Transduction of Receptor Signals by ??-Arrestins, Science, vol.308, issue.5721, pp.512-517, 2005. ,
DOI : 10.1126/science.1109237
Therapeutic potential of ??-arrestin- and G protein-biased agonists, Trends in Molecular Medicine, vol.17, issue.3, pp.126-139, 2011. ,
DOI : 10.1016/j.molmed.2010.11.004
Molecular Mechanism of ??-Arrestin-Biased Agonism at Seven-Transmembrane Receptors, Annual Review of Pharmacology and Toxicology, vol.52, issue.1, pp.179-197, 2012. ,
DOI : 10.1146/annurev.pharmtox.010909.105800
URL : https://hal.archives-ouvertes.fr/hal-01129592
Functional specialization of beta-arrestin interactions revealed by proteomic analysis, Proceedings of the National Academy of Sciences, vol.104, issue.29, pp.12011-12016, 2007. ,
DOI : 10.1073/pnas.0704849104
??-Arrestin-kinase scaffolds: turn them on or turn them off?, Wiley Interdisciplinary Reviews: Systems Biology and Medicine, vol.9, issue.Pt 3, pp.231-241, 2013. ,
DOI : 10.1002/wsbm.1203
MEK1 Binds Directly to ??Arrestin1, Influencing Both Its Phosphorylation by ERK and the Timing of Its Isoprenaline-stimulated Internalization, Journal of Biological Chemistry, vol.284, issue.17, pp.11425-11435, 2009. ,
DOI : 10.1074/jbc.M806395200
How Does Arrestin Assemble MAPKs into a Signaling Complex?, Journal of Biological Chemistry, vol.284, issue.1, pp.685-695, 2009. ,
DOI : 10.1074/jbc.M806124200
Beta-arrestins as regulators of signal termination and transduction: How do they determine what to scaffold?, Cellular Signalling, vol.23, issue.4, pp.621-629, 2011. ,
DOI : 10.1016/j.cellsig.2010.10.004
Ultra-fast FFT protein docking on graphics processors, Bioinformatics, vol.26, issue.19, pp.2398-405, 2010. ,
DOI : 10.1093/bioinformatics/btq444
URL : https://hal.archives-ouvertes.fr/inria-00537988
A Multidomain Flexible Docking Approach to Deal with Large Conformational Changes in the Modeling of Biomolecular Complexes, Structure, vol.19, issue.4, pp.555-565, 2011. ,
DOI : 10.1016/j.str.2011.01.014
Prediction of Multimolecular Assemblies by Multiple Docking, Journal of Molecular Biology, vol.349, issue.2, pp.435-447, 2005. ,
DOI : 10.1016/j.jmb.2005.03.039
Adrenergic Receptor-Src Protein Kinase Complexes, Science, vol.283, issue.5402, pp.655-661, 1999. ,
DOI : 10.1126/science.283.5402.655
The proliferative and antiapoptotic effects of substance P are facilitated by formation of a beta -arrestin-dependent scaffolding complex, Proceedings of the National Academy of Sciences, vol.97, issue.20, pp.11086-11091, 2000. ,
DOI : 10.1073/pnas.190276697
Arrestin Serves as a Molecular Switch, Linking Endogenous ??2-Adrenergic Receptor to SRC-dependent, but Not SRC-independent, ERK Activation, Journal of Biological Chemistry, vol.281, issue.36, pp.25948-25955, 2006. ,
DOI : 10.1074/jbc.M605415200
Mechanistic principles of RAF kinase signaling, Cellular and Molecular Life Sciences, vol.114, issue.4, pp.553-565, 2011. ,
DOI : 10.1007/s00018-010-0520-6
Crystal structure of the Src family tyrosine kinase Hck, Nature, vol.385, issue.6617, pp.602-609, 1997. ,
DOI : 10.1038/385602a0
Crystal Structure of the Src Family Kinase Hck SH3-SH2 Linker Regulatory Region Supports an SH3-dominant Activation Mechanism, Journal of Biological Chemistry, vol.285, issue.46, pp.35455-35461, 2010. ,
DOI : 10.1074/jbc.M110.145102
