메뉴 건너뛰기




Volumn 28, Issue 8, 2007, Pages 407-415

Collateral efficacy in drug discovery: taking advantage of the good (allosteric) nature of 7TM receptors

Author keywords

[No Author keywords available]

Indexed keywords

BETA ARRESTIN; BRIMONIDINE; CATECHOLAMINE; G PROTEIN COUPLED RECEPTOR; IMIDAZOLINE;

EID: 34447624153     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2007.06.009     Document Type: Review
Times cited : (192)

References (73)
  • 1
    • 27844519281 scopus 로고    scopus 로고
    • New concepts in drug discovery: collateral efficacy and permissive antagonism
    • Kenakin T. New concepts in drug discovery: collateral efficacy and permissive antagonism. Nat. Rev. Drug Discov. 4 (2005) 919-927
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 919-927
    • Kenakin, T.1
  • 2
    • 0010673662 scopus 로고    scopus 로고
    • A modification of receptor theory. 1956
    • Stephenson R.P. A modification of receptor theory. 1956. Br. J. Pharmacol. 11 (1997) 379-393
    • (1997) Br. J. Pharmacol. , vol.11 , pp. 379-393
    • Stephenson, R.P.1
  • 3
    • 0029054965 scopus 로고
    • Agonist-receptor efficacy II: agonist-trafficking of receptor signals
    • Kenakin T. Agonist-receptor efficacy II: agonist-trafficking of receptor signals. Trends Pharmacol. Sci. 16 (1995) 232-238
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 232-238
    • Kenakin, T.1
  • 4
    • 0026454221 scopus 로고
    • Comparative effects of receptor inactivation, 17 β-estradiol and pertussis toxin on dopaminergic inhibition of prolactin secretion in vitro
    • Meller E., et al. Comparative effects of receptor inactivation, 17 β-estradiol and pertussis toxin on dopaminergic inhibition of prolactin secretion in vitro. J. Pharmacol. Exp. Ther. 263 (1992) 462-469
    • (1992) J. Pharmacol. Exp. Ther. , vol.263 , pp. 462-469
    • Meller, E.1
  • 5
    • 0027240588 scopus 로고
    • Differential signal transduction by five splice variants of the PACAP receptor
    • Spengler D., et al. Differential signal transduction by five splice variants of the PACAP receptor. Nature 365 (1993) 170-175
    • (1993) Nature , vol.365 , pp. 170-175
    • Spengler, D.1
  • 6
    • 0033151286 scopus 로고    scopus 로고
    • Interactions of the novel antipsychotic aripiprazole (OPC-14597) with dopamine and serotonin receptor subtypes
    • Lawler C.P., et al. Interactions of the novel antipsychotic aripiprazole (OPC-14597) with dopamine and serotonin receptor subtypes. Neuropsychopharmacology 20 (1999) 612-627
    • (1999) Neuropsychopharmacology , vol.20 , pp. 612-627
    • Lawler, C.P.1
  • 7
    • 0029664618 scopus 로고    scopus 로고
    • 1 agonist containing a rigid β phenyldopamine pharmacophore
    • 1 agonist containing a rigid β phenyldopamine pharmacophore. J. Med. Chem. 39 (1996) 549-555
    • (1996) J. Med. Chem. , vol.39 , pp. 549-555
    • Ghosh, D.1
  • 8
    • 0043235844 scopus 로고    scopus 로고
    • Ligand-selective receptor conformations revisited: the promise and the problem
    • Kenakin T. Ligand-selective receptor conformations revisited: the promise and the problem. Trends Pharmacol. Sci. 24 (2003) 346-354
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 346-354
    • Kenakin, T.1
  • 9
    • 33845903110 scopus 로고    scopus 로고
    • Functional selectivity and classical concepts of quantitative pharmacology
    • Urban J.D., et al. Functional selectivity and classical concepts of quantitative pharmacology. J. Pharmacol. Exp. Ther. 320 (2006) 1-13
    • (2006) J. Pharmacol. Exp. Ther. , vol.320 , pp. 1-13
    • Urban, J.D.1
  • 10
    • 0035070287 scopus 로고    scopus 로고
    • 2A-adrenoceptor responses in HEL 92.1.7 cells
    • 2A-adrenoceptor responses in HEL 92.1.7 cells. Br. J. Pharmacol. 132 (2001) 1477-1484
    • (2001) Br. J. Pharmacol. , vol.132 , pp. 1477-1484
    • Kukkonen, J.P.1
