@article {2015|1586,
	title = {Investigating the Structural Variability and Binding Modes of the Glioma Targeting NFL-TBS.40-63 Peptide on Tubulin},
	journal = {Biochemistry},
	volume = {54},
	number = {23},
	year = {2015},
	month = {jun},
	pages = {3660{\textendash}3669},
	doi = {10.1021/acs.biochem5b00146},
	author = {Laurin, Y. and Savarin, P. and Charles H. Robert and M. Takahashi and Eyer, J. and Chantal Pr{\'e}vost and S Sacquin-Mora}
}
@article {2012|1527,
	title = {{S}tructure-function analysis of the {NFL}-{TBS}.40-63 peptide corresponding to the binding site of tubulin on the light neurofilament subunit},
	journal = {Plos One},
	volume = {7},
	year = {2012},
	pages = {e49436},
	author = {Berges, R. and Balzeau, J. and Takahashi, M. and Chantal Pr{\'e}vost and Eyer, J.}
}
@article {2009|1636,
	title = {Deforming DNA: from physics to biology},
	journal = {Chemphyschem},
	volume = {10},
	year = {2009},
	month = {jul},
	pages = {1399{\textendash}404},
	abstract = {<p>The DNA double helix has become a modern icon which symbolizes our understanding of the molecular basis of life. It is less widely recognized that the double helix proposed by Watson and Crick more than half a century ago is a remarkably adaptable molecule that can undergo major conformational rearrangements without being irreversibly damaged. Indeed, DNA deformation is an intrinsic feature of many of the biological processes in which it is involved. Over the last two decades, single-molecule experiments coupled with molecular modeling have transformed our understanding of DNA flexibility, while the accumulation of high-resolution structures of DNA-protein complexes have demonstrated how organisms can exploit this property as a useful feature for preserving, reading, replicating, and packaging the genetic message. In this Minireview we summarize the information now available on the extreme\&ndash;and the less extreme\&ndash;deformations of the double helix.</p>},
	doi = {10.1002/cphc.200900253},
	author = {Chantal Pr{\'e}vost and M. Takahashi and Richard Lavery}
}
@article {2003|1761,
	title = {Geometry of the DNA strands within the RecA nucleofilament: role in homologous recombination},
	journal = {Q. Rev. Biophys.},
	volume = {36},
	year = {2003},
	month = {nov},
	pages = {429{\textendash}53},
	abstract = {<p>Homologous recombination consists of exchanging DNA strands of identical or almost identical sequence. This process is important for both DNA repair and DNA segregation. In prokaryotes, it involves the formation of long helical filaments of the RecA protein on DNA. These filaments incorporate double-stranded DNA from the cell\&$\#$39;s genetic material, recognize sequence homology and promote strand exchange between the two DNA segments. DNA processing by these nucleofilaments is characterized by large amplitude deformations of the double helix, which is stretched by 50\% and unwound by 40\% with respect to B-DNA. In this article, information concerning the structure and interactions of the RecA, DNA and ATP molecules involved in DNA strand exchange is gathered and analyzed to present a view of their possible arrangement within the filament, their behavior during strand exchange and during ATP hydrolysis, the mechanism of RecA-promoted DNA deformation and the role of DNA deformation in the process of homologous recombination. In particular, the unusual characteristics of DNA within the RecA filament are compared to the DNA deformations locally induced by architectural proteins which bind in the DNA minor groove. The possible role and location of two flexible loops of RecA are discussed.</p>},
	author = {Chantal Pr{\'e}vost and M. Takahashi}
}
@article {2001|1841,
	title = {Sheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solution},
	journal = {J. Biol. Chem.},
	volume = {276},
	number = {49},
	year = {2001},
	pages = {46364{\textendash}46370},
	author = {S. A. Kozin and G. Bertho and Alexey K Mazur and H. Rabesona and J. P. Girault and T. Haertle and M. Takahashi and P. Debey and G. H. Hoa}
}
