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Methods in Cell Biology|May 15, 2010
Mass spectrometry analysis of C-terminal posttranslational modifications of tubulinsVirginie Redeker
Molecular Microbiology|March 5, 2014
A role for the proteasome in the turnover of Sup35p and in [PSI(+) ] prion propagationMehdi Kabani, Virginie Redeker, Ronald Melki
The Journal of Biological Chemistry|September 30, 2021
Structural mapping techniques distinguish the surfaces of fibrillar 1N3R and 1N4R human tauEmilie Caroux, Virginie Redeker, Karine Madiona, et al.
FEBS Letters|October 10, 2002
N-terminal acetylation of ectopic recombinant proteins in Escherichia coliElodie Charbaut, Virginie Redeker, Jean Rossier, et al.
Plos One|August 14, 2020
Polypeptides derived from α-Synuclein binding partners to prevent α-Synuclein fibrils interaction with and take-up by cellsElodie Monsellier, Maya Bendifallah, Virginie Redeker, 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.
The Journal of Biological Chemistry|May 2, 2021
The differential solvent exposure of N-terminal residues provides "fingerprints" of alpha-synuclein fibrillar polymorphsMaud Landureau, Virginie Redeker, Tracy Bellande, et al.
Plos One|June 27, 2015
The 26S Proteasome Degrades the Soluble but Not the Fibrillar Form of the Yeast Prion Ure2p In VitroKai Wang, Virginie Redeker, Karine Madiona, et al.
Research in Microbiology|December 30, 2023
The stringent response is strongly activated in the antibiotic producing strain, Streptomyces coelicolorClara Lejeune, David Cornu, Laila Sago, et al.
Frontiers in Microbiology|April 8, 2022
A Proteomic Analysis Indicates That Oxidative Stress Is the Common Feature Triggering Antibiotic Production in <i>Streptomyces coelicolor</i> and in the <i>pptA</i> Mutant of <i>Streptomyces lividans</i>Clara Lejeune, Laila Sago, David Cornu, et al.
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