  • 11
    • 0033663775 scopus 로고    scopus 로고
    • The use of stimulus-biased assay systems to detect agonist-specific receptor active states: implications for the trafficking of receptor stimulus by agonists
    • Watson C., et al. The use of stimulus-biased assay systems to detect agonist-specific receptor active states: implications for the trafficking of receptor stimulus by agonists. Mol. Pharmacol. 58 (2000) 1230-1238
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1230-1238
    • Watson, C.1
  • 13
    • 0035851139 scopus 로고    scopus 로고
    • 5]enkephalin
    • 5]enkephalin. J. Biol. Chem. 276 (2001) 37779-37786
    • (2001) J. Biol. Chem. , vol.276 , pp. 37779-37786
    • Liu, J.G.1
  • 14
    • 0032839908 scopus 로고    scopus 로고
    • 2+ current in mouse ventricular myocytes
    • 2+ current in mouse ventricular myocytes. Mol. Pharmacol. 56 (1999) 485-493
    • (1999) Mol. Pharmacol. , vol.56 , pp. 485-493
    • Zhou, Y.Y.1
  • 15
    • 0029162109 scopus 로고
    • Pharmacological proteus
    • Kenakin T. Pharmacological proteus. Trends Pharmacol. Sci. 16 (1995) 256-258
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 256-258
    • Kenakin, T.1
  • 16
    • 0030840923 scopus 로고    scopus 로고
    • Protean agonists: keys to receptor active state?
    • Kenakin T. Protean agonists: keys to receptor active state?. Ann. N. Y. Acad. Sci. 812 (1997) 116-125
    • (1997) Ann. N. Y. Acad. Sci. , vol.812 , pp. 116-125
    • Kenakin, T.1
  • 17
    • 8144222927 scopus 로고    scopus 로고
    • Receptor activity-independent recruitment of β-arrestin reveals specific signaling modes
    • Terrillon S., and Bouvier M. Receptor activity-independent recruitment of β-arrestin reveals specific signaling modes. EMBO J. 23 (2004) 3950-3961
    • (2004) EMBO J. , vol.23 , pp. 3950-3961
    • Terrillon, S.1    Bouvier, M.2
  • 18
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by β-arrestins
    • Lefkowitz R.J., and Shenoy S.K. Transduction of receptor signals by β-arrestins. Science 308 (2005) 512-517
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 19
    • 25844477611 scopus 로고    scopus 로고
    • Composition and function of G protein-coupled receptor signalsomes controlling mitogen-activated protein kinase activity
    • Luttrell L.M. Composition and function of G protein-coupled receptor signalsomes controlling mitogen-activated protein kinase activity. J. Mol. Neurosci. 26 (2005) 253-263
    • (2005) J. Mol. Neurosci. , vol.26 , pp. 253-263
    • Luttrell, L.M.1
  • 20
    • 0141703263 scopus 로고    scopus 로고
    • Independent β-arrestin 2 and G-protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2
    • Wei H., et al. Independent β-arrestin 2 and G-protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 10782-10787
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10782-10787
    • Wei, H.1
  • 21
    • 0141593597 scopus 로고    scopus 로고
    • β-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G-protein-coupled receptors
    • Azzi M., et al. β-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G-protein-coupled receptors. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 11406-11411
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 11406-11411
    • Azzi, M.1
  • 22
    • 33744957160 scopus 로고    scopus 로고
    • Distinct β-arrestin- and G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation
    • Gesty-Palmer D., et al. Distinct β-arrestin- and G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation. J. Biol. Chem. 281 (2006) 10856-10864
    • (2006) J. Biol. Chem. , vol.281 , pp. 10856-10864
    • Gesty-Palmer, D.1
  • 23
    • 0345735773 scopus 로고    scopus 로고
    • 2-adrenoceptor provide evidence for agonist-directed signaling
    • 2-adrenoceptor provide evidence for agonist-directed signaling. Mol. Pharmacol. 64 (2003) 1357-1369
