EDP Sciences logo
Subscriber Authentication Point
Search
Menu
Home All issues Volume 28 / No 10 (Octobre 2012) Med Sci (Paris), 28 10 (2012) 876-882 References
Free Access
Issue
Med Sci (Paris)
Volume 28, Number 10, Octobre 2012
Page(s) 876 - 882
Section Récepteurs couplés aux protéines G
DOI https://doi.org/10.1051/medsci/20122810017
Published online 12 October 2012
  1. Gloriam DE, Fredriksson R, Schioth HB. The G protein-coupled receptor subset of the rat genome. BMC Genomics 2007 ; 8 : 338. [CrossRef] [PubMed] [Google Scholar]
  2. DeWire SM, Ahn S, Lefkowitz RJ, Shenoy SK. Beta-arrestins and cell signaling. Annu Rev Physiol 2007 ; 69 : 483–510. [CrossRef] [PubMed] [Google Scholar]
  3. Kobilka BK, Deupi X. Conformational complexity of G-protein-coupled receptors. Trends Pharmacol Sci 2007 ; 28 : 397–406. [CrossRef] [PubMed] [Google Scholar]
  4. Dror RO, Arlow DH, Borhani DW, et al. Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations. Proc Natl Acad Sci USA 2009 ; 106 : 4689–4694. [CrossRef] [Google Scholar]
  5. Katritch V, Cherezov V, Stevens RC. Diversity and modularity of G protein-coupled receptor structures. Trends Pharmacol Sci 2012 ; 33 : 17–27. [CrossRef] [PubMed] [Google Scholar]
  6. Deupi X, Standfuss J. Structural insights into agonist-induced activation of G-protein-coupled receptors. Curr Opin Struct Biol 2011 ; 21 : 541–551. [CrossRef] [PubMed] [Google Scholar]
  7. Kobilka BK. Structural insights into adrenergic receptor function and pharmacology. Trends Pharmacol Sci 2011 ; 32 : 213–218. [CrossRef] [PubMed] [Google Scholar]
  8. Choe HW, Park JH, Kim YJ, Ernst OP. Transmembrane signaling by GPCRs: insight from rhodopsin and opsin structures. Neuropharmacology 2011 ; 60 : 52–57. [CrossRef] [PubMed] [Google Scholar]
  9. 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]
  10. Tate CG, Schertler GF. Engineering G protein-coupled receptors to facilitate their structure determination. Curr Opin Struct Biol 2009 ; 19 : 386–395. [CrossRef] [PubMed] [Google Scholar]
  11. Hanson MA, Cherezov V, Griffith MT, et al. A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor. Structure 2008 ; 16 : 897–905. [CrossRef] [PubMed] [Google Scholar]
  12. 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]
  13. 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]
  14. Wacker D, Fenalti G, Brown MA, et al. Conserved binding mode of human beta2 adrenergic receptor inverse agonists and antagonist revealed by X-ray crystallography. J Am Chem Soc 2010 ; 132 : 11443–11445. [CrossRef] [PubMed] [Google Scholar]
  15. Jaakola VP, Griffith MT, Hanson MA, et al. The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 2008 ; 322 : 1211–1217. [CrossRef] [PubMed] [Google Scholar]
  16. Chien EY, Liu W, Zhao Q, et al. Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist. Science 2010 ; 330 : 1091–1095. [CrossRef] [PubMed] [Google Scholar]
  17. Shimamura T, Shiroishi M, Weyand S, et al. Structure of the human histamine H1 receptor complex with doxepin. Nature 2011 ; 475 : 65–70. [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. Kruse AC, Hu J, Pan AC, et al. Structure and dynamics of the M3 muscarinic acetylcholine receptor. Nature 2012 ; 482 : 552–556. [CrossRef] [PubMed] [Google Scholar]
  20. Haga K, Kruse AC, Asada H, et al. Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist. Nature 2012 ; 482 : 547–551. [CrossRef] [PubMed] [Google Scholar]
  21. Hanson MA, Roth CB, Jo E, et al. Crystal structure of a lipid G protein-coupled receptor. Science 2012 ; 335 : 851–855. [CrossRef] [PubMed] [Google Scholar]
  22. Serrano-Vega MJ, Magnani F, Shibata Y, Tate CG. Conformational thermostabilization of the beta1-adrenergic receptor in a detergent-resistant form. Proc Natl Acad Sci USA 2008 ; 105 : 877–882. [CrossRef] [Google Scholar]
  23. Shibata Y, White JF, Serrano-Vega MJ, et al. Thermostabilization of the neurotensin receptor NTS1. J Mol Biol 2009 ; 390 : 262–277. [CrossRef] [PubMed] [Google Scholar]
