Métaphores, nomenclature et nouveaux paradigmes de signalisation par les récepteurs couplés aux protéines G

Michel Bouvier

doi:10.1051/medsci/20122810002

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Volume 28 / Numéro 10 (Octobre 2012)

Med Sci (Paris), 28 10 (2012) 801-803

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Editorial

Numéro		Med Sci (Paris) Volume 28, Numéro 10, Octobre 2012


Page(s)		801 - 803
Section		Éditoriaux
DOI		https://doi.org/10.1051/medsci/20122810002
Publié en ligne		12 octobre 2012

Maehle AH, Prüll CR, Halliwell RF. The emergence of the drug receptor theory. Nat Rev Drug Discov 2002 ; 1 : 637–641. [CrossRef] [PubMed] [Google Scholar]
Hill SJ. G-protein-coupled receptors: past, present and future. Br J Pharmacol 2006 ; 147 : S27–S37. [CrossRef] [PubMed] [Google Scholar]
Lewontin R. La triple hélice. Paris : Seuil, 2003 : 154 p. [Google Scholar]
Chidiac P, Hébert T, Dennis M, Bouvier M. Inverse agonist activity of β2-adrenergic antagonists. Mol Pharmacol 1994 ; 45 : 490–499. [PubMed] [Google Scholar]
Bond RA, Bouvier M. Inverse agonists and G protein-coupled receptors. In : Leff P, ed. Receptor-based drug design, chap. 16. New York : Marcel Dekker Inc., 1998 : 363–377. [Google Scholar]
Azzi M, Charest P, Angers S, et al. β-arrestin-dependent activation of MAPK pathway by β2-adrenergic receptor inverse agonists. Proc Natl Acad Sci USA 2003 ; 100 : 11406–11411. [CrossRef] [Google Scholar]
Kenakin TP. Collateral efficacy in drug discovery: taking advantage of the good (allosteric) nature of 7TM receptors. Trends Pharmacol Sci 2007 ; 28 : 407–415. [CrossRef] [PubMed] [Google Scholar]
Galandrin S, Oligny-Longpré G, Bouvier M. The evasive nature of drug efficacy : implications for drug discovery. Trends Pharmacol Sci 2007 ; 28 : 423–430. [CrossRef] [PubMed] [Google Scholar]
Angers S, Salahpour A, Bouvier M. Dimerization: an emerging concept for G protein-coupled receptors, ontogeny and function. Annu Rev Pharmacol Toxicol 2002 ; 42 : 409–435. [CrossRef] [PubMed] [Google Scholar]
Smith NJ, Milligan G. Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapes. Pharmacol Rev 2010 ; 62 : 701–725. [CrossRef] [PubMed] [Google Scholar]
Palczewski K, Kumasaka T, Hori T, et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 2000 ; 289 : 739–745. [CrossRef] [PubMed] [Google Scholar]
Cherezov V, Rosenbaum DM, Hanson MA, et al. High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 2007 ; 318 : 1258–1265. [CrossRef] [PubMed] [Google Scholar]
Rasmussen SG, Choi HJ, Rosenbaum DM, et al. Crystal structure of the human beta2 adrenergic G-protein-coupled receptor. Nature 2007 ; 450 : 383–387. [CrossRef] [PubMed] [Google Scholar]
Rosenbaum DM, Cherezov V, Hanson MA, et al. GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function. Science 2007 ; 318 : 1266–1273. [CrossRef] [PubMed] [Google Scholar]
Onaran H.A, Costa T. Where have all the active receptor states gone? Nat Chem Biol 2012 ; 8 : 674–647. [CrossRef] [PubMed] [Google Scholar]
Rasmussen SG, Choi HJ, Fung JJ, et al. Structure of a nanobody-stabilized active state of the beta2 adrenoceptor. Nature 2011 ; 469 : 175–180. [CrossRef] [PubMed] [Google Scholar]
Rasmussen SG, DeVree BT, Zou Y, et al. Crystal structure of the beta2 adrenergic receptor-Gs protein complex. Nature 2011 ; 477 : 549–555. [CrossRef] [PubMed] [Google Scholar]
Wu B, Chien EY, Mol CD, et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. Science 2010 ; 330 : 1066–1071. [CrossRef] [PubMed] [Google Scholar]
Manglik A, Kruse AC, Kobilka TS. Crystal structure of the micro-opioid receptor bound to a morphinan antagonist. Nature 2012 ; 485 : 321–326. [CrossRef] [PubMed] [Google Scholar]
Wu H, Wacker D, Mileni M, et al. Structure of the human kappa-opioid receptor in complex with JDTic. Nature 2012 ; 485 : 327–332. [CrossRef] [PubMed] [Google Scholar]

