 56290 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 56304 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 56304 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 56412 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 56412 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 56414 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 56414 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 143642 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 143642 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 146678 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 146678 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 153956 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 153956 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 204053 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 204053 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 151264 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 151264 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 152537 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 152537 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 144091 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 144091 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 149909 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 149909 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 151156 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 151156 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 152005 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 152005 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 160217 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 160217 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 160378 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 160378 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 96173 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 96173 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 83903 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 83903 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 83904 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 83904 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 3361 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 3361 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 3361 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 144424 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 144424 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 145731 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 145731 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 153328 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 153328 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 160825 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 160825 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 102631 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 102631 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 151870 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 151870 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 143136 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 143136 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 144576 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 144576 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 159993 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 159993 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 56415 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 56415 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 142765 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 142765 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 147050 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 147050 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 151868 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 151868 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 152005 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 152005 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 160161 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 160161 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 96172 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 96172 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 160365 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 160365 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 177733 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 177733 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 56410 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 56410 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 96308 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 96308 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 160365 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 160365 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 142864 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 142864 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 56406 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 56406 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 203870 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 203870 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 150419 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 150419 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 152288 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 152288 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 152369 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 152369 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 56294 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 56294 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 143027 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 143027 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 143402 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 143402 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 143576 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 143576 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 147567 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 147567 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 148679 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 148679 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 148896 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 148896 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 160795 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 160795 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 160811 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 160811 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 155282 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 155282 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 177542 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 177542 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 56288 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 56288 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 56417 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 56417 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 56418 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 56418 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 56421 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 56421 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 96120 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 96120 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 66852 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 66852 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 144548 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 144548 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 147520 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 147520 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 142751 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 142751 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 177164 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 177164 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 147060 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 147060 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 204063 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 204063 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 147634 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 147634 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 148138 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 148138 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 148239 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 148239 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 148782 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 148782 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 149590 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 149590 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 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 388 5 1 5 3.5 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3953157 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 388 5 1 5 3.5 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554909 160334 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 160334 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 160715 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 160715 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 56291 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 56291 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 56300 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 56300 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 95298 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 95298 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 160624 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 160624 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 177805 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 177805 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 150514 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 150514 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 150601 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 150601 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 151640 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 151640 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 154275 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 154275 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 149343 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 149343 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 2145 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 2145 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 2145 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 142994 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 142994 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 144804 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 144804 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 146383 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 146383 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 146774 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 146774 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 148487 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 148487 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 150724 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 150724 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 151141 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 151141 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 152407 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 152407 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 153495 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 153495 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 160402 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 160402 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 151427 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 151427 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 88704 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 88704 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 150574 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 150574 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 152712 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 152712 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 146774 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 146774 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 147383 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 147383 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 149916 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 149916 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 150724 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 150724 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 160660 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 160660 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 96308 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 96308 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 96308 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 96308 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 160170 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 160170 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 177727 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 177727 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 56416 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 56416 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 89182 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 89182 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 146341 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 146341 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 143149 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 143149 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 152895 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 152895 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 153434 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 153434 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 160865 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 160865 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 149343 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 149343 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 149919 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 149919 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 154168 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 154168 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 142951 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 142951 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 144792 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 144792 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 148248 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 148248 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 151423 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 151423 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 95864 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 95864 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 96264 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 96264 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 96267 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 96267 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 148218 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 148218 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 153375 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 153375 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 97695 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 97695 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 2400 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 2400 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 2400 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 152654 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 152654 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 160796 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 160796 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 143790 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 143790 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 148692 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 148692 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 89437 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 89437 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 97555 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 97555 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 56293 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 56293 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 56308 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 56308 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 145383 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 145383 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 145297 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 145297 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 153392 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 153392 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 144791 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 144791 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 149590 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 149590 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 152399 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 152399 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 160170 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 160170 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 96304 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 96304 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 177733 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 177733 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 177870 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 177870 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 149824 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 149824 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 143915 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 143915 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 159882 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 159882 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 3351 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 3351 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 3351 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 56298 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 56298 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 56299 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 56299 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 56425 