Zobrazeno 1 - 10
of 179
pro vyhledávání: '"Ken YOKOYAMA"'
Autor:
Jun-ichi Kishikawa, Yui Nishida, Atsuki Nakano, Takayuki Kato, Kaoru Mitsuoka, Kei-ichi Okazaki, Ken Yokoyama
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract ATP synthases play a crucial role in energy production by utilizing the proton motive force (pmf) across the membrane to rotate their membrane-embedded rotor c-ring, and thus driving ATP synthesis in the hydrophilic catalytic hexamer. Howeve
Externí odkaz:
https://doaj.org/article/022cd08ce6ee492fb5770ca374c5fabf
Autor:
Christoph Gerle, Chimari Jiko, Atsuki Nakano, Ken Yokoyama, Chai C. Gopalasingam, Hideki Shigematsu, Kazuhiro Abe
Publikováno v:
Pharmacological Research, Vol 209, Iss , Pp 107423- (2024)
Practical and conceptual barriers have kept human F-ATP synthase out of reach as a target for the treatment of human diseases. Although this situation has persisted for decades, it may change in the near future. In this review the principal functiona
Externí odkaz:
https://doaj.org/article/e62c9702b05742ac8c89d6f155c997bb
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-10 (2023)
Abstract F1 domain of ATP synthase is a rotary ATPase complex in which rotation of central γ-subunit proceeds in 120° steps against a surrounding α3β3 fueled by ATP hydrolysis. How the ATP hydrolysis reactions occurring in three catalytic αβ di
Externí odkaz:
https://doaj.org/article/bcb92185cc3d4adb8176a1a345df52b1
Autor:
Ryosuke Shimai, Shohei Ouchi, Tetsuro Miyazaki, Koji Hirabayashi, Hiroshi Abe, Kosuke Yabe, Midori Kakihara, Masaaki Maki, Hiroyuki Isogai, Takeshi Wada, Dai Ozaki, Yuki Yasuda, Fuminori Odagiri, Kazuhisa Takamura, Kenji Yaginuma, Ken Yokoyama, Takashi Tokano, Tohru Minamino
Publikováno v:
International Journal of Emergency Medicine, Vol 16, Iss 1, Pp 1-6 (2023)
Abstract Background Veno-arterial extracorporeal membrane oxygenation (V-A ECMO) requires a large amount of economic and human resources. The presence of bystander cardiopulmonary resuscitation (CPR) was focused on selecting appropriate V-A ECMO cand
Externí odkaz:
https://doaj.org/article/759ca04afcea4d678b663a1fd82cb508
Autor:
Ken Yokoyama
Publikováno v:
Frontiers in Molecular Biosciences, Vol 10 (2023)
V/A-ATPase is a rotary molecular motor protein that produces ATP through the rotation of its central rotor. The soluble part of this protein, the V1 domain, rotates upon ATP hydrolysis. However, the mechanism by which ATP hydrolysis in the V1 domain
Externí odkaz:
https://doaj.org/article/1dd0a0dd5cba444caee4e0e93bebdd00
Autor:
Ryosuke Shimai, Shohei Ouchi, Tetsuro Miyazaki, Koji Hirabayashi, Hiroshi Abe, Kosuke Yabe, Masaaki Maki, Hiroyuki Isogai, Takeshi Wada, Dai Ozaki, Fuminori Odagiri, Makoto Hiki, Kenji Yaginuma, Ken Yokoyama, Takashi Tokano, Tohru Minamino
Publikováno v:
Clinical Case Reports, Vol 9, Iss 9, Pp n/a-n/a (2021)
Abstract We experienced a case of primary percutaneous coronary intervention for ST‐elevation myocardial infarction (STEMI) with coronavirus disease 2019 (COVID‐19) using appropriate infection prevention protocol. However, recanalization was diff
Externí odkaz:
https://doaj.org/article/659807b6098e47ad8c2d491578e602af
Autor:
Jun-ichi Kishikawa, Atsuko Nakanishi, Aya Furuta, Takayuki Kato, Keiichi Namba, Masatada Tamakoshi, Kaoru Mitsuoka, Ken Yokoyama
Publikováno v:
eLife, Vol 9 (2020)
V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V1 domain, with proton flow through the Vo membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dis
Externí odkaz:
https://doaj.org/article/9b8c79b57c2a4057b6a108a7260c05dc
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
H+-ATPases employ a rotary catalytic mechanism to couple ATP synthesis/hydrolysis with proton translocation through the membrane. Here, the authors use high-resolution cryoEM to characterize three rotational states of a bacterial H+-ATPase, providing
Externí odkaz:
https://doaj.org/article/cfecab94ebe5407db9477c180e68a42b
Publikováno v:
Biophysics and Physicobiology, Vol 16 (2019)
Proton-translocating rotary ATPases couple proton influx across the membrane domain and ATP hydrolysis/synthesis in the soluble domain through rotation of the central rotor axis against the surrounding peripheral stator apparatus. It is a significant
Externí odkaz:
https://doaj.org/article/bb4ed790045548efb9da5cf279e8b2cc
Autor:
Jun-Ichi Kishikawa, Yuki Inoue, Makoto Fujikawa, Kenji Nishimura, Atsuko Nakanishi, Tsutomu Tanabe, Hiromi Imamura, Ken Yokoyama
Publikováno v:
PLoS ONE, Vol 13, Iss 1, p e0190213 (2018)
General anesthetics are indispensable for effective clinical care. Although, the mechanism of action of general anesthetics remains controversial, lipid bilayers and proteins have been discussed as their targets. In this study, we focused on the rela
Externí odkaz:
https://doaj.org/article/a0999540e1444d5e9af0e16dc9893230