Publications

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Journal Article
Tabet J-C, Prévost C, Bouillot A, Bastard J, Manh DDo Khae, Tondeur Y.  1986.  Ion-Molecule reaction in the gas phase part VI Regioselective SN2 reaction from terpenoid diastereoisomeric diols using CI/NH 4+. Helv. Chim. Acta. 69:806–815.
Saladin A, Amourda C., Poulain P., Férey N, Baaden M, Zacharias M, Delalande O., Prévost C.  2010.  Modeling the early stage of DNA sequence recognition within RecA nucleoprotein filaments. Nucleic Acids Res.. 38:6313–6323.
Bertucat G, Lavery R, Prévost C.  2000.  A mechanism for RecA-promoted sequence homology recognition and strand exchange between single-stranded DNA and duplex DNA, via triple-helical intermediates. J. Biomol. Struct. Dyn.. :147–153.
Bastard J, Khac DDo, Fetizon M, Prévost C, Beloeil J-C.  1991.  Mechanism of the rearrangement of the bicyclo [4.2. 0] octan system to the bicyclo [3.2. 1] octan system. Tetrahedron. 47:229–238.
Laurin Y, Eyer J, Robert CH, Prévost C, Sacquin-Mora S.  2017.  Mobility and core-protein binding patterns of disordered C-terminal tails in β-tubulin isotypes.. Biochemistry. 56(12):1746–1756.
Bertucat G, Lavery R, Prévost C.  1998.  A model for parallel triple helix formation by RecA: single-single association with a homologous duplex via the minor groove. J. Biomol. Struct. Dyn.. 16:535–46.
Bertucat G, Lavery R, Prévost C.  1999.  A molecular model for RecA-promoted strand exchange via parallel triple-stranded helices. Biophys. J.. 77:1562–76.
Vovelle F, Prévost C, Durand M, Maurizot JC.  1996.  Molecular modelling study of the netropsin complexation with a nucleic acid triple helix. J. Biomol. Struct. Dyn.. 14:293–302.
Prévost C, Sacquin-Mora S.  2021.  Moving pictures: Reassessing docking experiments with a dynamic view of protein interfaces.. Proteins.
Manh DDo Khac, Fetizon M, Prévost C, Roy P.  1991.  NMR and conformational studies of the cyclobutane ring involved in the bicyclo [4.2. 0] octane system of a tetracyclic diterpene structure. Magn. Reson. Chem.. 29:870–877.
Miné-Hattab J, Fleury G, Prévost C, Dutreix M, Viovy J-L.  2011.  Optimizing the design of oligonucleotides for homology directed gene targeting. Plos One. 6:e14795.
Prévost C, Louise-May S, Ravishanker G, Lavery R, Beveridge DL.  1993.  Persistence analysis of the static and dynamical helix deformations of DNA oligonucleotides: application to the crystal structure and molecular dynamics simulation of d(CGCGAATTCGCG)2. Biopolymers. 33:335–50.
Danilowicz C, Yang D, Kelley C, Prévost C, Prentiss M.  2015.  The poor homology stringency in the heteroduplex allows strand exchange to incorporate desirable mismatches without sacrificing recognition in vivo. Nucleic Acids Res.. 43:6473–85.
Li C, Danilowicz C, Tashjian TF, Godoy VG, Prévost C, Prentiss M.  2019.  The positioning of Chi sites allows the RecBCD pathway to suppress some genomic rearrangements. Nucleic Acids Res. 47:1836-1846.
Saladin A, Fiorucci S, Poulain P, Prévost C, Zacharias M.  2009.  PTools: an opensource molecular docking library.. Bmc Struct. Biol.. 9:27–37.
Isabelle V, Prévost C, Spotheim-Maurizot M, Sabattier R, Charlier M.  1995.  Radiation-induced damages in single- and double-stranded DNA. Int. J. Radiat. Biol.. 67:169–76.
Kim R, Kanamaru S, Mikawa T, Prévost C, Ishii K, Ito K, Uchiyama S, Oda M, Iwasaki H, Kim SK et al..  2018.  RecA requires two molecules of Mg2+ ions for its optimal strand exchange activity in vitro. Nucleic Acids Res. ahead of print
Tashjian TF, Danilowicz C, Molza A-E, Nguyen BH, Prévost C, Prentiss M, Godoy VG.  2019.  Residues in the fingers domain of the translesion DNA polymerase DinB enable its unique participation in error-prone double-strand break repair. J Biol Chem. 294:7588-7600.
Berges R., Balzeau J., Takahashi M., Prévost C, Eyer J..  2012.  Structure-function analysis of the NFL-TBS.40-63 peptide corresponding to the binding site of tubulin on the light neurofilament subunit. Plos One. 7:e49436.
Lu D, Danilowicz C, Tashjian TF, Prévost C, Godoy VG, Prentiss M.  2019.  Slow extension of the invading DNA strand in a D-loop formed by RecA-mediated homologous recombination may enhance recognition of DNA homology. J Biol Chem. 294:8606-8616.
Bornet O., Prévost C, Vovelle F., Chassignol M., Thuong N.T, Lancelot G..  1995.  Solution structure of oligonucleotides covalently linked to a psoralen derivative.. Nucleic Acids Res.. 23:788–795.
Tran L, Basdevant N, Prévost C, Ha-Duong T.  2016.  Structure of ring-shaped Aβ42 oligomers determined by conformational selection. Sci. Rep.. 6:21429.
Prentiss M, Prévost C, Danilowicz C.  2015.  Structure/function relationships in RecA protein-mediated homology recognition and strand exchange. Crit. Rev. Biochem. Mol. Biol.. 50:453–76.
Boyer B, Danilowicz C, Prentiss M, Prévost C.  2019.  Weaving DNA strands: structural insight on ATP hydrolysis in RecA-induced homologous recombination. Nucleic Acids Res. 47:7798-7808.
Sacquin-Mora S, Prévost C.  2021.  When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes. Biomolecules. 11:1529.

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