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Noboru Ohsawa
Researcher at Centre for Life
Publications - 22
Citations - 943
Noboru Ohsawa is an academic researcher from Centre for Life. The author has contributed to research in topics: Protein subunit & ATPase. The author has an hindex of 14, co-authored 22 publications receiving 799 citations.
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Journal ArticleDOI
Crystal structures of the human adiponectin receptors
Hiroaki Tanabe,Yoshifumi Fujii,Miki Okada-Iwabu,Masato Iwabu,Masato Iwabu,Yoshihiro Nakamura,Toshiaki Hosaka,Kanna Motoyama,Mariko Ikeda,Motoaki Wakiyama,Takaho Terada,Noboru Ohsawa,Masakatsu Hato,Satoshi Ogasawara,Tomoya Hino,Takeshi Murata,So Iwata,Kunio Hirata,Yoshiaki Kawano,Masaki Yamamoto,Tomomi Kimura-Someya,Mikako Shirouzu,Toshimasa Yamauchi,Takashi Kadowaki,Shigeyuki Yokoyama +24 more
TL;DR: In this article, the crystal structures of human AdipoR1 and AdipOR2 were reported at 2.9 and 2.4 A resolution, respectively, which represent a novel class of receptor structure.
Journal ArticleDOI
Rotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structures
Satoshi Arai,Shinya Saijo,Kano Suzuki,Kenji Mizutani,Kenji Mizutani,Kenji Mizutani,Yoshimi Kakinuma,Yoshiko Ishizuka-Katsura,Noboru Ohsawa,Takaho Terada,Mikako Shirouzu,Shigeyuki Yokoyama,So Iwata,Ichiro Yamato,Takeshi Murata,Takeshi Murata +15 more
TL;DR: These asymmetric structures represent the first high-resolution view of the rotational mechanism of V1-ATPase from the A3B3 and DF complexes and suggest a binding order in the right-handed rotational orientation in a cooperative manner.
Journal ArticleDOI
Allosteric regulation of γ-secretase activity by a phenylimidazole-type γ-secretase modulator.
Koji Takeo,Shun Tanimura,Takehiro Shinoda,Satoko Osawa,Ivan Krasmirov Zahariev,Naoki Takegami,Yoshiko Ishizuka-Katsura,Naoko Shinya,Shizuka Takagi-Niidome,Aya Tominaga,Noboru Ohsawa,Tomomi Kimura-Someya,Mikako Shirouzu,Satoshi Yokoshima,Shigeyuki Yokoyama,Tohru Fukuyama,Taisuke Tomita,Takeshi Iwatsubo +17 more
TL;DR: A model for the mechanism of action of the phenylimidazole-type GSM in which binding at the luminal side of PS induces a conformational change in the catalytic center of γ-secretase to modulate Aβ production is provided.
Journal ArticleDOI
Structural basis for mutual relief of the Rac guanine nucleotide exchange factor DOCK2 and its partner ELMO1 from their autoinhibited forms.
Kyoko Hanawa-Suetsugu,Mutsuko Kukimoto-Niino,Chiemi Mishima-Tsumagari,Ryogo Akasaka,Noboru Ohsawa,Shun-ichi Sekine,Takuhiro Ito,Naoya Tochio,Seizo Koshiba,Takanori Kigawa,Takaho Terada,Mikako Shirouzu,Akihiko Nishikimi,Takehito Uruno,Tomoya Katakai,Tatsuo Kinashi,Daisuke Kohda,Yoshinori Fukui,Shigeyuki Yokoyama +18 more
TL;DR: The present complex structure reveals the structural basis by which DOCK2 and ELMO1 mutually relieve their autoinhibition for the activation of Rac1 for lymphocyte chemotaxis.
Journal ArticleDOI
The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.
Akihiko Arakawa,Noriko Handa,Noboru Ohsawa,Meiri Shida,Takanori Kigawa,Fumiaki Hayashi,Mikako Shirouzu,Shigeyuki Yokoyama +7 more
TL;DR: BAG5 can function as the nucleotide exchange factor of Hsp70 for the enhancement of protein refolding and reduce the affinity of the NBD for ADP.