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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Journal ArticleDOI
COP9 Signalosome- and 26S Proteasome-dependent Regulation of SCFTIR1 Accumulation in Arabidopsis
Johannes Stuttmann,Esther Lechner,Raphael Guerois,Jane E. Parker,Laurent Nussaume,Pascal Genschik,Laurent D. Noël +6 more
TL;DR: Results are consistent with CSN-dependent protection of Arabidopsis CRLs from autocatalytic degradation, as observed in other eukaryotes, and provide evidence for antagonist roles of the CSN and 26S proteasome in modulating accumulation of the plant CRL SCFTIR1.
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Detection of a tandem BRCT in Nbs1 and Xrs2 with functional implications in the DNA damage response
TL;DR: The structure-based conservation analysis of the tandem BRCT in Nbs1 supports its function as a phosphoserine binding domain and the 5 bp deletion observed in 95% of NBS patients cleaves the tandem at the linker region while preserving the structural integrity of each BRCT domain in the resulting truncated gene products.
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Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly
Marie-Bénédicte Barrault,N. Richet,Chloe Godard,Brice Murciano,Benoît Le Tallec,Erwann Rousseau,Pierre Legrand,Jean-Baptiste Charbonnier,Marie-Hélène Le Du,Raphael Guerois,Françoise Ochsenbein,Anne Peyroche +11 more
TL;DR: It is shown that in both yeast and mammals, Hsm3 actually directly binds the AAA domain of Rpt2 and unexpectedly acts as an essential matchmaker for the Rpt1-Rpt1–Rpt2-Rpn1 assembly by bridging both Rpt 1 and Rpt 2.
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InterEvol database: exploring the structure and evolution of protein complex interfaces
TL;DR: The InterEvol database was designed for exploring 3D structures of homologous interfaces of protein complexes providing essential snapshots for studying interfaces evolution and provides tools to retrieve and visualize these structures.
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Structural characterization of Set1 RNA recognition motifs and their role in histone H3 lysine 4 methylation.
Lionel Trésaugues,Pierre-Marie Dehé,Raphael Guerois,Alfonso Rodríguez-Gil,Isabelle Varlet,Philippe Salah,Mercè Pamblanco,Pierre Luciano,Sophie Quevillon-Cheruel,Julie Sollier,Nicolas Leulliot,Joël Couprie,Vicente Tordera,Sophie Zinn-Justin,Sebastián Chávez,Herman van Tilbeurgh,Vincent Géli +16 more
TL;DR: The results suggest that Set1 RRMs bind RNA, but Set1 RNA-binding activity is not linked to H3K4 methylation.