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1357-1369
    • Baker, J.G.1
  • 24
    • 2542423686 scopus 로고    scopus 로고
    • Differential desensitization, receptor phosphorylation, β-arrestin recruitment, and ERK1/2 activation by two endogenous ligands for the CC chemokine receptor 7
    • Kohout T.A. Differential desensitization, receptor phosphorylation, β-arrestin recruitment, and ERK1/2 activation by two endogenous ligands for the CC chemokine receptor 7. J. Biol. Chem. 279 (2004) 23214-23222
    • (2004) J. Biol. Chem. , vol.279 , pp. 23214-23222
    • Kohout, T.A.1
  • 25
    • 33746265800 scopus 로고    scopus 로고
    • Agonist-selective mechanisms of μ-opioid receptor desensitization in human embryonic kidney 293 cells
    • Johnson E.A., et al. Agonist-selective mechanisms of μ-opioid receptor desensitization in human embryonic kidney 293 cells. Mol. Pharmacol. 70 (2006) 676-685
    • (2006) Mol. Pharmacol. , vol.70 , pp. 676-685
    • Johnson, E.A.1
  • 26
    • 33846456218 scopus 로고    scopus 로고
    • An opioid agonist that does not induce μ-opioid receptor-arrestin interactions or receptor internalization
    • Groer C.E., et al. An opioid agonist that does not induce μ-opioid receptor-arrestin interactions or receptor internalization. Mol. Pharmacol. 71 (2007) 549-557
    • (2007) Mol. Pharmacol. , vol.71 , pp. 549-557
    • Groer, C.E.1
  • 27
    • 0035891883 scopus 로고    scopus 로고
    • 2A receptors by agonists and antagonists
    • 2A receptors by agonists and antagonists. Brain Res. Bull. 56 (2001) 441-451
    • (2001) Brain Res. Bull. , vol.56 , pp. 441-451
    • Gray, J.A.1    Roth, B.L.2
  • 28
    • 0030993594 scopus 로고    scopus 로고
    • Antagonist-stimulated internalization of the G protein-coupled cholecystokinin receptor
    • Roettger B.F., et al. Antagonist-stimulated internalization of the G protein-coupled cholecystokinin receptor. Mol. Pharmacol. 51 (1997) 357-362
    • (1997) Mol. Pharmacol. , vol.51 , pp. 357-362
    • Roettger, B.F.1
  • 29
    • 0242384770 scopus 로고    scopus 로고
    • Activation-independent parathyroid hormone receptor internalization is regulated by NHERF1 (EPB50)
    • Sneddon W.B., et al. Activation-independent parathyroid hormone receptor internalization is regulated by NHERF1 (EPB50). J. Biol. Chem. 278 (2003) 43787-43796
    • (2003) J. Biol. Chem. , vol.278 , pp. 43787-43796
    • Sneddon, W.B.1
  • 30
    • 0032907534 scopus 로고    scopus 로고
    • Clozapine and other 5-hydroxytryptamine-2A receptor antagonists alter the subcellular distribution of 5-hydroxytryptamine-2A receptors in vitro and in vivo
    • Willins D.L., et al. Clozapine and other 5-hydroxytryptamine-2A receptor antagonists alter the subcellular distribution of 5-hydroxytryptamine-2A receptors in vitro and in vivo. Neuroscience 91 (1999) 599-606
    • (1999) Neuroscience , vol.91 , pp. 599-606
    • Willins, D.L.1
  • 31
    • 0035896585 scopus 로고    scopus 로고
    • 2A receptors during endocytosis
    • 2A receptors during endocytosis. J. Biol. Chem. 276 (2001) 8269-8277
    • (2001) J. Biol. Chem. , vol.276 , pp. 8269-8277
    • Bhatnagar, A.1
  • 32
    • 0030745286 scopus 로고    scopus 로고
    • HIV coreceptor downregulation as antiviral principle: SDF-1α-dependent internalization of the chemokine receptor CXCR4 contributes to inhibition of HIV replication
    • Amara A., et al. HIV coreceptor downregulation as antiviral principle: SDF-1α-dependent internalization of the chemokine receptor CXCR4 contributes to inhibition of HIV replication. J. Exp. Med. 186 (1997) 139-146
    • (1997) J. Exp. Med. , vol.186 , pp. 139-146
    • Amara, A.1
  • 33
    • 33745851881 scopus 로고    scopus 로고
    • Huamn β-defensin3- a novel antagonist of the HIV-1 coreceptor CXCR4
    • Feng Z., et al. Huamn β-defensin3- a novel antagonist of the HIV-1 coreceptor CXCR4. J. Immunol. 177 (2006) 782-786
