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Conformational disorder.
Longhi S, Lieutaud P, Canard B. Longhi S, et al. Among authors: canard b. Methods Mol Biol. 2010;609:307-25. doi: 10.1007/978-1-60327-241-4_18. Methods Mol Biol. 2010. PMID: 20221927
Structural genomics of the SARS coronavirus: cloning, expression, crystallization and preliminary crystallographic study of the Nsp9 protein.
Campanacci V, Egloff MP, Longhi S, Ferron F, Rancurel C, Salomoni A, Durousseau C, Tocque F, Brémond N, Dobbe JC, Snijder EJ, Canard B, Cambillau C. Campanacci V, et al. Among authors: canard b. Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1628-31. doi: 10.1107/s0907444903016779. Epub 2003 Aug 19. Acta Crystallogr D Biol Crystallogr. 2003. PMID: 12925794 Free PMC article.
Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein.
Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, Longhi S. Johansson K, et al. Among authors: canard b. J Biol Chem. 2003 Nov 7;278(45):44567-73. doi: 10.1074/jbc.M308745200. Epub 2003 Aug 27. J Biol Chem. 2003. PMID: 12944395 Free article.
The phosphoprotein of measles virus is a modular protein consisting of an intrinsically disordered N-terminal domain (Karlin, D., Longhi, S., Receveur, V., and Canard, B. (2002) Virology 296, 251-262) and of a C-terminal moiety (PCT) composed of alternating disorder …
The phosphoprotein of measles virus is a modular protein consisting of an intrinsically disordered N-terminal domain (Karlin, D., Longhi, S. …
Measles virus (MV) nucleoprotein binds to a novel cell surface receptor distinct from FcgammaRII via its C-terminal domain: role in MV-induced immunosuppression.
Laine D, Trescol-Biémont MC, Longhi S, Libeau G, Marie JC, Vidalain PO, Azocar O, Diallo A, Canard B, Rabourdin-Combe C, Valentin H. Laine D, et al. Among authors: canard b. J Virol. 2003 Nov;77(21):11332-46. doi: 10.1128/jvi.77.21.11332-11346.2003. J Virol. 2003. PMID: 14557619 Free PMC article.
279 results