J
J. Pablo Radicella
Researcher at Université Paris-Saclay
Publications - 73
Citations - 4783
J. Pablo Radicella is an academic researcher from Université Paris-Saclay. The author has contributed to research in topics: DNA repair & Base excision repair. The author has an hindex of 33, co-authored 68 publications receiving 4452 citations. Previous affiliations of J. Pablo Radicella include Erasmus University Rotterdam & 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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The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis.
Serge Boiteux,J. Pablo Radicella +1 more
TL;DR: Results point to 8-OH-G as an endogenous source of mutations in eukaryotes and to its likely involvement in the process of carcinogenesis and to a possible role in the prevention of cancer.
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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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Excision of oxidatively damaged DNA bases by the human α-hOgg1 protein and the polymorphic α-hOgg1(Ser326Cys) protein which is frequently found in human populations
TL;DR: Investigation of the substrate specificity of the major nuclear form of the human Ogg1 protein, referred as α-hOgg1, for excision of damaged bases from DNA exposed to γ-irradiation shows that it excises 8hydroxyguanine (8-OH-Gua) and 2,6-diamino-4-hydroxy5-formamidopyrimidine (FapyGua).