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Luc Bousset

Showing results (11-20 of 102) with videos related to

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Journal of Neurochemistry|June 30, 2019
α-synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicitiesParvez Alam, Luc Bousset, Ronald Melki, et al.
Scientific Reports|December 1, 2016
Nanomechanical properties of distinct fibrillar polymorphs of the protein α-synucleinAli Makky, Luc Bousset, Jérôme Polesel-Maris, et al.
Biochemical and Biophysical Research Communications|April 1, 2020
Dipeptide repeat derived from C9orf72 hexanucleotide expansions forms amyloids or natively unfolded structures in vitroLaurent Brasseur, Audrey Coens, Jehan Waeytens, et al.
Journal of Parkinson'S Disease|December 8, 2015
An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory MaterialsLuc Bousset, Patrik Brundin, Anja Böckmann, et al.
The Journal of Biological Chemistry|June 5, 2003
Assembly of the yeast prion Ure2p into protein fibrils. Thermodynamic and kinetic characterizationNicolas Fay, Yuji Inoue, Luc Bousset, et al.
The EMBO Journal|June 18, 2002
The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitroLuc Bousset, Neil H Thomson, Sheena E Radford, et al.
The Journal of Biological Chemistry|July 31, 2012
Identification of protein interfaces between α-synuclein, the principal component of Lewy bodies in Parkinson disease, and the molecular chaperones human Hsc70 and the yeast Ssa1pVirginie Redeker, Samantha Pemberton, Willy Bienvenut, et al.
Plos One|March 27, 2010
Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural contextLuc Bousset, Jonathan Bonnefoy, Yannick Sourigues, et al.
Comptes Rendus Biologies|February 28, 2002
Structure and assembly properties of the yeast prion Ure2pLuc Bousset, Carine Thual, Hassan Belrhali, et al.
Scientific Reports|July 19, 2018
Assessment of the efficacy of different procedures that remove and disassemble alpha-synuclein, tau and A-beta fibrils from laboratory material and surfacesAlexis Fenyi, Audrey Coens, Tracy Bellande, et al.
Pageof 11

Showing results (11-20 of 102) with videos related to

Sort By:
Pageof 11
Journal of Neurochemistry|June 30, 2019
α-synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicitiesParvez Alam, Luc Bousset, Ronald Melki, et al.
Scientific Reports|December 1, 2016
Nanomechanical properties of distinct fibrillar polymorphs of the protein α-synucleinAli Makky, Luc Bousset, Jérôme Polesel-Maris, et al.
Biochemical and Biophysical Research Communications|April 1, 2020
Dipeptide repeat derived from C9orf72 hexanucleotide expansions forms amyloids or natively unfolded structures in vitroLaurent Brasseur, Audrey Coens, Jehan Waeytens, et al.
Journal of Parkinson'S Disease|December 8, 2015
An Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory MaterialsLuc Bousset, Patrik Brundin, Anja Böckmann, et al.
The Journal of Biological Chemistry|June 5, 2003
Assembly of the yeast prion Ure2p into protein fibrils. Thermodynamic and kinetic characterizationNicolas Fay, Yuji Inoue, Luc Bousset, et al.
The EMBO Journal|June 18, 2002
The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitroLuc Bousset, Neil H Thomson, Sheena E Radford, et al.
The Journal of Biological Chemistry|July 31, 2012
Identification of protein interfaces between α-synuclein, the principal component of Lewy bodies in Parkinson disease, and the molecular chaperones human Hsc70 and the yeast Ssa1pVirginie Redeker, Samantha Pemberton, Willy Bienvenut, et al.
Plos One|March 27, 2010
Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural contextLuc Bousset, Jonathan Bonnefoy, Yannick Sourigues, et al.
Comptes Rendus Biologies|February 28, 2002
Structure and assembly properties of the yeast prion Ure2pLuc Bousset, Carine Thual, Hassan Belrhali, et al.
Scientific Reports|July 19, 2018
Assessment of the efficacy of different procedures that remove and disassemble alpha-synuclein, tau and A-beta fibrils from laboratory material and surfacesAlexis Fenyi, Audrey Coens, Tracy Bellande, et al.
Pageof 11