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 56425 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 2417 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 2417 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 2417 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 2417 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 143755 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 143755 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 147556 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 147556 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 2529 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 2529 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 2529 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 155492 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 155492 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 155665 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 155665 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 56297 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 56297 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 110538 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 110538 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 2417 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 2417 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 2417 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 2417 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 204062 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 204062 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 146395 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 146395 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 169948 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 169948 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 142674 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 142674 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 143755 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 143755 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 144146 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 144146 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 146542 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 146542 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 147214 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 147214 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 147306 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 147306 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 149217 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 149217 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 150201 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 150201 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 151881 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 151881 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 152399 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 152399 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 160046 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 160046 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 152829 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 152829 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 96303 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 96303 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 95955 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 95955 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 145371 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 145371 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 153843 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 153843 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 143115 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 143115 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 155778 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 155778 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 90053 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 90053 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 66457 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 66457 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 149481 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 149481 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 66114 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 66114 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 142994 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 142994 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 143025 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 143025 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 152829 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 152829 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 153415 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 153415 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 155586 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 155586 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 56296 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 56296 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 2417 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 2417 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 2417 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 2417 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 144523 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 144523 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 150105 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 150105 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 153929 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 153929 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 177173 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 177173 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 142994 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 142994 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 143425 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 143425 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 152573 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 152573 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 152874 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 152874 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 153153 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 153153 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 168372 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 168372 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 154602 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 154602 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 143631 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 143631 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 147350 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 147350 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 147839 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 147839 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 143016 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 143016 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 146446 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 146446 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 149587 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 149587 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 149874 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 149874 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 150397 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 150397 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 151463 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 151463 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 96129 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 96129 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 178107 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 178107 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 143208 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 143208 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 149522 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 149522 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 102873 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 102873 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 160799 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 160799 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 88654 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 88654 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 89319 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 89319 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 160799 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 160799 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 160799 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 160799 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 56424 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 56424 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 160799 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 160799 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 159844 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 159844 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 88759 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 88759 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 149640 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 149640 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 154603 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 154603 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 203934 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 203934 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 149872 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 149872 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 150084 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 150084 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 150509 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 150509 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 153835 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 153835 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 95863 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 95863 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 177992 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 177992 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 160614 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 160614 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 143353 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 143353 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 56420 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 56420 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 148952 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 148952 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 142609 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 142609 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 150027 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 150027 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 150484 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 150484 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 89317 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 89317 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 88605 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 88605 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 151446 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 151446 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 95934 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 95934 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 56423 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 56423 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 67560 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 67560 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 88606 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 88606 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 3351 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 3351 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 3351 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 3351 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 3351 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 3351 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 148774 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 148774 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 159268 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 159268 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 145484 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 145484 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 146675 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 146675 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 149032 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 149032 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 90064 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 90064 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 88757 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 88757 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 154974 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 154974 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 152650 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 152650 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 146892 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 146892 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 150264 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 150264 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 152318 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 152318 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 153647 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 153647 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 153955 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 153955 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 158994 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 158994 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 203564 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 203564 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 89609 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 89609 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 142540 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 142540 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 148782 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 148782 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 153876 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 153876 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 152425 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 152425 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 142994 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 142994 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 147284 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 147284 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 155008 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 155008 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 155008 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 155008 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 90063 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 90063 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 155008 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 155008 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 155008 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 155008 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 155008 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 155008 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 100152 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 100152 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 155008 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 155008 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 143709 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 143709 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 56404 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 56404 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 88751 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 88751 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 142534 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 142534 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 149342 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 149342 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 97517 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 97517 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 160046 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 160046 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 177573 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 177573 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 89915 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 89915 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 177266 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 177266 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 152861 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 152861 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 146409 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 146409 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 89050 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 89050 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 95213 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 95213 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 146197 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 146197 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 152883 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 152883 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 96050 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 96050 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 145224 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 145224 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 144666 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 144666 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 150955 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 150955 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 95915 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 95915 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 56405 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 56405 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 147862 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 147862 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 143327 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 