    • (2006) J. Immunol. , vol.177 , pp. 782-786
    • Feng, Z.1
  • 34
    • 15744377605 scopus 로고    scopus 로고
    • Distinct conformations of the corticotrophin releasing factor type 1 receptor adopted following agonist and antagonist binding are differentially regulated
    • Perry S.J., et al. Distinct conformations of the corticotrophin releasing factor type 1 receptor adopted following agonist and antagonist binding are differentially regulated. J. Biol. Chem. 280 (2005) 11560-11568
    • (2005) J. Biol. Chem. , vol.280 , pp. 11560-11568
    • Perry, S.J.1
  • 35
    • 0037664644 scopus 로고    scopus 로고
    • Agonist- and antagonist-induced sequestration/internalization of neuropeptide YY1 receptors in HEK293 cells
    • Pheng L.H., et al. Agonist- and antagonist-induced sequestration/internalization of neuropeptide YY1 receptors in HEK293 cells. Br. J. Pharmacol. 139 (2003) 695-704
    • (2003) Br. J. Pharmacol. , vol.139 , pp. 695-704
    • Pheng, L.H.1
  • 36
    • 0036178934 scopus 로고    scopus 로고
    • Multiple active states and oligermization of CCR5 revealed by functional properties of monoclonal antibodies
    • Blanpain C., et al. Multiple active states and oligermization of CCR5 revealed by functional properties of monoclonal antibodies. Mol. Biol. Cell 13 (2002) 723-737
    • (2002) Mol. Biol. Cell , vol.13 , pp. 723-737
    • Blanpain, C.1
  • 37
    • 33745077706 scopus 로고    scopus 로고
    • Long-lasting CCR5 internalization by antibodies in a subset of long-term nonprogressors: a possible protective effect against disease progression
    • Pastori C., et al. Long-lasting CCR5 internalization by antibodies in a subset of long-term nonprogressors: a possible protective effect against disease progression. Blood 107 (2006) 4825-4833
    • (2006) Blood , vol.107 , pp. 4825-4833
    • Pastori, C.1
  • 38
    • 33751162165 scopus 로고    scopus 로고
    • 2 adrenergic receptor ligands toward adenylyl cyclase and mitogen-activated protein kinase reveal the pluridimensionality of efficacy
    • 2 adrenergic receptor ligands toward adenylyl cyclase and mitogen-activated protein kinase reveal the pluridimensionality of efficacy. Mol. Pharmacol. 70 (2006) 1575-1584
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1575-1584
    • Galandrin, S.1    Bouvier, M.2
  • 39
    • 20344375461 scopus 로고    scopus 로고
    • Regulation of receptor-coupling to (multiple) G proteins. A challenge for basic research and drug discovery
    • Kukkonen J.P. Regulation of receptor-coupling to (multiple) G proteins. A challenge for basic research and drug discovery. Receptors Channels 10 (2004) 167-183
    • (2004) Receptors Channels , vol.10 , pp. 167-183
    • Kukkonen, J.P.1
  • 40
    • 0038540318 scopus 로고    scopus 로고
    • Biochemical and pharmacological control of the multiplicity of coupling at G-protein receptors
    • Hermans E. Biochemical and pharmacological control of the multiplicity of coupling at G-protein receptors. Pharmacol. Ther. 99 (2003) 25-44
    • (2003) Pharmacol. Ther. , vol.99 , pp. 25-44
    • Hermans, E.1
  • 41
    • 22944487986 scopus 로고    scopus 로고
    • Multiple signaling states of G-protein coupled receptors
    • Perez D.M., and Karnick S.S. Multiple signaling states of G-protein coupled receptors. Pharmacol. Rev. 57 (2005) 147-161
    • (2005) Pharmacol. Rev. , vol.57 , pp. 147-161
    • Perez, D.M.1    Karnick, S.S.2
  • 42
    • 0032544060 scopus 로고    scopus 로고
    • The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble
    • Hilser V.J., et al. The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 9903-9908
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9903-9908
    • Hilser, V.J.1
  • 43
    • 0027361710 scopus 로고
    • Is the slow-exchange core the protein folding core?