  24. Magnani F, Shibata Y, Serrano-Vega MJ, Tate CG. Co-evolving stability and conformational homogeneity of the human adenosine A2a receptor. Proc Natl Acad Sci USA 2008 ; 105 : 10744–10749. [CrossRef] [Google Scholar]
  25. Lebon G, Bennett K, Jazayeri A, Tate CG. Thermostabilisation of an agonist-bound conformation of the human adenosine A(2A) receptor. J Mol Biol 2011 ; 409 : 298–310. [CrossRef] [PubMed] [Google Scholar]
  26. Warne T, Serrano-Vega MJ, Baker JG, et al. Structure of a beta1-adrenergic G-protein-coupled receptor. Nature 2008 ; 454 : 486–491. [CrossRef] [PubMed] [Google Scholar]
  27. Dore AS, Robertson N, Errey JC, et al. Structure of the adenosine A(2A) receptor in complex with ZM241385 and the xanthines XAC and caffeine. Structure 2011 ; 19 : 1283–1293. [CrossRef] [PubMed] [Google Scholar]
  28. Moukhametzianov R, Warne T, Edwards PC, et al. Two distinct conformations of helix 6 observed in antagonist-bound structures of a beta1-adrenergic receptor. Proc Natl Acad Sci USA 2011 ; 108 : 8228–8232. [CrossRef] [Google Scholar]
  29. Rasmussen SG, Choi HJ, Fung JJ, et al. Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor. Nature 2011 ; 469 : 175–180. [CrossRef] [PubMed] [Google Scholar]
  30. Steyaert J, Kobilka BK. Nanobody stabilization of G protein-coupled receptor conformational states. Curr Opin Struct Biol 2011 ; 21 : 567–572. [CrossRef] [PubMed] [Google Scholar]
  31. Warne T, Moukhametzianov R, Baker JG, et al. The structural basis for agonist and partial agonist action on a beta1-adrenergic receptor. Nature 2011 ; 469 : 241–244. [CrossRef] [PubMed] [Google Scholar]
  32. Rosenbaum DM, Zhang C, Lyons JA, et al. Structure and function of an irreversible agonist-beta2 adrenoceptor complex. Nature 2011 ; 469 : 236–240. [CrossRef] [PubMed] [Google Scholar]
  33. Standfuss J, Edwards PC, D’Antona A, et al. The structural basis of agonist-induced activation in constitutively active rhodopsin. Nature 2011 ; 471 : 656–660. [CrossRef] [PubMed] [Google Scholar]
  34. Choe HW, Kim YJ, Park JH, et al. Crystal structure of metarhodopsin II. Nature 2011 ; 471 : 651–655. [CrossRef] [PubMed] [Google Scholar]
  35. Scheerer P, Park JH, Hildebrand PW, et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 2008 ; 455 : 497–502. [CrossRef] [PubMed] [Google Scholar]
  36. Lebon G, Warne T, Edwards PC, et al. Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation. Nature 2011 ; 474 : 521–525. [CrossRef] [PubMed] [Google Scholar]
  37. Lebon G, Tate CG. Structure tridimensionnelle du récepteur de l’adénosine A2A lié à son agoniste naturel l’adénosine. Med Sci (Paris) 2011 ; 27 : 926–928. [CrossRef] [EDP Sciences] [PubMed] [Google Scholar]
  38. Xu F, Wu H, Katritch V, et al. Structure of an agonist-bound human A2A adenosine receptor. Science 2011 ; 332 : 322–327. [CrossRef] [PubMed] [Google Scholar]
  39. 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]
  40. 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]
  41. Fritze O, Filipek S, Kuksa V, et al. Role of the conserved NPxxY(x)5, 6F motif in the rhodopsin ground state and during activation. Proc Natl Acad Sci USA 2003 ; 100 : 2290–2295. [CrossRef] [Google Scholar]
  42. Granier S. Structure des récepteurs mu et delta des opiacés. Med Sci (Paris) 2012 ; 28 : 870–875. [CrossRef] [EDP Sciences] [PubMed] [Google Scholar]
  43. Banères JL, Mouillac B. Manipulation des RCPG : expression, purification et stabilisation in vitro. Med Sci (Paris) 2012 ; 28 : 837–844. [CrossRef] [EDP Sciences] [PubMed] [Google Scholar]

Current usage metrics show cumulative count of Article Views (full-text article views including HTML views, PDF and ePub downloads, according to the available data) and Abstracts Views on Vision4Press platform.

Data correspond to usage on the plateform after 2015. The current usage metrics is available 48-96 hours after online publication and is updated daily on week days.

Initial download of the metrics may take a while.