143327 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 144303 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 144303 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 154273 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 154273 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 149398 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 149398 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 96263 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 96263 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 56305 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 56305 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 56307 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 56307 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 56407 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 56407 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 56408 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 56408 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 56413 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 56413 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 95955 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 95955 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 144569 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 144569 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 89051 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 89051 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 56419 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 56419 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 66937 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 66937 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 167411 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 167411 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 147944 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 147944 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 177171 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 177171 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 145247 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 145247 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 177714 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 177714 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 151049 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 151049 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 144225 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 144225 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 143014 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 143014 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 145415 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 145415 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 149660 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 149660 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 152652 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 152652 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 96174 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 96174 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 142831 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 142831 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 96680 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 96680 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 153720 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 153720 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 89181 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 89181 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 142962 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 142962 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 142962 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 142950 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 142950 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 148315 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 148315 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 150485 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 150485 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 152242 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 152242 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 159962 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 159962 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 155297 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 155297 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 167568 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 167568 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 144921 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 144921 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 149716 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 149716 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 153306 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 153306 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 203977 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 203977 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 153098 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 153098 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 66753 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 66753 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 150951 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 150951 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 150959 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 150959 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 153797 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 153797 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 147952 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 147952 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 150959 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 150959 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 146595 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 146595 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 149451 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 149451 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 151744 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 151744 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 152515 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 152515 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 56287 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 56287 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 56401 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 56401 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 83909 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 83909 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 150397 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 150397 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 3361 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 3361 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 3361 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 148682 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 148682 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 159887 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 159887 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 148158 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 148158 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 153443 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 153443 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 144111 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 144111 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 160168 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 160168 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 151263 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 151263 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 143690 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 143690 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 145204 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 145204 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 146451 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 146451 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 147046 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 147046 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 147570 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 147570 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 152249 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 152249 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 148714 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 148714 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 144076 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 144076 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 150385 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 150385 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 102260 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 102260 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 153326 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 153326 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 150369 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 150369 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 150385 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 150385 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 150959 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 150959 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 56422 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 56422 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 148928 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 148928 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 150601 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 150601 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 152005 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 152005 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 152800 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 152800 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 153981 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 153981 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 95384 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 95384 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 56289 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 56289 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 56295 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 56295 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 56309 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 56309 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 155898 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 155898 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 89049 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 89049 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 89318 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 89318 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 96133 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 96133 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 146093 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 146093 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 146093 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 146093 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 143972 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 143972 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 147504 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 147504 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 146908 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 146908 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 150567 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 150567 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 153987 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 153987 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 95051 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 95051 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 7527 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 7527 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 149058 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 149058 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 149058 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 149058 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 149058 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 149058 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 147476 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 147476 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 88604 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 88604 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 152111 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 152111 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 154185 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 154185 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 56411 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 56411 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 149487 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 149487 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 150939 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 150939 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 142528 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 142528 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 148697 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 148697 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 2144 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 2144 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 2144 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 2144 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 89916 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 89916 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 152895 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 152895 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 177424 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 177424 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 145181 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 145181 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 152513 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 152513 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 1539 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 1539 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 1539 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 1539 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 146852 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 146852 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 148458 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 148458 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 150044 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 150044 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 150961 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 150961 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 151394 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 151394 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 152800 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 152800 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 157939 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 157939 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 168835 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 168835 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 56303 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 56303 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 83908 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 83908 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 167697 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 167697 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 142344 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 142344 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 150224 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 150224 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 168806 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 168806 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 167778 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 167778 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 144048 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 144048 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 144642 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 144642 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 95677 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 95677 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 150337 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 150337 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 160602 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 160602 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 204041 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 204041 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 143339 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 143339 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 152296 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 152296 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 159906 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 159906 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 161770 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 161770 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 2469 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 2469 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 2469 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 150034 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 150034 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 162545 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 162545 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 142962 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 142962 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 142962 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 144250 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 144250 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 145223 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 145223 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 148331 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 148331 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 148637 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 148637 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 151099 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 151099 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 152521 