Sonia Terrillon - Publications
Affiliations: | Pharmacy | Universite de Montpellier, Montpellier, Occitanie, France |
Year | Citation | Score | |||
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2005 | Charest PG, Terrillon S, Bouvier M. Monitoring agonist-promoted conformational changes of beta-arrestin in living cells by intramolecular BRET. Embo Reports. 6: 334-40. PMID 15776020 DOI: 10.1038/Sj.Embor.7400373 | 0.605 | |||
2004 | Granier S, Terrillon S, Pascal R, Déméné H, Bouvier M, Guillon G, Mendre C. A cyclic peptide mimicking the third intracellular loop of the V2 vasopressin receptor inhibits signaling through its interaction with receptor dimer and G protein. The Journal of Biological Chemistry. 279: 50904-14. PMID 15452133 DOI: 10.1074/Jbc.M405089200 | 0.625 | |||
2004 | Terrillon S, Bouvier M. Receptor activity-independent recruitment of betaarrestin2 reveals specific signalling modes. The Embo Journal. 23: 3950-61. PMID 15385966 DOI: 10.1038/Sj.Emboj.7600387 | 0.706 | |||
2004 | Terrillon S, Barberis C, Bouvier M. Heterodimerization of V1a and V2 vasopressin receptors determines the interaction with beta-arrestin and their trafficking patterns. Proceedings of the National Academy of Sciences of the United States of America. 101: 1548-53. PMID 14757828 DOI: 10.1073/Pnas.0305322101 | 0.722 | |||
2004 | Terrillon S, Bouvier M. Roles of G-protein-coupled receptor dimerization. Embo Reports. 5: 30-4. PMID 14710183 DOI: 10.1038/Sj.Embor.7400052 | 0.678 | |||
2003 | Terrillon S, Durroux T, Mouillac B, Breit A, Ayoub MA, Taulan M, Jockers R, Barberis C, Bouvier M. Oxytocin and vasopressin V1a and V2 receptors form constitutive homo- and heterodimers during biosynthesis. Molecular Endocrinology (Baltimore, Md.). 17: 677-91. PMID 12554793 DOI: 10.1210/Me.2002-0222 | 0.596 | |||
2002 | Terrillon S, Cheng LL, Stoev S, Mouillac B, Barberis C, Manning M, Durroux T. Synthesis and characterization of fluorescent antagonists and agonists for human oxytocin and vasopressin V(1)(a) receptors. Journal of Medicinal Chemistry. 45: 2579-88. PMID 12036367 DOI: 10.1021/Jm010526+ | 0.635 | |||
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