Zobrazeno 1 - 10
of 95
pro vyhledávání: '"Toshiro Oda"'
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 11 (2023)
The dynamic assembly of actin is controlled by the hydrolysis of ATP, bound to the center of the molecule. Upon polymerization, actin undergoes a conformational change from the monomeric G-form to the fibrous F-form, which is associated with the flip
Externí odkaz:
https://doaj.org/article/6da4a691afc74d179e34ce18633ac0b1
Autor:
Kotaro Tanaka, Shuichi Takeda, Kaoru Mitsuoka, Toshiro Oda, Chieko Kimura-Sakiyama, Yuichiro Maéda, Akihiro Narita
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Cofilin is a small actin-binding protein that accelerates actin turnover by disassembling actin filaments. Here the authors present the 3.8 Å cryo-EM structure of a cofilin-decorated actin filament and discuss mechanistic implications.
Externí odkaz:
https://doaj.org/article/fdefc781b9034aa19dc5ebb979aa6664
Autor:
Mizuki Matsuzaki, Ikuko Fujiwara, Sae Kashima, Tomoharu Matsumoto, Toshiro Oda, Masahito Hayashi, Kayo Maeda, Kingo Takiguchi, Yuichiro Maéda, Akihiro Narita
Publikováno v:
Biomolecules, Vol 10, Iss 5, p 736 (2020)
Depolymerization and polymerization of the actin filament are indispensable in eukaryotes. The DNase I binding loop (D-loop), which forms part of the interface between the subunits in the actin filament, is an intrinsically disordered loop with a lar
Externí odkaz:
https://doaj.org/article/fc59643c7e0c43719903a5a493ade663
Autor:
Naoya Masumori, Shintaro Miyamoto, Taiji Tsukamoto, Seiji Furuya, Akihiko Iwasawa, Takashi Sato, Naoki Itoh, Akihiko Shibuya, Toshiro Oda
Publikováno v:
Advances in Urology, Vol 2011 (2011)
Objectives. To prospectively examine the efficacy and safety of propiverine hydrochloride in patients with overactive bladder (OAB) symptoms who poorly responded to previous treatment with solifenacin, tolterodine or imidafenacin. Methods. Patients a
Externí odkaz:
https://doaj.org/article/de3f18a5bddc48d9a67bebe441bdee9b
Autor:
Yusuke Kanematsu, Akihiro Narita, Toshiro Oda, Ryotaro Koike, Motonori Ota, Yu Takano, Kei Moritsugu, Ikuko Fujiwara, Kotaro Tanaka, Hideyuki Komatsu, Takayuki Nagae, Nobuhisa Watanabe, Mitsusada Iwasa, Yuichiro Maéda, Shuichi Takeda
Publikováno v:
Proceedings of the National Academy of Sciences. 119
The major cytoskeleton protein actin undergoes cyclic transitions between the monomeric G-form and the filamentous F-form, which drive organelle transport and cell motility. This mechanical work is driven by the ATPase activity at the catalytic site
Autor:
Toshiro Oda, Yuichiro Maéda
Publikováno v:
Biophysical Reviews
Prof. Fumio Oosawa passed away in Nagoya on March 4, 2019, at the age of 96. As two of his former students we, like a great many scientists both in Japan and around the world, were much inspired and influenced by him. We have, at the request of the j
Publikováno v:
Journal of molecular biology. 431(17)
Information on the structural polymorphism of a protein is essential to understand the mechanisms of how it functions at an atomic level. Numerous studies on actin have accumulated substantial amounts of information about its polymorphism, and there
Autor:
Kenji Nakajima, Tatsuhito Matsuo, Toshiaki Arata, Tatsuya Kikuchi, Toshiro Oda, Seiko Ohira-Kawamura, Satoru Fujiwara
Publikováno v:
Biochemistry and Biophysics Reports
Hydration water is essential for a protein to perform its biological function properly. In this study, the dynamics of hydration water around F-actin and myosin subfragment-1 (S1), which are the partner proteins playing a major role in various cellul
Autor:
Masahito Hayashi, Tomoharu Matsumoto, Yuichiro Maéda, Ikuko Fujiwara, Akihiro Narita, Toshiro Oda, Kayo Maeda, Sae Kashima, Mizuki Matsuzaki, Kingo Takiguchi
Publikováno v:
Biomolecules
Biomolecules, Vol 10, Iss 736, p 736 (2020)
Volume 10
Issue 5
Biomolecules, Vol 10, Iss 736, p 736 (2020)
Volume 10
Issue 5
Depolymerization and polymerization of the actin filament are indispensable in eukaryotes. The DNase I binding loop (D-loop), which forms part of the interface between the subunits in the actin filament, is an intrinsically disordered loop with a lar