R
Robert P. P. Fuchs
Researcher at Centre national de la recherche scientifique
Publications - 174
Citations - 10261
Robert P. P. Fuchs is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: DNA & DNA polymerase. The author has an hindex of 55, co-authored 172 publications receiving 9992 citations. Previous affiliations of Robert P. P. Fuchs include University of Strasbourg & Aix-Marseille University.
Papers
More filters
Journal ArticleDOI
The Y-Family of DNA Polymerases
Haruo Ohmori,Errol C. Friedberg,Robert P. P. Fuchs,Myron F. Goodman,Fumio Hanaoka,David C. Hinkle,Thomas A. Kunkel,Christopher W. Lawrence,Zvi Livneh,Takehiko Nohmi,Louise Prakash,Satya Prakash,Takeshi Todo,Graham C. Walker,Zhigang Wang,Roger Woodgate +15 more
TL;DR: The unrooted phylogenetic tree shown in Figure 1 shows the progression of tree-like structures formed over time in the presence of E.coli and shows the relationships between E. Coli and Tournaisian trees.
Journal ArticleDOI
The dinB Gene Encodes a Novel E. coli DNA Polymerase, DNA Pol IV, Involved in Mutagenesis
Jérôme Wagner,Petr Grúz,Su-Ryang Kim,Masami Yamada,Keiko Matsui,Robert P. P. Fuchs,Takehiko Nohmi +6 more
TL;DR: Results indicate that the uncovered DNA polymerase activity may be a common feature of all these homologous proteins within the UmuC-like protein family.
Journal ArticleDOI
Human SLX4 is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases
Samira Fekairi,Sarah Scaglione,Charly Chahwan,Ewan R. Taylor,Agnès Tissier,Stéphane Coulon,Meng-Qiu Dong,Cristian I. Ruse,John R. Yates,Paul Russell,Robert P. P. Fuchs,Clare H. McGowan,Pierre-Henri L. Gaillard +12 more
TL;DR: The identification of Slx4 orthologs in metazoa, including fly MUS312, essential for meiotic recombination, and human BTBD12, an ATM/ATR checkpoint kinase substrate, are reported, suggesting that SLX4 acts as a docking platform for multiple structure-specific endonucleases.
Journal ArticleDOI
Trading places: how do DNA polymerases switch during translesion DNA synthesis?
TL;DR: This review addresses recent advances in the understanding of DNA polymerase switching during TLS in bacteria such as E. coli and in lower and higher eukaryotes.
Journal ArticleDOI
All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis.
TL;DR: It is shown that, depending upon the nature of the DNA damage and its sequence context, the two additional SOS‐inducible DNA polymerases, Pol II (polB) and Pol IV (dinB), are also involved in error‐free and mutagenic translesion synthesis (TLS).