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Author Title [ Type(Desc)] Year
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Journal Article
Bastard K, Saladin A, Prévost C.  2011.  Accounting for large amplitude protein deformation during in silico macromolecular docking. Int. J. Mol. Sci.. 12:1316–33.
Bastard K, Prévost C, Zacharias M.  2006.  Accounting for loop flexibility during protein-protein docking. Proteins. 62:956–969.
Danilowicz C, Hermans L, Coljee V, Prévost C, Prentiss M.  2017.  ATP hydrolysis provides functions that promote rejection of pairings between different copies of long repeated sequences. Nucleic Acids Res. 45:8448-8462.
Schneider S., Saladin A, Fiorucci S., Prévost C, Zacharias M..  2012.  ATTRACT and PTOOLS: Open source programs for protein-protein docking. Methods Mol. Biol.. 819:221–232.
Loriot S, Sachdeva S, Bastard K, Prévost C, Cazals F.  2011.  On the characterization and selection of diverse conformational ensembles with applications to flexible docking. Ieee/acm Trans. Comput. Biol. Bioinform.. 8:487–98.
Gabb H., Prévost C, Bertucat G., Robert CH, Lavery R.  1997.  Collective-variable Monte Carlo simulation of DNA. J. Comp. Chem.. 18:2001–2011.
Prévost C, Takahashi M., Lavery R.  2009.  Deforming DNA: from physics to biology. Chemphyschem. 10:1399–404.
Prévost C, Boudvillain M, Beudaert P, Leng M, Lavery R, Vovelle F.  1997.  Distortions of the DNA double helix induced by 1,3-trans-diamminedichloroplatinum(II)-intrastrand cross-link: An internal coordinate molecular modeling study. J. Biomol. Struct. Dyn.. 14:703–714.
Bastard K, Thureau A, Lavery R, Prévost C.  2003.  Docking macromolecules with flexible segments. J. Comput. Chem.. 24:1910–20.
Sacquin-Mora S, Prévost C.  2015.  Docking Peptides on Proteins: How to Open a Lock, in the Dark, with a Flexible Key. Structure. 23:1373–1374.
Gabb HA, Lavery R, Prévost C.  1995.  Efficient conformational space sampling for nucleosides using internal coordinate Monte-Carlo simulations and a modified furanose description. J. Comput. Chem.. 16:667–680.
Gabb HA, Sanghani SR, Robert CH, Prévost C.  1996.  Finding and visualizing nucleic acid base stacking. J Mol Graph. 14:6–11.
Prévost C, Takahashi M..  2003.  Geometry of the DNA strands within the RecA nucleofilament: role in homologous recombination. Q. Rev. Biophys.. 36:429–53.
Selmane T, Camadro JM, Conilleau S, Fleury F, Tran V, Prévost C, Takahashi M.  2004.  Identification of the subunit-subunit interface of Xenopus Rad51.1 protein: Similarity to RecA. J. Mol. Biol.. 335:895–904.
Danilowicz C, Vietorisz E, Godoy-Carter V, Prévost C, Prentiss M.  2021.  Influences of ssDNA-RecA Filament Length on the Fidelity of Homologous Recombination. Journal of Molecular Biology. 433:167143.
Poulain P, Saladin A, Hartmann B, Prévost C.  2008.  Insights on protein-DNA recognition by coarse grain modelling. J. Comput. Chem.. 29:2582–92.
Yang D, Boyer B, Prévost C, Danilowicz C, Prentiss M.  2015.  Integrating multi-scale data on homologous recombination into a new recognition mechanism based on simulations of the RecA-ssDNA/dsDNA structure. Nucleic Acids Res.. 43:10251–63.
Boyer B, Ezelin J, Poulain P, Saladin A, Zacharias M, Robert CH, Prévost C.  2015.  An integrative approach to the study of filamentous oligomeric assemblies, with application to RecA. Plos One. in press:e0116414.