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Antonio E. Vidal
Researcher at National Institutes of Health
Publications - 10
Citations - 1486
Antonio E. Vidal is an academic researcher from National Institutes of Health. The author has contributed to research in topics: DNA polymerase & AP endonuclease. The author has an hindex of 8, co-authored 8 publications receiving 1448 citations. Previous affiliations of Antonio E. Vidal include French Alternative Energies and Atomic Energy Commission.
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Journal ArticleDOI
XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein–protein interactions
TL;DR: It is reported here that XRCC1, another essential protein involved in the maintenance of genome stability, physically interacts with APE1 and stimulates its enzymatic activities, extending the coordinating role of XR CC1 to the initial step of the repair of DNA abasic sites.
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Mechanism of stimulation of the DNA glycosylase activity of hOGG1 by the major human AP endonuclease: bypass of the AP lyase activity step
TL;DR: In vitro, in the presence of HAP1, the BER of 8-oxoG residues can be highly efficient by bypassing the AP lyase activity of hOGG1 and thus excluding a potentially rate limiting step.
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Role of XRCC1 in the Coordination and Stimulation of Oxidative DNA Damage Repair Initiated by the DNA Glycosylase hOGG1
Stéphanie Marsin,Antonio E. Vidal,Marguerite Sossou,Josiane Ménissier-de Murcia,Florence Le Page,Serge Boiteux,Gilbert de Murcia,J. Pablo Radicella +7 more
TL;DR: A highly coordinated mechanism by which XRCC1, through its multiple protein-protein interactions, extends its orchestrating role from the base excision step to the resealing of the repaired DNA strand is unveiled.
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Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells.
Patricia Kannouche,Antonio R. Fernández de Henestrosa,Antonio R. Fernández de Henestrosa,Barry Coull,Antonio E. Vidal,Colin Gray,Daniel Zicha,Roger Woodgate,Alan R. Lehmann +8 more
TL;DR: It is shown that DNA polymerase ι (polι), like polη, associates with the replication machinery and accumulates at stalled replication forks following DNA‐damaging treatment, and that the C‐terminal 224 amino acids of polι are sufficient for both the interaction withpolη and accumulation in replication foci.
Journal ArticleDOI
Controlling the subcellular localization of DNA polymerases ι and η via interactions with ubiquitin
Brian S. Plosky,Antonio E. Vidal,Antonio R. Fernández de Henestrosa,Mary P. McLenigan,John P. McDonald,Samantha Mead,Roger Woodgate +6 more
TL;DR: Y‐family DNA polymerases have spacious active sites that can accommodate a wide variety of geometric distortions, and one such mechanism employed by human cells relies on a specific and direct interaction between DNA polymerase ι and η with ubiquitin (Ub).