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 152521 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 159867 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 159867 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 160101 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 160101 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 160284 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 160284 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 56301 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 56301 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 56306 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 56306 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 56403 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 56403 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 56409 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 56409 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 90052 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 90052 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 142690 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 142690 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 142466 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 142466 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 88655 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 88655 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 150234 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 150234 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 150705 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 150705 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 145225 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 145225 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 148338 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 148338 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 154601 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 154601 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 148181 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 148181 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 147207 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 147207 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 150377 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 150377 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 147341 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 147341 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 143984 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 143984 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 160935 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 160935 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 56292 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 56292 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 88758 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 88758 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 146628 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 146628 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 265 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 265 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 265 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 265 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 151315 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 151315 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 142690 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 142690 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 144091 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 144091 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 148284 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 148284 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 150439 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 150439 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 153977 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 153977 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 154198 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 154198 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 160202 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 160202 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 96647 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 96647 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 157736 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 157736 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 95215 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 95215 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 142690 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 142690 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 56284 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 56284 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 157736 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 157736 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 83907 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 83907 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 145974 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 145974 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 145146 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 145146 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 177220 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 177220 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 96276 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 96276 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 89183 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 89183 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 146544 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 146544 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 142708 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 142708 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 148975 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 148975 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 154744 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 154744 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 145563 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 145563 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 95087 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 95087 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 166615 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 166615 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 148635 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 148635 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 3015 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 3015 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 3015 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 157111 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 157111 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 158140 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 158140 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 157035 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 157035 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 156122 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 156122 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 157166 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 157166 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 157260 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 157260 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 157189 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 157189 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 157193 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 157193 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 3802 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 3802 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 3802 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 158390 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 158390 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 156461 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 156461 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 157093 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 157093 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 158338 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 158338 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 157153 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 157153 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 156894 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 156894 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 157174 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 157174 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 157629 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 157629 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 156364 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 156364 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 158618 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 158618 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 664 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 664 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 664 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 158744 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 158744 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 156463 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 156463 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 158231 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 158231 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 157609 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 157609 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 158525 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 158525 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 156050 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 156050 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 158045 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 158045 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 158356 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 158356 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 158290 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 158290 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 157338 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 157338 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 159679 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 159679 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 158749 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 158749 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 156472 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 156472 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 156225 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 156225 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 158741 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 158741 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 157178 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 157178 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 2143 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 2143 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 2143 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 2143 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 157225 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 157225 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 155863 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 155863 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 555 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 555 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 555 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 555 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 159461 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 159461 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 159392 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 159392 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 156908 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 156908 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 157274 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 157274 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 159658 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 159658 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 156122 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 156122 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 142312 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 142312 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 126769 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 126769 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 65447 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 65447 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 127153 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 127153 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 159461 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 159461 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 66323 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 66323 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 96604 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 96604 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 157338 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 157338 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 157153 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 157153 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 158390 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 158390 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 158338 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 158338 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 183618 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 183618 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 183618 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 1061 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 1061 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 1061 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 100429 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 100429 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 161318 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 161318 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 115252 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 115252 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 124034 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 124034 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 157629 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 157629 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 156463 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 156463 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 157174 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 157174 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 123097 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 123097 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 1340 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 1340 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 1340 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 123409 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 123409 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 171852 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 171852 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 156588 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 156588 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 67342 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 67342 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 180213 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 180213 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 123397 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 123397 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 90061 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 90061 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 1539 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 1539 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 1539 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 1539 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 123406 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 123406 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 158921 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 158921 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 2421 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 2421 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 2421 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 2421 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 2421 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 2421 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 183679 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 183679 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 183679 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 126294 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 126294 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 156364 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 156364 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 123402 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 123402 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 123396 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 123396 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 137600 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 137600 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 2145 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 2145 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 2145 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 66995 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 66995 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 146992 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 146992 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 141965 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 141965 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 159284 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 159284 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 155894 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 155894 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 2422 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 2422 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 2422 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 171852 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 171852 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 90052 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 90052 