    • Woodward C. Is the slow-exchange core the protein folding core?. Trends Biochem. Sci. 18 (1993) 359-360
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 359-360
    • Woodward, C.1
  • 44
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H., et al. The energy landscapes and motions of proteins. Science 254 (1991) 1598-1603
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1
  • 45
    • 0035423908 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: implications for vision and beyond
    • Okada T., and Palczewski K. Crystal structure of rhodopsin: implications for vision and beyond. Curr. Opin. Struct. Biol. 11 (2001) 420-426
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 420-426
    • Okada, T.1    Palczewski, K.2
  • 46
    • 0028856707 scopus 로고
    • 2-adrenergic receptor: evidence for ligand specific conformational changes
    • 2-adrenergic receptor: evidence for ligand specific conformational changes. J. Biol. Chem. 270 (1995) 28268-28275
    • (1995) J. Biol. Chem. , vol.270 , pp. 28268-28275
    • Gether, U.1
  • 47
    • 0035816704 scopus 로고    scopus 로고
    • 2-adrenergic receptor
    • 2-adrenergic receptor. J. Biol. Chem. 276 (2001) 24433-24436
    • (2001) J. Biol. Chem. , vol.276 , pp. 24433-24436
    • Ghanouni, P.1
  • 48
    • 0035860802 scopus 로고    scopus 로고
    • The neurokinin A receptor activates calcium and cAMP responses through distinct conformational states
    • Palanche T., et al. The neurokinin A receptor activates calcium and cAMP responses through distinct conformational states. J. Biol. Chem. 276 (2001) 34853-34861
    • (2001) J. Biol. Chem. , vol.276 , pp. 34853-34861
    • Palanche, T.1
  • 49
    • 0345791508 scopus 로고    scopus 로고
    • 2 adrenoceptor: kinetic evidence for intermediate conformational states
    • 2 adrenoceptor: kinetic evidence for intermediate conformational states. J. Biol. Chem. 279 (2004) 686-691
    • (2004) J. Biol. Chem. , vol.279 , pp. 686-691
    • Swaminath, G.1
  • 50
    • 0019790028 scopus 로고
    • Conformational changes and drug action
    • Burgen A.S.V. Conformational changes and drug action. Fed. Proc. 40 (1966) 2723-2728
    • (1966) Fed. Proc. , vol.40 , pp. 2723-2728
    • Burgen, A.S.V.1
  • 51
    • 34447636845 scopus 로고    scopus 로고
    • Collateral efficacy as a pharmacological problem applied to new drug discovery
    • Kenakin T.P. Collateral efficacy as a pharmacological problem applied to new drug discovery. Expert. Opin. Drug Disc. 1 (2006) 635-652
    • (2006) Expert. Opin. Drug Disc. , vol.1 , pp. 635-652
    • Kenakin, T.P.1
  • 52
    • 0036177114 scopus 로고    scopus 로고
    • Efficacy at G protein coupled receptors
    • Kenakin T. Efficacy at G protein coupled receptors. Annu. Rev. Pharmacol. Toxicol. 42 (2002) 349-379
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 349-379
    • Kenakin, T.1
  • 53
    • 0024250994 scopus 로고
    • Opioid receptors are coupled tightly to G proteins but loosely to adenylate cyclase in NG108-15 cell membranes
    • Costa T., et al. Opioid receptors are coupled tightly to G proteins but loosely to adenylate cyclase in NG108-15 cell membranes. Mol. Pharmacol. 34 (1988) 744-754
    • (1988) Mol. Pharmacol. , vol.34 , pp. 744-754
    • Costa, T.1
  • 54
    • 1842333847 scopus 로고    scopus 로고
    • Positive cooperativity of acetylcholine and other agonists with allosteric ligands on muscarinic acetylcholine receptors
    • Jakubik J., et al. Positive cooperativity of acetylcholine and other agonists with allosteric ligands on muscarinic acetylcholine receptors. Mol. Pharmacol. 52 (1997) 172-179
    • (1997) Mol. Pharmacol. , vol.52 , pp. 172-179
    • Jakubik, J.1
