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Yassmine Chebaro
Researcher at University of Strasbourg
Publications - 27
Citations - 1401
Yassmine Chebaro is an academic researcher from University of Strasbourg. The author has contributed to research in topics: Nuclear receptor & Gene. The author has an hindex of 16, co-authored 25 publications receiving 1127 citations. Previous affiliations of Yassmine Chebaro include Paris Diderot University & French Institute of Health and Medical Research.
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Journal ArticleDOI
Allostery in Its Many Disguises: From Theory to Applications
Shoshana J. Wodak,Emanuele Paci,Nikolay V. Dokholyan,Nikolay V. Dokholyan,Igor N. Berezovsky,Amnon Horovitz,Jing Li,Vincent J. Hilser,Ivet Bahar,John Karanicolas,Gerhard Stock,Peter Hamm,Roland H. Stote,Jerome Eberhardt,Yassmine Chebaro,Annick Dejaegere,Marco Cecchini,Jean-Pierre Changeux,Peter G. Bolhuis,Jocelyne Vreede,Pietro Faccioli,Simone Orioli,Riccardo Ravasio,Le Yan,Carolina Brito,Matthieu Wyart,Paraskevi Gkeka,Ivan Rivalta,Giulia Palermo,Giulia Palermo,J. Andrew McCammon,Joanna Panecka-Hofman,Rebecca C. Wade,Rebecca C. Wade,Antonella Di Pizio,Masha Y. Niv,Ruth Nussinov,Chung-Jung Tsai,Hyunbum Jang,Dzmitry Padhorny,Dima Kozakov,Tom McLeish +41 more
TL;DR: An overview of the progress and remaining limitations in the understanding of the mechanistic foundations of allostery gained from computational and experimental analyses of real protein systems and model systems is provided.
Journal ArticleDOI
Crucial role of nonspecific interactions in amyloid nucleation
TL;DR: It is shown that oligomers not only help peptides meet each other but also, create an environment that facilitates the conversion of monomers into the β-sheet–rich form characteristic of fibrils, which is in direct contrast with predictions from classical nucleation theory.
Journal ArticleDOI
The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems.
Fabio Sterpone,Simone Melchionna,Pierre Tufféry,Samuela Pasquali,Normand Mousseau,Tristan Cragnolini,Yassmine Chebaro,Jean-François St-Pierre,Maria Kalimeri,Alessandro Barducci,Yoann Laurin,Alex Tek,Marc Baaden,Phuong H. Nguyen,Philippe Derreumaux,Philippe Derreumaux +15 more
TL;DR: The current state of the OPEP coarse-grained protein model and the most exciting applications using advanced conformational sampling methods are reviewed and a perspective on the ongoing developments is presented.
Journal ArticleDOI
The coarse-grained OPEP force field for non-amyloid and amyloid proteins.
TL;DR: A refined version of the coarse-grained optimized potential for efficient protein structure prediction (OPEP) based on a six-bead representation is presented, indicating the effectiveness of the OPEP4 coarse- grained model for protein folding and aggregation, and report two future directions for improvement.
Journal ArticleDOI
Structures and Thermodynamics of Alzheimer’s Amyloid-β Aβ(16−35) Monomer and Dimer by Replica Exchange Molecular Dynamics Simulations: Implication for Full-Length Aβ Fibrillation
TL;DR: The loop structure ensemble reported in Abeta16-35 monomer and dimer has high similarity to the loop formed by the Abeta21-30 peptide in solution and, to a lesser extent, to the loops found in AbETA1-40 fibrils.