@article {2017,
	title = {Mobility and core-protein binding patterns of disordered C-terminal tails in β-tubulin isotypes.},
	journal = {Biochemistry},
	volume = { 56},
	year = {2017},
	pages = {1746{\textendash}1756},
	chapter = {1746},
	abstract = {<p>Although they play a significant part in the regulation of microtubule structure, dynamics and function, the disordered C-terminal tails of tubulin remain invisible to experimental structural methods and do not appear in the crystallographic structures that are currently available in the Protein Data Bank. Interestingly, these tails concentrate most of the sequence variability between tubulin isotypes, and are the sites of the principal post-translational modifications undergone by this protein. Using homology modeling, we developed two complete models for the human αI/βI and αI/βIII tubulin isotypes that include their C-terminal tails. We then investigated the conformational variability of the two β-tails using long time-scale classical Molecular Dynamics (MD) simulations that revealed similar features, notably the unexpected presence of common anchoring regions on the surface of the tubulin dimer, but also distinctive mobility or interaction patterns, some of which could be related to the tail lengths and charge distributions. We also observed in our simulations that the C-terminal tail from the βI isotype, but not the βIII, formed contacts in the putative binding site of a recently discovered peptide that disrupts microtubule formation in glioma cells. Hindering the binding site in the βI isotype would be consistent with this peptide\&rsquo;s preferential disruption of microtubule formation in glioma, whose cells overexpress βIII, compared to normal glial cells. While these observations need to be confirmed with more intensive sampling, our study opens up new perspectives for the development of isotype-specific chemotherapy drugs.</p>
},
	doi = {10.1021/acs.biochem.6b00988},
	author = {Laurin, Yoann and Eyer, Joel and Charles H. Robert and Chantal Pr{\'e}vost and S Sacquin-Mora}
}
@article {2015|1965,
	title = {An integrative approach to the study of filamentous oligomeric assemblies, with application to {R}ec{A}},
	journal = {Plos One},
	volume = {in press},
	year = {2015},
	pages = {e0116414},
	abstract = {<p>Oligomeric macromolecules in the cell self-organize into a wide variety of geometrical motifs such as helices, rings or linear filaments. The recombinase proteins involved in homologous recombination present many such assembly motifs. Here, we examine in particular the polymorphic characteristics of RecA, the most studied member of the recombinase family, using an integrative approach that relates local modes of monomer/monomer association to the global architecture of their screw-type organization. In our approach, local modes of association are sampled via docking or Monte Carlo simulations. This enables shedding new light on fiber morphologies that may be adopted by the RecA protein. Two distinct RecA helical morphologies, the so-called \&quot;extended\&quot; and \&quot;compressed\&quot; forms, are known to play a role in homologous recombination. We investigate the variability within each form in terms of helical parameters and steric accessibility. We also address possible helical discontinuities in RecA filaments due to multiple monomer-monomer association modes. By relating local interface organization to global filament morphology, the strategies developed here to study RecA self-assembly are particularly well suited to other DNA-binding proteins and to filamentous protein assemblies in general.</p>},
	doi = {10.1371/journal.pone.0116414},
	author = {Benjamin Boyer and Johann Ezelin and Pierre Poulain and A Saladin and Martin Zacharias and Charles H. Robert and Chantal Pr{\'e}vost}
}
@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 {1997|1680,
	title = {Collective-variable Monte Carlo simulation of DNA},
	journal = {J. Comp. Chem.},
	volume = {18},
	year = {1997},
	pages = {2001{\textendash}2011},
	author = {H. Gabb and Chantal Pr{\'e}vost and G. Bertucat and Charles H. Robert and Richard Lavery}
}
@article {1996|1666,
	title = {Finding and visualizing nucleic acid base stacking},
	journal = {J Mol Graph},
	volume = {14},
	number = {1},
	year = {1996},
	month = {feb},
	pages = {6{\textendash}11},
	author = {Gabb, H A and Sanghani, S R and Charles H. Robert and Chantal Pr{\'e}vost}
}
