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Number of documents

35

Sophie Sacquin-Mora


Journal articles30 documents

  • Nicolas Bourassin, Marc Baaden, Elisabeth Lojou, Sophie Sacquin-Mora. Implicit Modeling of the Impact of Adsorption on Solid Surfaces for Protein Mechanics and Activity with a Coarse-Grain Representation. Journal of Physical Chemistry B, American Chemical Society, 2020, 15, ⟨10.1021/acs.jpcb.0c05347⟩. ⟨hal-02939019⟩
  • Hugo Schweke, Marie-Hélène Mucchielli, Sophie Sacquin-Mora, Wanying Bei, Anne Lopes. Protein interaction energy landscapes are shaped by functional and also non-functional partners. Journal of Molecular Biology, Elsevier, 2020, 432 (4), pp.1183. ⟨10.1016/j.jmb.2019.12.047⟩. ⟨hal-02445555⟩
  • Charles Bou-Nader, Ludovic Pecqueur, Pierre Barraud, Marc Fontecave, Carine Tisné, et al.. Conformational Stability Adaptation of a Double-Stranded RNA-Binding Domain to Transfer RNA Ligand. Biochemistry, American Chemical Society, 2019, ⟨10.1021/acs.biochem.9b00111⟩. ⟨hal-02307946⟩
  • Sophie Sacquin-Mora. Coarse-grain simulations on NMR conformational ensembles highlight functional residues in proteins. Journal of the Royal Society Interface, the Royal Society, 2019, 16 (156), pp.20190075. ⟨10.1098/rsif.2019.0075⟩. ⟨hal-02307948⟩
  • Vivek Hitaishi, Romain Clément, Nicolas Bourassin, Marc Baaden, Anne de Poulpiquet, et al.. Controlling Redox Enzyme Orientation at Planar Electrodes. Catalysts, MDPI, 2018, 8 (5), pp.192. ⟨10.3390/catal8050192⟩. ⟨hal-01793660⟩
  • Nika Abdollahi, Alexandre Albani, Eric Anthony, Agnes Baud, Mélissa Cardon, et al.. Meet-U: educating through research immersion. PLoS Computational Biology, Public Library of Science, 2018, 14 (3), pp.1-10. ⟨10.1371/journal.pcbi.1005992⟩. ⟨hal-01722019⟩
  • Sophie Sacquin-Mora. Mechanical variations in proteins with large-scale motions highlight the formation of structural locks. Journal of Structural Biology, Elsevier, 2018, 203 (3), pp.195-204. ⟨10.1016/j.jsb.2018.05.006⟩. ⟨hal-02104314⟩
  • Nathalie Lagarde, Alessandra Carbone, Sophie Sacquin-Mora. Hidden partners: Using cross-docking calculations to predict binding sites for proteins with multiple interactions. Proteins - Structure, Function and Bioinformatics, Wiley, 2018, 86 (7), pp.723-737. ⟨10.1002/prot.25506⟩. ⟨hal-02104315⟩
  • 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.), MAIK Nauka/Interperiodica : Springer Science+Business Media LLC, 2017, ⟨10.1021/acs.biochem.6b00988⟩. ⟨hal-01497972⟩
  • Nathalie Colloc’h, Sophie Sacquin-Mora, Giovanna Avella, Anne-Claire Dhaussy, Thierry Prangé, et al.. Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography.. Scientific Reports, Nature Publishing Group, 2017, 7 (1), pp.1858. ⟨10.1038/s41598-017-02097-1⟩. ⟨hal-01523850⟩
  • Sophie Sacquin-Mora. Bridging Enzymatic Structure Function via Mechanics: A Coarse-Grain Approach. Methods in Enzymology, Elsevier, 2016, ⟨10.1016/bs.mie.2016.05.022⟩. ⟨hal-01451158⟩
  • 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, 84 (10), pp.1408-1421 ⟨10.1002/prot.25086⟩. ⟨hal-01347160⟩
  • Yoann Laurin, Philippe Savarin, Charles Robert, 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⟩
  • Sophie Sacquin-Mora. Fold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus?. Journal of the Royal Society Interface, the Royal Society, 2015, ⟨10.1098/rsif.2015.0876⟩. ⟨hal-01451165⟩
  • Sophie Sacquin-Mora, Lydie Vamparys, Alessandra Carbone. How binding incorrect partners can lead to the prediction of correct interfaces: Results from a massive cross-docking study on proteins. Protein Science, Wiley, 2015, 24 (1, SI), pp.243-244. ⟨hal-01528524⟩
  • Sophie Sacquin-Mora, Chantal Prévost. Docking Peptides on Proteins: How to Open a Lock, in the Dark, with a Flexible Key. Structure, Elsevier (Cell Press), 2015, ⟨10.1016/j.str.2015.07.004⟩. ⟨hal-01451174⟩
  • 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, 16 (23), pp.11318-11322. ⟨10.1039/C4CP00510D⟩. ⟨hal-01493492⟩
  • 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, the Royal Society, 2014, 11 (91), pp.20130935. ⟨10.1098/rsif.2013.0935⟩. ⟨hal-01498046⟩
  • 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⟩
  • 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, 118 (48), in pres. ⟨10.1021/jp5089965⟩. ⟨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⟩
  • 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⟩
  • 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.. Journal of Biological Inorganic Chemistry, Springer Verlag, 2013, 18 (1), pp.111-22. ⟨10.1007/s00775-012-0956-2⟩. ⟨hal-00783539⟩
  • 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. Journal of the Royal Society Interface, the Royal Society, 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⟩
  • 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⟩
  • (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⟩
  • S. Sacquin-Mora, R. Lavery. Investigating the local flexibility of functional residues in hemoproteins.. Biophysical Journal, Biophysical Society, 2006, 90, pp.2706-2717. ⟨hal-00313391⟩

Conference papers2 documents

  • N Colloc'H, E Girard, T Prangé, P Carpentier, S Sacquin-Mora, et al.. Determinants of neuroglobin plasticity highlighted by high pressure crystallography and crystallography under moderate gas pressure. 13th SOLEIL user's meeting, Jan 2018, Palaiseau, France. ⟨hal-02267167⟩
  • N Colloc'H, E Girard, T Prangé, P Carpentier, S Sacquin-Mora, et al.. Determinants of neuroglobin plasticity highlighted by high pressure crystallography and crystallography under moderate gas pressure. 56th european high pressure research group meeting, Sep 2018, Aveiro, Portugal. ⟨hal-02267162⟩

Poster communications1 document

  • Thierry Prangé, E. Girard, Carpentier Philippe, S Sacquin-Mora, B Vallone, et al.. Determinants of neuroglobin plasticity highlighted by high pressure crystallography and crystallography under moderate gas pressure.. ESRF Usermeeting Symposium Opportunities in high pressure science at the ESRF, Feb 2018, Grenoble, France. ⟨hal-02266178⟩

Theses1 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⟩

Habilitation à diriger des recherches1 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⟩