  • 55
    • 3543144738 scopus 로고    scopus 로고
    • Spirodiketopiperazine-based CCR5 inhibitor which preserves CC-chemokine/CCR5 interactions and exerts potent activity against R5 human immunodeficiency virus type 1 in vitro
    • Maeda K., et al. Spirodiketopiperazine-based CCR5 inhibitor which preserves CC-chemokine/CCR5 interactions and exerts potent activity against R5 human immunodeficiency virus type 1 in vitro. J. Virol. 78 (2004) 8654-8662
    • (2004) J. Virol. , vol.78 , pp. 8654-8662
    • Maeda, K.1
  • 56
    • 15744391870 scopus 로고    scopus 로고
    • The CCR5 receptor-based mechanism of action of 873140, a potent allosteric non-competitive HIV entry-inhibitor
    • Watson C., et al. The CCR5 receptor-based mechanism of action of 873140, a potent allosteric non-competitive HIV entry-inhibitor. Mol. Pharmacol. 67 (2005) 1268-1282
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1268-1282
    • Watson, C.1
  • 57
    • 0023958554 scopus 로고
    • Estimation of the affinities of allosteric ligands using radioligand binding and pharmacological null methods
    • Ehlert F.J. Estimation of the affinities of allosteric ligands using radioligand binding and pharmacological null methods. Mol. Pharmacol. 33 (1988) 187-194
    • (1988) Mol. Pharmacol. , vol.33 , pp. 187-194
    • Ehlert, F.J.1
  • 58
    • 0021058380 scopus 로고
    • Operational models of pharmacological agonists
    • Black J.W., and Leff P. Operational models of pharmacological agonists. Proc. Roy. Soc. Lond. (Biol.) 220 (1983) 141-162
    • (1983) Proc. Roy. Soc. Lond. (Biol.) , vol.220 , pp. 141-162
    • Black, J.W.1    Leff, P.2
  • 59
    • 33751183557 scopus 로고    scopus 로고
    • Determining the potency and molecular mechanism of action of insurmountable antagonists
    • Kenakin T., et al. Determining the potency and molecular mechanism of action of insurmountable antagonists. J. Pharmacol. Exp. Ther. 319 (2006) 710-723
    • (2006) J. Pharmacol. Exp. Ther. , vol.319 , pp. 710-723
    • Kenakin, T.1
  • 60
    • 34447636846 scopus 로고    scopus 로고
    • Relationships between aplaviroc binding to CCR5 and binding of Sch-C, Sch-D, TAK779 and UK-427,857
    • Sage
    • Watson C., et al. Relationships between aplaviroc binding to CCR5 and binding of Sch-C, Sch-D, TAK779 and UK-427,857. Society for Biomolecular Sciences Handbook (2006), Sage 169
    • (2006) Society for Biomolecular Sciences Handbook , pp. 169
    • Watson, C.1
  • 61
    • 15744390934 scopus 로고    scopus 로고
    • β-Arrestin 2-dependent angiotensin II type 1A receptor-mediated pathway of chemotaxis
    • Hunton D.L., et al. β-Arrestin 2-dependent angiotensin II type 1A receptor-mediated pathway of chemotaxis. Mol. Pharmacol. 67 (2006) 1229-1236
    • (2006) Mol. Pharmacol. , vol.67 , pp. 1229-1236
    • Hunton, D.L.1
  • 62
    • 0034689003 scopus 로고    scopus 로고
    • β-Arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2
    • Defea K.A., et al. β-Arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2. J. Cell Biol. 148 (2000) 1267-1281
    • (2000) J. Cell Biol. , vol.148 , pp. 1267-1281
    • Defea, K.A.1
  • 63
    • 0037088585 scopus 로고    scopus 로고
    • 1a receptor stimulation
    • 1a receptor stimulation. J. Biol. Chem. 277 (2002) 9429-9436
    • (2002) J. Biol. Chem. , vol.277 , pp. 9429-9436
    • Tohgo, A.1
  • 64
    • 33645995745 scopus 로고    scopus 로고
    • The multiple personalities of the chemokine receptor CCR7 in dendritic cells
    • Sanchez-Sanchez N., et al. The multiple personalities of the chemokine receptor CCR7 in dendritic cells. J. Immunol. 176 (2006) 5153-5159
    • (2006) J. Immunol. , vol.176 , pp. 5153-5159
    • Sanchez-Sanchez, N.1
