T
Tsutomu Kamiyama
Researcher at Hoffmann-La Roche
Publications - 28
Citations - 533
Tsutomu Kamiyama is an academic researcher from Hoffmann-La Roche. The author has contributed to research in topics: Fibrinogen receptor & DNA gyrase. The author has an hindex of 15, co-authored 28 publications receiving 512 citations.
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Journal ArticleDOI
The Structure of the Polycyclic Nonadecapeptide Ro 09-0198†
Horst Kessler,S. Steuernagel,Martin Will,Günther Jung,Roland Kellner,Dieter Gillessen,Tsutomu Kamiyama +6 more
TL;DR: In this article, the authors used NMR spectroscopy at highest field and automated Edman degradation yielded a complete determination of the connectivity pattern of the peptide antibiotic Ro 09-0198, which exhibits an interesting separation of amino acids with hydrophilic and hydrophobic side chains.
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Complete Sequence Determination and Localisation of One Imino and Three Sulfide Bridges of the Nonadecapeptide Ro 09–0198 by Homonuclear 2D-NMR Spectroscopy. The DQF-RELAYED-NOESY-Experiment†
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Biological characterization of cyclothialidine, a new DNA gyrase inhibitor.
Naoki Nakada,Hisao Shimada,Takahiro Hirata,Yuko Aoki,Tsutomu Kamiyama,J. Watanabe,Mikio Arisawa +6 more
TL;DR: Results provide a basis for cyclothialidine to be a lead structure for novel antibacterial agents with DNA gyrase inhibitory activities and suggest that it can enter the cells of Eubacterium and exert antibacterial activity through interference with the DNA g Kyrase within the cells, although its penetration into most bacterial cells appears to be poor.
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Sulfobacins A and B, Novel von Willebrand Factor Receptor Antagonists: I. Production, Isolation, Characterization and Biological Activities
Tsutomu Kamiyama,Takayuki Umino,Tomoko Satoh,Sayoko Sawairi,Michiko Shirane,Shoichi Ohshima,Kazuteru Yokose +6 more
TL;DR: The physico-chemical properties of the sulfobacins indicate that their structures are completely different from that of aurintricarboxylic acid, the one known vWF receptor antagonist.
Journal ArticleDOI
Tetrafibricin, a novel fibrinogen receptor antagonist. I: Taxonomy, fermentation, isolation, characterization and biological activities
Tsutomu Kamiyama,Takayuki Umino,Noriko Fujisaki,Kumiko Fujimori,Tomoko Satoh,Yuko Yamashita,Shoichi Ohshima,J. Watanabe,Kazuteru Yokose +8 more
TL;DR: Tetrafibricin strongly inhibited the binding of fibrinogen to its receptors with an IC50 of 46 nM and inhibited ADP-, collagen-, and thrombin-induced aggregation of human platelets with IC50s of 5.6, 11.0 and 7.6 microM, respectively.