R
Raphael Guerois
Researcher at Université Paris-Saclay
Publications - 141
Citations - 6919
Raphael Guerois is an academic researcher from Université Paris-Saclay. The author has contributed to research in topics: Homologous recombination & DNA repair. The author has an hindex of 41, co-authored 129 publications receiving 6001 citations. Previous affiliations of Raphael Guerois include Centre national de la recherche scientifique & French Alternative Energies and Atomic Energy Commission.
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Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations.
TL;DR: The present energy function uses a minimum of computational resources and can therefore easily be used in protein design algorithms, and in the field of protein structure and folding pathways prediction where one requires a fast and accurate energy function.
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Activation of NRF2 by Nitrosative Agents and H2O2 Involves KEAP1 Disulfide Formation
TL;DR: It is proposed that KEAP1 intermolecular disulfide formation via Cys151 underlies the activation of NRF2 by reactive oxygen and nitrogen species.
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Structural basis for signaling by exclusive EDS1 heteromeric complexes with SAG101 or PAD4 in plant innate immunity.
Stephan Wagner,Johannes Stuttmann,Steffen Rietz,Raphael Guerois,Raphael Guerois,Elena Brunstein,Jaqueline Bautor,Karsten Niefind,Jane E. Parker +8 more
TL;DR: Although there is evolutionary conservation of α/β hydrolase topology in all three proteins, a noncatalytic resistance mechanism is indicated and the respective N-terminal domains appear to facilitate binding of the essential EP domains to create novel interaction surfaces on the heterodimer.
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PP2C Phosphatases Ptc2 and Ptc3 Are Required for DNA Checkpoint Inactivation after a Double-Strand Break
Christophe Leroy,Sang Eun Lee,Moreshwar B. Vaze,Françoise Ochsenbien,Raphael Guerois,James E. Haber,Marie Claude Marsolier-Kergoat +6 more
TL;DR: In this paper, the PP2C-like phosphatases Ptc2 and Ptc3 are shown to specifically bind to the Rad53 FHA1 domain and inactivate Rad53-dependent pathways during adaptation and recovery by dephosphorylating Rad53.
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20S Proteasome Assembly Is Orchestrated by Two Distinct Pairs of Chaperones in Yeast and in Mammals
Benoît Le Tallec,Marie Bénédicte Barrault,Régis Courbeyrette,Raphael Guerois,Marie Claude Marsolier-Kergoat,Anne Peyroche +5 more
TL;DR: This work reports a phenotype related to the DNA damage response that allowed them to isolate four other chaperones of yeast 20S proteasomes, which are named Poc1-Poc4, providing evidence for a remarkable conservation of a pairwise chaperone-assisted proteasome assembly throughout evolution.