T
Toshiki Tsurimoto
Researcher at Kyushu University
Publications - 100
Citations - 7609
Toshiki Tsurimoto is an academic researcher from Kyushu University. The author has contributed to research in topics: DNA replication & Replication factor C. The author has an hindex of 42, co-authored 99 publications receiving 7310 citations. Previous affiliations of Toshiki Tsurimoto include Nara Institute of Science and Technology & Osaka University.
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Journal ArticleDOI
Rad18 guides polη to replication stalling sites through physical interaction and PCNA monoubiquitination
Kenji Watanabe,Satoshi Tateishi,Michio Kawasuji,Toshiki Tsurimoto,Hirokazu Inoue,Masaru Yamaizumi +5 more
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 ArticleDOI
Regulation of DNA-replication origins during cell-cycle progression.
Katsuhiko Shirahige,Yuji Hori,Katsuya Shiraishi,Minoru Yamashita,Keiko Takahashi,Chikashi Obuse,Toshiki Tsurimoto,Hiroshi Yoshikawa +7 more
TL;DR: The effects of a DNA-damaging agent, methyl methane sulphonate (MMS), and of mutations in checkpoint genes such as rad53 on the activity of origins and on cell-cycle progression are studied, measured by two-dimensional gel analysis and by fluorescence-activated cell sorting.
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Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target human Cdt1 for proteolysis.
Hideo Nishitani,Nozomi Sugimoto,Vassilis Roukos,Yohsuke Nakanishi,Masafumi Saijo,Chikashi Obuse,Toshiki Tsurimoto,Keiichi I. Nakayama,Keiko Nakayama,Masatoshi Fujita,Zoi Lygerou,Takeharu Nishimoto +11 more
TL;DR: It is shown here that the N‐terminal 100 amino acids of human Cdt1 are recognized for proteolysis by two distinct E3 ubiquitin ligases during S–G2 phases, which are essential for DDB1‐Cul4‐mediated proteolyses and following ultraviolet‐irradiation.
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Sequential initiation of lagging and leading strand synthesis by two different polymerase complexes at the SV40 DNA replication origin.
TL;DR: A model for polymerase switching during initiation of DNA replication is presented and some prokaryotic DNA polymerase complexes can replace the eukaryotic polymerase δ complex.
Journal ArticleDOI
Replication factors required for SV40 DNA replication in vitro. I. DNA structure-specific recognition of a primer-template junction by eukaryotic DNA polymerases and their accessory proteins.
Toshiki Tsurimoto,Bruce Stillman +1 more
TL;DR: Results suggest that the sequential binding of RF-C, PCNA, and pol delta to a primer-template junction might directly account for the initiation of leading strand DNA synthesis at a replication origin.