M. Koenig, A. P. Monaco, and L. M. Kunkel, The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein, Cell, vol.53, issue.2, pp.219-226, 1988.
DOI : 10.1016/0092-8674(88)90383-2

M. Koenig, E. P. Hoffman, C. J. Bertelson, A. P. Monaco, C. Feener et al., Complete cloning of the duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals, Cell, vol.50, issue.3, pp.509-517, 1987.
DOI : 10.1016/0092-8674(87)90504-6

L. Rumeur, E. Hubert, J. F. Winder, and S. J. , A new twist to coiled coil, FEBS Letters, vol.380, issue.17, pp.2717-2739, 2012.
DOI : 10.1016/j.febslet.2012.05.004

URL : https://hal.archives-ouvertes.fr/inserm-00700015

L. Rumeur, E. Winder, S. J. Hubert, and J. F. , Dystrophin: More than just the sum of its parts, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1804, issue.9, pp.1713-1722, 2010.
DOI : 10.1016/j.bbapap.2010.05.001

URL : https://hal.archives-ouvertes.fr/hal-00592430

S. J. Winder, T. J. Gibson, K. , and J. , Dystrophin and utrophin: the missing links!, FEBS Letters, vol.288, issue.1, pp.27-33, 1995.
DOI : 10.1016/0014-5793(95)00398-S

K. J. Amann, B. A. Renley, and J. M. Ervasti, A Cluster of Basic Repeats in the Dystrophin Rod Domain Binds F-actin through an Electrostatic Interaction, Journal of Biological Chemistry, vol.273, issue.43, 1998.
DOI : 10.1074/jbc.273.43.28419

I. N. Rybakova, K. J. Amann, and J. M. Ervasti, A new model for the interaction of dystrophin with F-actin, The Journal of Cell Biology, vol.135, issue.3, pp.661-672, 1996.
DOI : 10.1083/jcb.135.3.661

Y. Lai, G. D. Thomas, Y. Yue, H. T. Yang, D. Li et al., Dystrophins carrying spectrin-like repeats 16 and 17 anchor nNOS to the sarcolemma and enhance exercise performance in a mouse model of muscular dystrophy, Journal of Clinical Investigation, vol.119, issue.3, pp.624-635, 2009.
DOI : 10.1172/JCI36612DS1

Y. Lai, J. Zhao, Y. Yue, and D. Duan, ??2 and ??3 helices of dystrophin R16 and R17 frame a microdomain in the ??1 helix of dystrophin R17 for neuronal NOS binding, Proceedings of the National Academy of Sciences, vol.110, issue.2, pp.525-530, 2012.
DOI : 10.1073/pnas.1211431109

S. Legardinier, C. Raguenes-nicol, C. Tascon, C. Rocher, S. Hardy et al., Mapping of the Lipid-Binding and Stability Properties of the Central Rod Domain of Human Dystrophin, Journal of Molecular Biology, vol.389, issue.3, pp.546-558, 2009.
DOI : 10.1016/j.jmb.2009.04.025

URL : https://hal.archives-ouvertes.fr/inserm-00404317

J. Sarkis, V. Vié, S. J. Winder, A. Renault, E. Le-rumeur et al., Resisting sarcolemmal rupture: dystrophin repeats increase membrane-actin stiffness, The FASEB Journal, vol.27, issue.1, pp.359-67, 2013.
DOI : 10.1096/fj.12-208967

URL : https://hal.archives-ouvertes.fr/hal-00806086

S. Tuffery-giraud, C. Béroud, F. Leturcq, R. B. Yaou, D. Hamroun et al., Genotype-phenotype analysis in 2,405 patients with a dystrophinopathy using the UMD-DMD database: a model of nationwide knowledgebase, Human Mutation, vol.23, issue.6, pp.934-979, 2009.
DOI : 10.1002/humu.20976

A. Tek, M. Chavent, M. Baaden, O. Delalande, P. Bourdot et al., Advances in Human-Protein Interaction -Interactive and Immersive Molecular Simulations, Protein-Protein Interactions -Computational and Experimental Tools, Nucleic Acids Research, vol.38, issue.16, pp.978-953, 2010.

M. Muthu, K. A. Richardson, A. J. Sutherland-smith, M. Delarue, and Y. H. Sanejouand, PLoS One 7, e40066. (20), J Mol Biol Protein Engineering, vol.320, issue.14, pp.1011-1035, 2001.

S. Schneider, A. Saladin, S. Fiorucci, C. Prévost, M. Zacharias et al., ATTRACT and PTOOLS: Open Source Programs for Protein???Protein Docking, Methods Mol Biol Proteins, vol.819, issue.60, pp.221-253, 2005.
DOI : 10.1007/978-1-61779-465-0_15

URL : https://hal.archives-ouvertes.fr/hal-01498107

X. Periole, M. Cavalli, S. J. Marrink, M. Ceruso, C. Globisch et al., Combining an Elastic Network With a Coarse-Grained Molecular Force Field: Structure, Dynamics, and Intermolecular Recognition, Proc Natl Acad Sci U S A 98, pp.2531-2574, 1998.
DOI : 10.1021/ct9002114

M. V. Petoukhov, D. Franke, A. V. Shkumatov, G. Tira, A. G. Kikhney et al., program package for small-angle scattering data analysis, Journal of Applied Crystallography, vol.36, issue.2, pp.342-50, 2012.
DOI : 10.1107/S0021889812007662/fs5015sup1.pdf

W. Humphrey, A. Dalke, and K. Schulten, VMD: Visual molecular dynamics, Journal of Molecular Graphics, vol.14, issue.1, pp.33-38, 1996.
DOI : 10.1016/0263-7855(96)00018-5

O. Delalande, N. Férey, G. Grasseau, and M. Baaden, Complex molecular assemblies at hand via interactive simulations, Journal of Computational Chemistry, vol.39, issue.2 Part 1, pp.2375-87, 2009.
DOI : 10.1002/jcc.21235

URL : https://hal.archives-ouvertes.fr/inserm-00713313

E. F. Pettersen, T. D. Goddard, C. C. Huang, G. S. Couch, D. M. Greenblatt et al., UCSF Chimera?A visualization system for exploratory research and analysis, Journal of Computational Chemistry, vol.373, issue.13, pp.1605-1617, 2004.
DOI : 10.1002/jcc.20084

T. V. Pyrkov, A. O. Chugunov, N. A. Krylov, D. E. Noldel, R. G. Efremov et al., PLATINUM: a web tool for analysis of hydrophobic/hydrophilic organization of biomolecular complexes, Bioinformatics, vol.25, issue.9, pp.1201-1202, 2009.
DOI : 10.1093/bioinformatics/btp111

E. Giudice, A. E. Molza, Y. Laurin, A. Nicolas, E. Le-rumeur et al., Molecular Clues about the Dystrophin???Neuronal Nitric Oxide Synthase Interaction: A Theoretical Approach, Biochemistry, vol.52, issue.44, pp.7777-84, 2013.
DOI : 10.1021/bi400794p

URL : https://hal.archives-ouvertes.fr/hal-00935150

K. Y. Chan, J. Gumbart, R. Mcgreevy, J. M. Watermeyer, B. T. Sewell et al., Symmetry-Restrained Flexible Fitting for Symmetric EM Maps, Structure, vol.19, issue.9, pp.1211-1229, 2011.
DOI : 10.1016/j.str.2011.07.017