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 122351 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 122351 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 123404 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 123404 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 173840 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 173840 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 158045 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 158045 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 2144 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 2144 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 2144 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 2144 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 155947 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 155947 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 66356 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 66356 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 65316 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 65316 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 158525 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 158525 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 159679 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 159679 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 2529 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 2529 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 2529 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 157035 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 157035 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 66937 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 66937 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 2529 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 2529 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 2529 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 66457 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 66457 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 157609 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 157609 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 168372 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 168372 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 124356 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 124356 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 127085 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 127085 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 149627 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 149627 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 66687 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 66687 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 183686 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 183686 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 183686 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 2421 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 2421 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 2421 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 100268 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 100268 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 161897 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 161897 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 163171 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 163171 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 183691 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 183691 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 183691 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 157166 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 157166 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 158513 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 158513 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 158422 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 158422 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 114499 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 114499 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 158290 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 158290 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 115251 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 115251 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 31341 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 31341 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 1539 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 1539 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 1539 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 1539 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 90053 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 90053 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 173840 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 173840 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 183675 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 183675 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 183675 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 100324 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 100324 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 157189 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 157189 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 124318 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 124318 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 2143 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 2143 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 2143 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 2143 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 123401 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 123401 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 183622 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 183622 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 183622 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 123407 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 123407 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 7527 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 7527 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 183719 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 183719 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 183719 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 158961 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 158961 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 157093 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 157093 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 64607 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 64607 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 66676 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 66676 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 2417 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 2417 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 2417 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 2417 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 158744 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 158744 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 67560 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 67560 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 67391 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 67391 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 2528 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 2528 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 2528 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 122026 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 122026 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 156908 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 156908 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 158140 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 158140 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 122335 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 122335 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 35817 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 35817 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 126551 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 126551 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 123831 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 123831 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 124352 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 124352 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 169474 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 169474 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 156472 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 156472 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 183728 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 183728 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 183728 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 168480 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 168480 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 158568 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 158568 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 159392 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 159392 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 66753 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 66753 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 163373 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 163373 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 156124 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 156124 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 123408 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 123408 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 2421 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 2421 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 2421 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 555 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 555 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 555 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 555 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 158618 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 158618 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 66114 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 66114 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 159236 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 159236 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 123803 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 123803 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 125036 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 125036 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 176000 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 176000 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 166277 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 166277 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 67127 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 67127 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 2417 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 2417 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 2417 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 2417 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 66827 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 66827 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 83247 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 83247 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 122275 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 122275 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 67338 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 67338 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 67466 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 67466 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 123670 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 123670 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 206508 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 206508 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 206508 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 206508 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 100321 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 100321 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 100494 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 100494 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 169095 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 169095 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 2422 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 2422 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 2422 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 157655 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 157655 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 90060 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 90060 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 183731 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 183731 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 183731 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 90057 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 90057 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 114800 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 114800 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 156225 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 156225 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 168340 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 168340 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 183687 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 183687 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 183687 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 156461 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 156461 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 183653 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 183653 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 183653 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 124739 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 124739 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 67458 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 67458 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 124445 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 124445 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 67544 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 67544 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 176000 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 176000 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 65534 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 65534 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 123875 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 123875 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 83247 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 83247 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 157178 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 157178 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 156787 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 156787 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 156545 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 156545 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 214430 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 214430 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 156641 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 156641 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 157111 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 157111 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 157193 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 157193 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 173840 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 173840 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 158356 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 158356 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 66837 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 66837 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 155863 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 155863 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 664 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 664 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 664 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 123403 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 123403 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 1089 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 1089 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 1089 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 156050 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 156050 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 157225 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 157225 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 173840 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 173840 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 158682 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 158682 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 215217 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 215217 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 158741 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 158741 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 126776 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 126776 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 56348 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 56348 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 123400 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 123400 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 206508 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 206508 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 123102 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 123102 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 66208 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 66208 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 159658 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 159658 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 66852 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 66852 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 67320 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 67320 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 156894 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 156894 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 152255 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 