Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Yoshiko Ishizuka-Katsura"'
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:
Suhaila Rahman, Ichiro Yamato, Shinya Saijo, Kenji Mizutani, Yoshiko Ishizuka-Katsura, Noboru Ohsawa, Takaho Terada, Mikako Shirouzu, Shigeyuki Yokoyama, So Iwata, Takeshi Murata
Publikováno v:
PLoS ONE, Vol 8, Iss 2, p e55704 (2013)
Peripheral stalk subunits of eukaryotic or mammalian vacuolar ATPases (V-ATPases) play key roles in regulating its assembly and disassembly. In a previous study, we purified several subunits and their isoforms of the peripheral stalk region of Homo s
Externí odkaz:
https://doaj.org/article/c540dc9b071547f798fa61cc56b570e2
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
Autor:
Toshiaki Hosaka, Kazushige Katsura, Yoshiko Ishizuka-Katsura, Kazuharu Hanada, Kaori Ito, Yuri Tomabechi, Mio Inoue, Ryogo Akasaka, Chie Takemoto, Mikako Shirouzu
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 18; Pages: 10399
Genetically encoded caged amino acids can be used to control the dynamics of protein activities and cellular localization in response to external cues. In the present study, we revealed the structural basis for the recognition of O-(2-nitrobenzyl)-L-
Autor:
Masaki Yamamoto, Keitaro Yamashita, Kentaro Ihara, So Iwata, Eriko Nango, Yoshiko Ishizuka-Katsura, Kensuke Tono, Takanori Nakane, Mikako Shirouzu, Toshiaki Hosaka, Kunio Hirata, Rie Tanaka, Osamu Nureki, Tomomi Kimura-Someya, M. Sugahara, Masakatsu Hato, Tomoyuki Tanaka
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-12 (2020)
Scientific Reports
Scientific Reports
In meso crystallization of membrane proteins relies on the use of lipids capable of forming a lipidic cubic phase (LCP). However, almost all previous crystallization trials have used monoacylglycerols, with 1-(cis-9-octadecanoyl)-rac-glycerol (MO) be
Autor:
Takaho Terada, Fumitaka Oyama, Haruko Miyazaki, Shun-ichi Sekine, Shisako Shoji, Nobuyuki Nukina, Mikako Shirouzu, Hideaki Shimizu, Yoshiko Ishizuka-Katsura, Shigeyuki Yokoyama, Asako Tosaki, Noboru Ohsawa
Publikováno v:
The Journal of Biological Chemistry
Voltage-gated sodium channels (VGSCs) are transmembrane proteins required for the generation of action potentials in excitable cells and essential for propagating electrical impulses along nerve cells. VGSCs are complexes of a pore-forming α subunit
Autor:
Shigeyuki Yokoyama, Mikako Shirouzu, Masateru Okazaki, Mikiko Sodeoka, Yoshiko Ishizuka-Katsura, Toshiaki Hosaka, Kosuke Dodo, Kaori Ito, Tomomi Kimura-Someya
Publikováno v:
Protein Science. 26:1749-1758
Voltage-dependent anion channel 1 (VDAC1), which is located in the outer mitochondrial membrane, plays important roles in various cellular processes. For example, oligomerization of VDAC1 is involved in the release of cytochrome c to the cytoplasm, l
Autor:
Takayuki Uchihashi, Ichiro Yamato, Fabiana L. Imai, Yoshiko Ishizuka-Katsura, Takeshi Murata, Mikako Shirouzu, Motonori Imamura, Kano Suzuki, Hideyuki Matsunami, Kenji Mizutani, Hikaru Sasaki, Shintaro Maruyama, Tomomi Kimura-Someya, Toshio Ando, Yasuko Saito
Publikováno v:
Science Advances. 5
V1-ATPase is an ATP-driven rotary motor that is composed of a ring-shaped A3B3 complex and a central DF shaft. The nucleotide-free A3B3 complex of Enterococcus hirae, composed of three identical A1B1 heterodimers, showed a unique asymmetrical structu
Autor:
Shintaro, Maruyama, Kano, Suzuki, Motonori, Imamura, Hikaru, Sasaki, Hideyuki, Matsunami, Kenji, Mizutani, Yasuko, Saito, Fabiana L, Imai, Yoshiko, Ishizuka-Katsura, Tomomi, Kimura-Someya, Mikako, Shirouzu, Takayuki, Uchihashi, Toshio, Ando, Ichiro, Yamato, Takeshi, Murata
Publikováno v:
Science Advances
The V1-ATPase motor forms metastable asymmetrical structures that suggest the basis for the cooperative transition mechanism.
V1-ATPase is an ATP-driven rotary motor that is composed of a ring-shaped A3B3 complex and a central DF shaft. The nucl
V1-ATPase is an ATP-driven rotary motor that is composed of a ring-shaped A3B3 complex and a central DF shaft. The nucl
Autor:
Toshiaki, Hosaka, Masateru, Okazaki, Tomomi, Kimura-Someya, Yoshiko, Ishizuka-Katsura, Kaori, Ito, Shigeyuki, Yokoyama, Kosuke, Dodo, Mikiko, Sodeoka, Mikako, Shirouzu
Publikováno v:
Protein science : a publication of the Protein Society. 26(9)
Voltage‐dependent anion channel 1 (VDAC1), which is located in the outer mitochondrial membrane, plays important roles in various cellular processes. For example, oligomerization of VDAC1 is involved in the release of cytochrome c to the cytoplasm,