A Single Mutation in Arrestin-2 Prevents ERK1/2 Activation by Reducing c-Raf1 Binding, Biochemistry, vol.50, issue.32, pp.6951-6958, 2011. ,
DOI : 10.1021/bi200745k
Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes, EMBO J, vol.13, pp.1123-1131, 1994. ,
-adrenoceptor signalling via the ERK1/2 MAPKs, Biochemical Journal, vol.413, issue.1, pp.51-60, 2008. ,
DOI : 10.1042/BJ20080685
URL : https://hal.archives-ouvertes.fr/cea-01058940
Visualization of arrestin recruitment by a G-protein-coupled receptor, Nature, vol.157, issue.7513, pp.218-240, 2014. ,
DOI : 10.1038/nature13430
Structure and function of an irreversible agonist-??2 adrenoceptor complex, Nature, vol.14, issue.7329, pp.236-240, 2011. ,
DOI : 10.1038/nature09665
Few Residues within an Extensive Binding Interface Drive Receptor Interaction and Determine the Specificity of Arrestin Proteins, Journal of Biological Chemistry, vol.286, issue.27, pp.24288-24299, 2011. ,
DOI : 10.1074/jbc.M110.213835
Role of Receptor-attached Phosphates in Binding of Visual and Non-visual Arrestins to G Protein-coupled Receptors, Journal of Biological Chemistry, vol.287, issue.12, pp.9028-9040, 2012. ,
DOI : 10.1074/jbc.M111.311803
Manipulation of Very Few Receptor Discriminator Residues Greatly Enhances Receptor Specificity of Non-visual Arrestins, Journal of Biological Chemistry, vol.287, issue.35, pp.29495-29505, 2012. ,
DOI : 10.1074/jbc.M112.366674
Mapping the Arrestin-Receptor Interface: STRUCTURAL ELEMENTS RESPONSIBLE FOR RECEPTOR SPECIFICITY OF ARRESTIN PROTEINS, Journal of Biological Chemistry, vol.279, issue.2, pp.1262-1268, 2004. ,
DOI : 10.1074/jbc.M308834200
The interaction with the cytoplasmic loops of rhodopsin plays a crucial role in arrestin activation and binding, Journal of Neurochemistry, vol.272, issue.5, pp.1040-1050, 2003. ,
DOI : 10.1046/j.1471-4159.2003.01598.x
Probing the Structural Determinants for the Function of Intracellular Loop 2 in Structurally Cognate G-Protein-Coupled Receptors, Biochemistry, vol.49, issue.50, pp.10691-10701, 2010. ,
DOI : 10.1021/bi100580s
A proline-rich sequence unique to MEK1 and MEK2 is required for raf binding and regulates MEK function., Molecular and Cellular Biology, vol.15, issue.10, pp.5214-5225, 1995. ,
DOI : 10.1128/MCB.15.10.5214
Structure of active ??-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide, Nature, vol.27, issue.7447, pp.137-141, 2013. ,
DOI : 10.1038/nature12120
Distinct Phosphorylation Sites on the ??2-Adrenergic Receptor Establish a Barcode That Encodes Differential Functions of ??-Arrestin, Science Signaling, vol.4, issue.185, pp.10-1126, 2011. ,
DOI : 10.1126/scisignal.2001707
Competing G protein-coupled receptor kinases balance G protein and ??-arrestin signaling, Molecular Systems Biology, vol.3, p.590, 2012. ,
DOI : 10.1038/msb.2012.22
URL : https://hal.archives-ouvertes.fr/hal-00776169
Protein???Protein Docking with Backbone Flexibility, Journal of Molecular Biology, vol.373, issue.2, pp.503-519, 2007. ,
DOI : 10.1016/j.jmb.2007.07.050
Structure of an Arrestin2-Clathrin Complex Reveals a Novel Clathrin Binding Domain That Modulates Receptor Trafficking, Journal of Biological Chemistry, vol.284, issue.43, pp.29860-29872, 2009. ,
DOI : 10.1074/jbc.M109.023366
Arrestin-Dependent Activation of ERK and Src Family Kinases, Handb Exp Pharmacol, vol.219, pp.225-257, 2014. ,
