S
Shin Sato
Researcher at Centre for Life
Publications - 23
Citations - 533
Shin Sato is an academic researcher from Centre for Life. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 9, co-authored 18 publications receiving 405 citations.
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Journal ArticleDOI
Structurally Designed trans-2-Phenylcyclopropylamine Derivatives Potently Inhibit Histone Demethylase LSD1/KDM1,,§
TL;DR: Several candidate compounds to inhibit LSD1 are designed and synthesized, based on the structures of LSD1 and monoamine oxidase B (MAO-B), in complex with an antidepressant tranylcypromine (2-PCPA) derivative, potential pharmaceutical candidates for cancer or latent virus infection.
Journal ArticleDOI
Crystallographic study of a site-specifically cross-linked protein complex with a genetically incorporated photoreactive amino acid
Shin Sato,Shinya Mimasu,Aya Sato,Nobumasa Hino,Kensaku Sakamoto,Takashi Umehara,Shigeyuki Yokoyama +6 more
TL;DR: The crystal structure of the cross-linked complex of the liver oncoprotein gankyrin and the C-terminal domain of S6 proteasomal protein (S6C) was determined, showing the high selectivity of formation of cross-links by pBpa and exhibiting little structural distortion from the native complex structure.
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Discovery of Novel Spiroindoline Derivatives as Selective Tankyrase Inhibitors.
Fumiyuki Shirai,Takeshi Tsumura,Yoko Yashiroda,Hitomi Yuki,Hideaki Niwa,Shin Sato,Tsubasa Chikada,Yasuko Koda,Kenichi Washizuka,Nobuko Yoshimoto,Masako Abe,Tetsuo Onuki,Yui Mazaki,Chizuko Hirama,Takehiro Fukami,Hirofumi Watanabe,Teruki Honma,Takashi Umehara,Mikako Shirouzu,Masayuki Okue,Yuko Kano,Takashi Watanabe,Kouichi Kitamura,Eiki Shitara,Yukiko Muramatsu,Haruka Yoshida,Anna Mizutani,Hiroyuki Seimiya,Minoru Yoshida,Hiroo Koyama +29 more
TL;DR: Spiroindoline derivative 40c (RK-287107) was discovered as a potent TNKS/TNKS2 inhibitor with >7000-fold selectivity against the PARP1 enzyme, which inhibits WNT-responsive TCF reporter activity and proliferation of human colorectal cancer cell line COLO-320DM.
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Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain.
Naoya Tochio,Takashi Umehara,Yoshiko Munemasa,Toru Suzuki,Shin Sato,Kengo Tsuda,Seizo Koshiba,Takanori Kigawa,Ryozo Nagai,Shigeyuki Yokoyama +9 more
TL;DR: It is reported that the LRR domain of ANP32B possesses histone chaperone activity and forms a curved structure with a parallel beta-sheet on the concave side and mostly helical elements on the convex side, which provides a structural framework for understanding the functional mechanisms of acidic hist one chaperones.
Journal ArticleDOI
Multiple site-specific installations of Nε-monomethyl-L-lysine into histone proteins by cell-based and cell-free protein synthesis.
Tatsuo Yanagisawa,Mihoko Takahashi,Takahito Mukai,Shin Sato,Masatoshi Wakamori,Mikako Shirouzu,Kensaku Sakamoto,Takashi Umehara,Shigeyuki Yokoyama +8 more
TL;DR: This method enables the installation of authentic Nε‐monomethyllysines at multiple positions within a protein for large‐scale production.