O
Osamu Koiwai
Researcher at Tokyo University of Science
Publications - 73
Citations - 2292
Osamu Koiwai is an academic researcher from Tokyo University of Science. The author has contributed to research in topics: DNA polymerase & Processivity. The author has an hindex of 26, co-authored 73 publications receiving 2211 citations. Previous affiliations of Osamu Koiwai include Nagoya University & Kobe Gakuin University.
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Journal ArticleDOI
A Biochemically Defined System for Mammalian Nonhomologous DNA End Joining
Yunmei Ma,Haihui Lu,Brigette Tippin,Myron F. Goodman,Noriko Shimazaki,Osamu Koiwai,Chih-Lin Hsieh,Klaus Schwarz,Michael R. Lieber +8 more
TL;DR: The NHEJ reactions have been reconstituted in vitro by using purified Ku, DNA-PK(cs), Artemis, and XRCC4:DNA ligase IV proteins to join incompatible ends to yield diverse junctions to lead to an iterative strand-processing model for the steps of N HEJ.
Journal ArticleDOI
Molecular cloning of a cDNA of a camptothecin-resistant human DNA topoisomerase I and identification of mutation sites
Hiroomi Tamura,Chie Kohchi,Ryutaro Yamada,Tomotake Ikeda,Osamu Koiwai,Eric B. Patterson,Jack D. Keene,Kosuke Okada,Eigil Kjeldsen,Ken Nishikawa,Toshiwo Andoh +10 more
TL;DR: Results indicate that either or both of the two amino acid changes identified in the mutant enzyme is responsible for the resistance to CPT.
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A Single Amino Acid Alteration in Cytoplasmic Domain Determines IL-2 Promoter Activation by Ligation of CD28 but Not Inducible Costimulator (ICOS)
Yohsuke Harada,Daisuke Ohgai,Ryosuke Watanabe,Kazuhiro Okano,Osamu Koiwai,Kazunari Tanabe,Hiroshi Toma,Amnon Altman,Ryo Abe +8 more
TL;DR: In this article, the authors showed that the difference of a single amino acid, which affects Grb2 binding ability, may define a functional difference between the CD28 and ICOS-mediated costimulatory signals.
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Over‐expression of human DNA polymerase lambda in E. coli and characterization of the recombinant enzyme
TL;DR: This work has identified a new member of the family X of DNA polymerases in eukaryotic cells that contains a nuclear localization signal, a BRCA1‐C terminal domain, a proline‐rich region, helix‐hairpin‐helix (HhH), and pol X motifs.
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The UL34 gene product of herpes simplex virus type 2 is a tail-anchored type II membrane protein that is significant for virus envelopment.
C Shiba,C Shiba,Tohru Daikoku,Fumi Goshima,Hiroki Takakuwa,Yohei Yamauchi,Osamu Koiwai,Yukihiro Nishiyama +7 more
TL;DR: The hypothesis that the UL34 protein is inserted into the viral envelope as a tail-anchored type II membrane protein and is significant for virus envelopment is strongly supported.