Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Kano, Suzuki"'
Autor:
Tomohiro Ishizuka1, Kano Suzuki2, Masae Konno1,3, Keisei Shibata1, Yuma Kawasaki1, Hidefumi Akiyama1, Takeshi Murata2,4 t.murata@faculty.chiba-u.jp, Keiichi Inoue1 inoue@issp.u-tokyo.ac.jp
Publikováno v:
Journal of Biological Chemistry. Oct2024, Vol. 300 Issue 10, p1-13. 13p.
Publikováno v:
Seibutsu Butsuri. 63:91-96
Autor:
Abhishek Singharoy, Chris Chipot, Toru Ekimoto, Kano Suzuki, Mitsunori Ikeguchi, Ichiro Yamato, Takeshi Murata
Publikováno v:
Frontiers in Physiology, Vol 10 (2019)
V1-ATPase exemplifies the ubiquitous rotary motor, in which a central shaft DF complex rotates inside a hexagonally arranged catalytic A3B3 complex, powered by the energy from ATP hydrolysis. We have recently reported a number of crystal structures o
Externí odkaz:
https://doaj.org/article/e5583df1bdad4aa188574cf64909c389
Autor:
Kano Suzuki, Kenji Mizutani, Shintaro Maruyama, Kazumi Shimono, Fabiana L. Imai, Eiro Muneyuki, Yoshimi Kakinuma, Yoshiko Ishizuka-Katsura, Mikako Shirouzu, Shigeyuki Yokoyama, Ichiro Yamato, Takeshi Murata
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
V1-ATPases are rotary molecular motors that are powered by ATP hydrolysis. Here, the authors report two of the missing rotary states of this protein complex, and perform biochemical analysis to investigate the binding mode of the nucleotides.
Externí odkaz:
https://doaj.org/article/5851f81ae2544c9da73cb1883a72a8dc
Autor:
Mrinal Shekhar, Chitrak Gupta, Kano Suzuki, Chun Kit Chan, Takeshi Murata, Abhishek Singharoy
Publikováno v:
ACS central science. 8(7)
The mechanism of rotatory catalysis in ATP-hydrolyzing molecular motors remains an unresolved puzzle in biological energy transfer. Notwithstanding the wealth of available biochemical and structural information inferred from years of experiments, kno
The mechanism of rotatory catalysis in ATP-hydrolyzing molecular motors remain an unresolved puzzle in biological energy transfer. Notwith standing the wealth of available biochemical and structural information inferred from years of experiments, kno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::206f3ce63da06890125d3446308cdf4a
https://doi.org/10.1101/2021.12.07.471682
https://doi.org/10.1101/2021.12.07.471682
Autor:
Takeshi Murata, Nobuyasu Koga, Toshihiko Sugiki, Rie Koga, Kano Suzuki, Toshimichi Fujiwara, Naoya Kobayashi, Takahiro Kosugi, Koya Sakuma, Toshio Nagashima, Naohiro Kobayashi
A wide range of de novo protein structure designs have been achieved, but the complexity of naturally occurring protein structures is still far beyond these designs. To expand the diversity and complexity of de novo designed protein structures, we so
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f267d06870edbe50e080cc12b004b1bb
https://doi.org/10.1101/2021.07.14.449347
https://doi.org/10.1101/2021.07.14.449347
Autor:
Kano Suzuki, M. Tamanaha, Tomoaki Nishiyama, K. Yoshimura, Takeshi Murata, Kaoru Ito, Hidetoshi Sakayama, Motoki Tominaga, T. Imi, Takeshi Haraguchi
Cytoplasmic streaming with extremely high velocity (~70 μm s−1) occurs in cells of the characean algae (Chara). Because cytoplasmic streaming is caused by organelle-associated myosin XI sliding along actin filaments, it has been suggested that a m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9c3a3a0c59995eb8e6fdc9e97b223fb6
https://doi.org/10.1101/2021.05.06.442907
https://doi.org/10.1101/2021.05.06.442907
Autor:
Kano Suzuki, María del Carmen Marín, Masae Konno, Reza Bagherzadeh, Takeshi Murata, Keiichi Inoue
Publikováno v:
Journal of Biological Chemistry. 298:101722
DTG/DTS rhodopsin, which was named based on a three-residue motif (DTG or DTS) that is important for its function, is a light-driven proton-pumping microbial rhodopsin using a retinal chromophore. In contrast to other light-driven ion-pumping rhodops
Autor:
Md Jahangir Alam, Satoshi Arai, Shinya Saijo, Kano Suzuki, Kenji Mizutani, Yoshiko Ishizuka-Katsura, Noboru Ohsawa, Takaho Terada, Mikako Shirouzu, Shigeyuki Yokoyama, So Iwata, Yoshimi Kakinuma, Ichiro Yamato, Takeshi Murata
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e74291 (2013)
Vacuolar ATPases (V-ATPases) function as proton pumps in various cellular membrane systems. The hydrophilic V1 portion of the V-ATPase is a rotary motor, in which a central-axis DF complex rotates inside a hexagonally arranged catalytic A3B3 complex
Externí odkaz:
https://doaj.org/article/7ce6aa0c250c47519ec4ac08b05364f9