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[1] Maehle AH, Prüll CR, Halliwell RF. The emergence of the drug receptor theory. Nat Rev Drug Discov 2002 ; 1 : 637–641. [CrossRef] [PubMed] [Google Scholar]

[2] Hill SJ. G-protein-coupled receptors: past, present and future. Br J Pharmacol 2006 ; 147 : S27–S37. [CrossRef] [PubMed] [Google Scholar]

[3] Lewontin R. La triple hélice. Paris : Seuil, 2003 : 154 p. [Google Scholar]

[4] Chidiac P, Hébert T, Dennis M, Bouvier M. Inverse agonist activity of β2-adrenergic antagonists. Mol Pharmacol 1994 ; 45 : 490–499. [PubMed] [Google Scholar]

[5] Bond RA, Bouvier M. Inverse agonists and G protein-coupled receptors. In : Leff P, ed. Receptor-based drug design, chap. 16. New York : Marcel Dekker Inc., 1998 : 363–377. [Google Scholar]

[6] Azzi M, Charest P, Angers S, et al. β-arrestin-dependent activation of MAPK pathway by β2-adrenergic receptor inverse agonists. Proc Natl Acad Sci USA 2003 ; 100 : 11406–11411. [CrossRef] [Google Scholar]

[7] Kenakin TP. Collateral efficacy in drug discovery: taking advantage of the good (allosteric) nature of 7TM receptors. Trends Pharmacol Sci 2007 ; 28 : 407–415. [CrossRef] [PubMed] [Google Scholar]

[8] Galandrin S, Oligny-Longpré G, Bouvier M. The evasive nature of drug efficacy : implications for drug discovery. Trends Pharmacol Sci 2007 ; 28 : 423–430. [CrossRef] [PubMed] [Google Scholar]

[9] Angers S, Salahpour A, Bouvier M. Dimerization: an emerging concept for G protein-coupled receptors, ontogeny and function. Annu Rev Pharmacol Toxicol 2002 ; 42 : 409–435. [CrossRef] [PubMed] [Google Scholar]

[10] Smith NJ, Milligan G. Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapes. Pharmacol Rev 2010 ; 62 : 701–725. [CrossRef] [PubMed] [Google Scholar]

[11] Palczewski K, Kumasaka T, Hori T, et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 2000 ; 289 : 739–745. [CrossRef] [PubMed] [Google Scholar]

[12] Cherezov V, Rosenbaum DM, Hanson MA, et al. High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 2007 ; 318 : 1258–1265. [CrossRef] [PubMed] [Google Scholar]

[13] Rasmussen SG, Choi HJ, Rosenbaum DM, et al. Crystal structure of the human beta2 adrenergic G-protein-coupled receptor. Nature 2007 ; 450 : 383–387. [CrossRef] [PubMed] [Google Scholar]

[14] Rosenbaum DM, Cherezov V, Hanson MA, et al. GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function. Science 2007 ; 318 : 1266–1273. [CrossRef] [PubMed] [Google Scholar]

[15] Onaran H.A, Costa T. Where have all the active receptor states gone? Nat Chem Biol 2012 ; 8 : 674–647. [CrossRef] [PubMed] [Google Scholar]

[16] Rasmussen SG, Choi HJ, Fung JJ, et al. Structure of a nanobody-stabilized active state of the beta2 adrenoceptor. Nature 2011 ; 469 : 175–180. [CrossRef] [PubMed] [Google Scholar]

[17] Rasmussen SG, DeVree BT, Zou Y, et al. Crystal structure of the beta2 adrenergic receptor-Gs protein complex. Nature 2011 ; 477 : 549–555. [CrossRef] [PubMed] [Google Scholar]

[18] Wu B, Chien EY, Mol CD, et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. Science 2010 ; 330 : 1066–1071. [CrossRef] [PubMed] [Google Scholar]

[19] Manglik A, Kruse AC, Kobilka TS. Crystal structure of the micro-opioid receptor bound to a morphinan antagonist. Nature 2012 ; 485 : 321–326. [CrossRef] [PubMed] [Google Scholar]

[20] Wu H, Wacker D, Mileni M, et al. Structure of the human kappa-opioid receptor in complex with JDTic. Nature 2012 ; 485 : 327–332. [CrossRef] [PubMed] [Google Scholar]