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Masaru Yamaizumi

Researcher at Kumamoto University

Publications -  49
Citations -  3372

Masaru Yamaizumi is an academic researcher from Kumamoto University. The author has contributed to research in topics: Xeroderma pigmentosum & DNA repair. The author has an hindex of 29, co-authored 49 publications receiving 3264 citations. Previous affiliations of Masaru Yamaizumi include Kyoto University.

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Rad18 guides polη to replication stalling sites through physical interaction and PCNA monoubiquitination

TL;DR: It is shown that polη does not form nuclear foci in RAD18−/− cells after UV irradiation, and Rad18 is crucial for recruitment ofPolη to the damaged site through protein–protein interaction and PCNA monoubiquitination.
Journal Article

U.v.-induced nuclear accumulation of p53 is evoked through DNA damage of actively transcribed genes independent of the cell cycle.

TL;DR: Results strongly suggest that u.v.-induced nuclear accumulation of p53 is evoked through DNA damage of actively transcribed genes, which is related to DNA repair capacity.
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Multiple roles of Rev3, the catalytic subunit of polζ in maintaining genome stability in vertebrates

TL;DR: Interestingly, REV3−/− cells showed reduced gene targeting efficiencies and significant increase in the level of chromosomal breaks in the subsequent M phase after IR in the G2 phase, suggesting the involvement of Rev3 in HR‐mediated double‐strand break repair.
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Rad18 Regulates DNA Polymerase κ and Is Required for Recovery from S-Phase Checkpoint-Mediated Arrest

TL;DR: Results indicate that ATR/Chk1 signaling is required for Rad18-mediated PCNA monoubiquitination, and recruitment of Polκ to ubiquitinated PCNA enables lesion bypass and eliminates stalled forks, thereby attenuating the S-phase checkpoint.
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Human Damage-specific DNA-binding Protein p48 CHARACTERIZATION OF XPE MUTATIONS AND REGULATION FOLLOWING UV IRRADIATION

TL;DR: Results indicate that compound heterozygous mutations in DDB2 (p48) lead to a L350P change from one allele and a Asn-349 deletion from the other and they do not affect nuclear localization of p48, implying that p48 limits DDB activity in vivo.