An efficient kinetic model for assemblies of amyloid fibrils and its application to polyglutamine aggregation.

Autor: Stéphanie Prigent, Annabelle Ballesta, Frédérique Charles, Natacha Lenuzza, Pierre Gabriel, Léon Matar Tine, Human Rezaei, Marie Doumic

Publikováno v: PLoS ONE, Vol 7, Iss 11, p e43273 (2012)

Protein polymerization consists in the aggregation of single monomers into polymers that may fragment. Fibrils assembly is a key process in amyloid diseases. Up to now, protein aggregation was commonly mathematically simulated by a polymer size-struc

Externí odkaz: https://doaj.org/article/f5c069e2c26242c9a0d45eaf9bbec75a

Binding of methylene blue to a surface cleft inhibits the oligomerization and fibrillization of prion protein

Autor: Vincenzo Granata, Annalisa Pastore, Kris Pauwels, Stéphanie Prigent, Paola Cavaliere, Human Rezaei, Adriana Zagari, Joan Torrent

Publikováno v: BBA-Biochimica et Biophysica Acta
BBA-Biochimica et Biophysica Acta, Elsevier, 2013, 1832 (1), pp.20-8. ⟨10.1016/j.bbadis.2012.09.005⟩

International audience; Neurodegenerative protein misfolding diseases, including prionopathies, share the common feature of accumulating specific misfolded proteins, with a molecular mechanism closely related. Misfolded prion protein (PrP) generates

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c82ac78255a8cddfeb41539f2071501
https://doi.org/10.1016/j.bbadis.2012.09.005

Mechanistic insights into cellular alteration of prion by poly‐D‐lysine: the role of H2H3 domain

Autor: Stéphanie Prigent, Zhou Xu, A. Pastore, Franck Mouthon, Miquel Adrover, Jean-Philippe Deslys, Human Rezaei, Emmanuel Comoy

Publikováno v: FASEB Journal
FASEB Journal, 2011, 25 (10), pp.3426-35. ⟨10.1096/fj.11-187534⟩
www.fasebj.org
FASEB Journal, Federation of American Society of Experimental Biology, 2011, 25 (10), pp.3426-35. ⟨10.1096/fj.11-187534⟩

International audience; Misfolding of the prion protein (PrP) is the central feature of prion diseases. The conversion of the normal α-helical PrP(C) into a pathological β-enriched PrP(Sc) constitutes an early event in the infectious process. Sever

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04d97945902cf6cc24fb19c94433d755
https://doi.org/10.1096/fj.11-187534

SIZE DISTRIBUTION OF AMYLOID FIBRILS. MATHEMATICAL MODELS AND EXPERIMENTAL DATA

Autor: Harvey Thomas Banks, Marie Doumic, Hadjer Wafaa Haffaf, Marc Hoffmann, Human Rezaei, Stéphanie Prigent

Publikováno v: International Journal of Pure and Applied Mathematics
International Journal of Pure and Applied Mathematics, Academic Publishing Ltd, 2014, 93 (6), pp.845-878. ⟨10.12732/ijpam.v93i6.10⟩
International Journal of Pure and Apllied Mathematics
International Journal of Pure and Applied Mathematics, 2014, 93 (6), pp.845-878. ⟨10.12732/ijpam.v93i6.10⟩

International audience; More than twenty types of proteins can adopt misfolded conformations, which can co-aggregate into amyloid fibrils, and are related to pathologies such as Alzheimer's disease. This article surveys mathematical models for aggreg

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f48ebccdb32faff20a80f65f4d207aa
https://doi.org/10.12732/ijpam.v93i6.10

Decrypting Prion Protein Conversion into a β-Rich Conformer by Molecular Dynamics

Autor: Jens Kleinjung, Arianna Fornili, Cécile A. Dreiss, Franca Fraternali, Human Rezaei, Stéphanie Prigent, Nesrine Chakroun

Publikováno v: Journal of Chemical Theory and Computation
Journal of Chemical Theory and Computation, American Chemical Society, 2013, 9 (5), pp.2455-2465. ⟨10.1021/ct301118j⟩

International audience; Prion diseases are fatal neurodegenerative diseases characterized by the formation of β-rich oligomers and the accumulation of amyloid fibrillar deposits in the central nervous system. Understanding the conversion of the cell

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e685f19e57d94c3a32f7614f433a4410
https://hal.sorbonne-universite.fr/hal-00906739