Nombre de documents

22

CV de Sophie Sacquin-Mora


Article dans une revue20 documents

  • Yoann Laurin, Joël Eyer, Charles H. Robert, C Prévost, S. Sacquin-Mora. Mobility and core-protein binding patterns of disordered C-terminal tails in β-tubulin isotypes.. Biochemistry (mosc.), 2017, <10.1021/acs.biochem.6b00988>. <hal-01497972>
  • Lydie Vamparys, Benoist Laurent, Alessandra Carbone, Sophie Sacquin-Mora. Great interactions: How binding incorrect partners can teach us about protein recognition and function. Proteins - Structure, Function and Bioinformatics, Wiley, 2016, <10.1002/prot.25086>. <hal-01347160>
  • Sophie Sacquin-Mora, Chantal Prévost. Docking Peptides on Proteins: How to Open a Lock, in the Dark, with a Flexible Key. Structure, 2015, <10.1016/j.str.2015.07.004>. <hal-01451174>
  • Sophie Sacquin-Mora. Fold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus?. Journal of the Royal Society Interface, Royal Society, 2015, <10.1098/rsif.2015.0876>. <hal-01451165>
  • Yoann Laurin, Philippe Savarin, Charles Roberts, Masayuki Takahashi, Joël Eyer, et al.. Investigating the Structural Variability and Binding Modes of the Glioma Targeting NFL-TBS.40-63 Peptide on Tubulin. Biochemistry, American Chemical Society, 2015, <10.1021/acs.biochem.5b00146>. <hal-01451181>
  • Francesco Oteri, Alexandre Ciaccafava, Anne De Poulpiquet, Marc Baaden, Elisabeth. Lojou, et al.. The weak, fluctuating, dipole moment of membrane-bound hydrogenase from Aquifex aeolicus accounts for its adaptability to charged electrodes. PCCP : Physical chemistry chemical physics, Royal Society of Chemistry, 2014, 16, pp.11318-11322. <http://pubs.rsc.org/en/Content/ArticleLanding/2014/CP/c4cp00510d#!divAbstract>. <10.1039/C4CP00510D >. <hal-01493492>
  • Francesco Oteri, Alexandre Ciaccafava, Anne De Poulpiquet, Marc Baaden, Elisabeth Lojou, et al.. The weak, fluctuating, dipole moment of membrane-bound hydrogenase from Aquifex aeolicus accounts for its adaptability to charged electrodes.. Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2014, pp.11318-22. <hal-01084630>
  • Sophie Sacquin-Mora. Motions and mechanics: investigating conformational transitions in multi-domain proteins with coarse-grain simulations. Mol. Simul., 2014, 40 (1-3), pp.229--236. <10.1080/08927022.2013.843176>. <hal-01498044>
  • Sree V. Chintapalli, Christopher J. R. Illingworth, Graham J. G. Upton, Sophie Sacquin-Mora, Philip J. Reeves, et al.. Assessing the effect of dynamics on the closed-loop protein-folding hypothesis. Journal of the Royal Society Interface, Royal Society, 2014, 11 (91), pp.20130935. <10.1098/rsif.2013.0935>. <hal-01498046>
  • Francesco Oteri, Marc Baaden, Elisabeth Lojou, Sophie Sacquin-Mora. Multiscale Simulations Give Insight into the Hydrogen in- and out-Pathways of [NiFe]-Hydrogenases from Aquifex Aeolicus and Desulfovibrio Fructosovorans.. Journal of Physical Chemistry B, American Chemical Society, 2014, in pres. <hal-01084622>
  • A Bocahut, V Derrien, S Bernad, P. Sebban, S Sacquin-Mora, et al.. Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin. Journal of Biological Inorganic Chemistry, Springer Verlag, 2013, 18 (1). <hal-01326196>
  • Anthony Bocahut, Valérie Derrien, Sophie Bernad, Pierre Sebban, Sophie Sacquin-Mora, et al.. Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin.. J Biol Inorg Chem, 2013, 18 (1), pp.111-22. <10.1007/s00775-012-0956-2>. <hal-00783539>
  • Anne Lopes, Sophie Sacquin-Mora, Viktoriya Dimitrova, Elodie Laine, Yann Ponty, et al.. Protein-protein interactions in a crowded environment: an analysis via cross-docking simulations and evolutionary information. PLoS Computational Biology, Public Library of Science, 2013, 9 (12), pp.e1003369. <10.1371/journal.pcbi.1003369>. <hal-00875116>
  • A. M. Stadler, C. J. Garvey, A. Bocahut, S. Sacquin-Mora, I. Digel, et al.. Thermal fluctuations of haemoglobin from different species: adaptation to temperature via conformational dynamics. J. R. Soc. Interface, 2012, 9 (76), pp.2845--2855. <10.1098/rsif.2012.0364>. <hal-01498101>
  • Olivier Delalande, Sophie Sacquin-Mora, Marc Baaden. Enzyme closure and nucleotide binding structurally lock guanylate kinase.. Biophysical Journal, Biophysical Society, 2011, 101 (6), pp.1440-9. <10.1016/j.bpj.2011.07.048>. <hal-00645163>
  • Sophie Sacquin-Mora, Olivier Delalande, Marc Baaden. Functional Modes and Residue Flexibility Control the Anisotropic Response of Guanylate Kinase to Mechanical Stress. Biophysical Journal, Biophysical Society, 2010, 99 (10), pp.3412-3419. <10.1016/j.bpj.2010.09.026>. <hal-00602505>
  • Stefan Engelen, Ladislas Trojan, Sophie Sacquin-Mora, Richard Lavery, Alessandra Carbone. Joint evolutionary trees: a large-scale method to predict protein interfaces based on sequence sampling.. PLoS Computational Biology, Public Library of Science, 2009, 5 (1), pp.e1000267. <10.1371/journal.pcbi.1000267>. <inserm-00705756>
  • (lavery Laveryr, (sacquin-Mora Sacquin-Moras, Xxxx Sophie). Probing macromolecular mechanics: Heterogeneity and function. JOURNAL OF BIOMOLECULAR STRUCTURE, 2007, xxx, pp.763-763. <hal-00315127>
  • R. Lavery, S. Sacquin-Mora. Protein mechanics: a route from structure to function.. Journal of Biosciences, Indian Academy of Sciences, 2007, 32, pp.891-898. <hal-00315141>
  • S. Sacquin-Mora, R. Lavery. Investigating the local flexibility of functional residues in hemoproteins.. Biophys J, 2006, 90, pp.2706-2717. <hal-00313391>

HDR1 document

  • Sacquin-Mora Sophie. Représentations gros-grain pour la modélisation des protéines : Propriétés mécaniques et interactions. Chimie théorique et/ou physique. Université Paris-Diderot - Paris VII, 2011. <tel-00652917>

Thèse1 document

  • Sophie Sacquin-Mora. Fluides nanoconfinés dans des systèmes de basse symétrie : Simulations et théorie. Analyse de données, Statistiques et Probabilités [physics.data-an]. Université Paris Sud - Paris XI, 2003. Français. <tel-00008790>