152255 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 2146 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 2146 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 2146 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 2146 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 2146 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 2146 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 127508 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 127508 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 158749 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 158749 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 100439 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 100439 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 183670 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 183670 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 183670 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 144789 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 144789 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 3802 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 3802 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 3802 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 183647 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 183647 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 183647 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 123405 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 123405 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 124394 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 124394 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 157274 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 157274 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 66659 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 66659 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 183721 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 183721 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 183721 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 158231 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 158231 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 1110 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 1110 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 1110 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 100223 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 100223 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 206508 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 206508 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 123398 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 123398 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 1539 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 1539 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 1539 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 1539 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 110538 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 110538 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 156881 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 156881 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 90059 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 90059 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 183640 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 183640 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 183640 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 157260 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 157260 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 66222 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 66222 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 66853 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 66853 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 123399 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 123399 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 69375 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 69375 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 2146 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 2146 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 2146 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 2143 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 2143 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 2143 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 2143 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 2143 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 2143 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 2143 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 2143 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 42 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 42 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 42 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 42 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 1539 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 1539 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 1539 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 1539 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 2417 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 2417 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 2417 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 2417 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 216333 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 1970 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 1970 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 1970 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 1970 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 1970 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 1970 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 1970 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 1970 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 1970 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 1970 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 1970 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 1970 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2514 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 2514 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 2514 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 2514 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 2514 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 2862 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 2862 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 2862 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 3263 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 3263 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 3263 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 3263 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 3263 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 3263 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 3263 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 3263 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 3263 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 3263 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 3263 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 3263 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 3464 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 3464 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 3464 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 3464 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 27112 30 Functional -38 42 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 27112 30 Functional -38 42 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 99865 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 99865 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 101737 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 101737 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 112047 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 112047 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 112047 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 112047 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 112047 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 112047 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 133521 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 133521 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 161322 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 161322 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 161322 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 161322 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 161322 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 161322 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 167791 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 167791 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 170252 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 170252 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 170252 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 170252 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 202274 22 Functional -239 43 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 CC(N)C(O)c1ccccc1 None
4786 202274 22 Functional -239 43 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 CC(N)C(O)c1ccccc1 None
CHEMBL61006 202274 22 Functional -239 43 Rat 5.0 pKi = 5 Binding
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 CC(N)C(O)c1ccccc1 None
139054390 204923 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 204923 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 204923 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 204923 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 204923 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 204923 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 204923 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 204923 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 204923 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 206367 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 206367 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 206367 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 206367 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 206367 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 215953 0 Functional -141253 58 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 216009 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 216172 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 216172 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 216179 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 216179 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 216316 0 Functional -1 39 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 216317 0 Functional -1 38 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 216325 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 216326 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 216336 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 216345 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 216345 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 216362 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 216362 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 216363 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 216363 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 216364 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 216364 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 216365 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 216365 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 216400 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 216409 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 216409 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 216490 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 216491 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 321 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 321 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 321 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 216172 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 216172 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 216334 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 216399 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 216334 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 216335 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 216332 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 216332 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 216332 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 2146 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 2146 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 2146 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 1061 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 1061 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 1061 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 1110 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 1110 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 1110 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 1089 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 1089 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 1089 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 2422 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 2422 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 2422 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 3351 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 3351 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 3351 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 2145 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 2145 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 2145 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 3351 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 3351 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 3351 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 3358 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 3358 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 3353 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 3353 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 2475 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 2475 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 2475 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 2475 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 2475 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 33 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 33 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 33 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 1538 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 1538 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 1538 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 1538 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 1538 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 1538 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 2475 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 2475 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 2475 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 2475 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 2475 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 2081 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 2081 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 2081 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 73 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 73 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 73 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 33 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 33 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 33 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 33 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 33 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 33 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 365 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 365 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 365 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2315 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 2290 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 2290 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 2290 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 1340 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 1340 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 1340 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 2290 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 2290 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 2290 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 2290 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 2290 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 2290 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 1539 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 1539 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 1539 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 1539 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 1340 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 1340 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 1340 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 1340 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 1340 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 1340 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 1539 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 2421 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 2421 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 2421 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 2417 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 2417 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 2417 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 2417 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 2417 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 2417 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 2417 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 2417 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 2417 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 2417 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 2417 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 2417 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 2529 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 2529 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 2529 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 2529 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 2529 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 2529 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 2528 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 2528 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 2528 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