DOI : 10.1007/978-3-642-41199-1_12
Integration of Protein Abundance and Structure Data Reveals Competition in the ErbB Signaling Network, Science Signaling, vol.6, issue.306, pp.10-1126, 2013. ,
DOI : 10.1126/scisignal.2004560
Assessment of CAPRI predictions in rounds 3-5 shows progress in docking procedures, Proteins: Structure, Function, and Bioinformatics, vol.13, issue.Suppl 6, pp.150-69, 2005. ,
DOI : 10.1002/prot.20551
A new protein protein docking scoring function based on interface residue properties, Bioinformatics, vol.23, issue.5, pp.555-62, 2007. ,
DOI : 10.1093/bioinformatics/btl654
URL : https://hal.archives-ouvertes.fr/inria-00431697
Reducing the Time Complexity of the Derandomized Evolution Strategy with Covariance Matrix Adaptation (CMA-ES), Evolutionary Computation, vol.11, issue.1, pp.1-18, 2003. ,
DOI : 10.1162/106365601750190398
Protein-protein docking benchmark version 4.0, Proteins: Structure, Function, and Bioinformatics, vol.20, issue.Web Server issu, pp.3111-3115, 2010. ,
DOI : 10.1002/prot.22830
DiMoVo: a Voronoi tessellation-based method for discriminating crystallographic and biological protein-protein interactions, Bioinformatics, vol.24, issue.5, pp.652-660, 2008. ,
DOI : 10.1093/bioinformatics/btn022
URL : https://hal.archives-ouvertes.fr/inria-00431696
A statistical test for comparing success rates, Proceedings of the fifth metaheuristics international conference (MIC2003), p.7812, 2003. ,
Nonvisual Arrestin Oligomerization and Cellular Localization Are Regulated by Inositol Hexakisphosphate Binding, Journal of Biological Chemistry, vol.281, issue.14, pp.9812-9823, 2006. ,
DOI : 10.1074/jbc.M512703200
Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes, Journal of Molecular Biology, vol.406, issue.3, pp.467-478, 2011. ,
DOI : 10.1016/j.jmb.2010.12.034
Three-dimensional structure of the tyrosine kinase c-Src, Nature, vol.385, issue.6617, pp.595-602, 1997. ,
DOI : 10.1038/385595a0
Ras/Rap effector specificity determined by charge reversal, Nature Structural Biology, vol.11, issue.8, pp.723-729, 1996. ,
DOI : 10.1107/S0021889892009944
Crystal Structures of MEK1 Binary and Ternary Complexes with Nucleotides and Inhibitors, Biochemistry, vol.48, issue.12, pp.2661-2674, 2009. ,
DOI : 10.1021/bi801898e
Crystal structure of human mono-phosphorylated ERK1 at Tyr204, Biochemical and Biophysical Research Communications, vol.377, issue.4, pp.1123-1127, 2008. ,
DOI : 10.1016/j.bbrc.2008.10.127
Crystal structure of the ??2 adrenergic receptor???Gs protein complex, Nature, vol.61, issue.7366, pp.549-555, 2011. ,
DOI : 10.1038/nature10361
A beta-Arrestin Binding Determinant Common to the Second Intracellular Loops of Rhodopsin Family G Protein-coupled Receptors, Journal of Biological Chemistry, vol.281, issue.5, pp.2932-2938, 2006. ,
DOI : 10.1074/jbc.M508074200
Allosteric Modulation of M1 Muscarinic Acetylcholine Receptor Internalization and Subcellular Trafficking, Journal of Biological Chemistry, vol.289, issue.22, pp.15856-15866, 2014. ,
DOI : 10.1074/jbc.M113.536672
beta -Arrestin1 Interacts with the Catalytic Domain of the Tyrosine Kinase c-SRC. ROLE OF beta -ARRESTIN1-DEPENDENT TARGETING OF c-SRC IN RECEPTOR ENDOCYTOSIS, Journal of Biological Chemistry, vol.275, issue.15, pp.11312-11319, 2000. ,
DOI : 10.1074/jbc.275.15.11312