  • 65
    • 0026743033 scopus 로고
    • The thyrotropin receptor and the regulation of thyrocyte function and growth
    • Vassart G., and Dumont J.E. The thyrotropin receptor and the regulation of thyrocyte function and growth. Endocr. Rev. 13 (1992) 596-611
    • (1992) Endocr. Rev. , vol.13 , pp. 596-611
    • Vassart, G.1    Dumont, J.E.2
  • 66
    • 0034748701 scopus 로고    scopus 로고
    • Human pheochromocytomas express orexin receptor type 2 gene and display an in vitro secretory response to orexins A and B
    • Mazzocchi G., et al. Human pheochromocytomas express orexin receptor type 2 gene and display an in vitro secretory response to orexins A and B. J. Clin. Endocrinol. Metab. 86 (2001) 4818-4821
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 4818-4821
    • Mazzocchi, G.1
  • 67
    • 0035097290 scopus 로고    scopus 로고
    • Orexin A stimulates cortisol secretion from human adrenocortical cells through activation of the adenylate cyclase-dependent signaling cascade
    • Mazzocchi G., et al. Orexin A stimulates cortisol secretion from human adrenocortical cells through activation of the adenylate cyclase-dependent signaling cascade. J. Clin. Endocrinol. Metab. 86 (2001) 778-782
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 778-782
    • Mazzocchi, G.1
  • 68
    • 0036463901 scopus 로고    scopus 로고
    • Efficacy at G protein coupled receptors
    • Kenakin T.P. Efficacy at G protein coupled receptors. Nat. Rev. Drug Discov. 1 (2002) 103-109
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 103-109
    • Kenakin, T.P.1
  • 69
    • 0035958925 scopus 로고    scopus 로고
    • Bombesin and substance P analogues differentially regulate G-protein coupling to the bombesin receptor. Direct evidence for biased agonism
    • MacKinnon A.C., et al. Bombesin and substance P analogues differentially regulate G-protein coupling to the bombesin receptor. Direct evidence for biased agonism. J. Biol. Chem. 276 (2001) 28083-28091
    • (2001) J. Biol. Chem. , vol.276 , pp. 28083-28091
    • MacKinnon, A.C.1
  • 70
    • 0029778172 scopus 로고    scopus 로고
    • Morphine activates opioid receptors without causing their rapid internalization
    • Duane E., et al. Morphine activates opioid receptors without causing their rapid internalization. J. Biol. Chem. 271 (1996) 19021-19024
    • (1996) J. Biol. Chem. , vol.271 , pp. 19021-19024
    • Duane, E.1
  • 71
    • 25144499754 scopus 로고    scopus 로고
    • Differential activation of adenylate cyclase and receptor internalization by novel dopamine D1 receptor agonists
    • Ryman-Rasmussen J.P., et al. Differential activation of adenylate cyclase and receptor internalization by novel dopamine D1 receptor agonists. Mol. Pharmacol. 68 (2005) 1039-1048
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1039-1048
    • Ryman-Rasmussen, J.P.1
  • 72
    • 0031814749 scopus 로고    scopus 로고
    • 5]-enkephalin-μ-opioid receptor complexes demonstrated by cAMP-dependent protein kinase phosphorylation
    • 5]-enkephalin-μ-opioid receptor complexes demonstrated by cAMP-dependent protein kinase phosphorylation. J. Neurochem. 71 (1998) 231-239
    • (1998) J. Neurochem. , vol.71 , pp. 231-239
    • Chakrabarthi, S.1
  • 73
    • 14844333116 scopus 로고    scopus 로고
    • Internalization and Src activity regulate the time course of ERK activation by δ opioid receptor ligands
    • Audet N., et al. Internalization and Src activity regulate the time course of ERK activation by δ opioid receptor ligands. J. Biol. Chem. 280 (2005) 7808-7816
    • (2005) J. Biol. Chem. , vol.280 , pp. 7808-7816
    • Audet, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.