Zobrazeno 1 - 10
of 305
pro vyhledávání: '"Hideto, Miyoshi"'
Autor:
Jun-ichi Kishikawa, Moe Ishikawa, Takahiro Masuya, Masatoshi Murai, Yuki Kitazumi, Nicole L. Butler, Takayuki Kato, Blanca Barquera, Hideto Miyoshi
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
The Na+-pumping NADH-ubiquinone oxidoreductase (Na+-NQR) is a unique respiratory enzyme found in many pathogenic bacteria. Here, the authors present high-resolution cryo-EM structures of Na+-NQR from V. cholerae with or without a bound inhibitor.
Externí odkaz:
https://doaj.org/article/9ddb4f055cc94baea25575c6856ebbc2
Autor:
Melanie Radloff, Isam Elamri, Tamara N. Grund, Luca F. Witte, Katharina F. Hohmann, Sayaka Nakagaki, Hojjat G. Goojani, Hamid Nasiri, Hideto Miyoshi, Dirk Bald, Hao Xie, Junshi Sakamoto, Harald Schwalbe, Schara Safarian
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
Abstract Cytochrome bd-type oxidases play a crucial role for survival of pathogenic bacteria during infection and proliferation. This role and the fact that there are no homologues in the mitochondrial respiratory chain qualify cytochrome bd as a pot
Externí odkaz:
https://doaj.org/article/93a47c381cd747e793e88d2862b66fb8
Autor:
Kento Tsukada, Shono Shinki, Akiho Kaneko, Kazuma Murakami, Kazuhiro Irie, Masatoshi Murai, Hideto Miyoshi, Shingo Dan, Kumi Kawaji, Hironori Hayashi, Eiichi N. Kodama, Aki Hori, Emil Salim, Takayuki Kuraishi, Naoya Hirata, Yasunari Kanda, Teigo Asai
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
Combining genome mining and heterologous expression in a genetically tractable host can lead to bioactive natural products discovery and production. Here, the authors employ this strategy for new decalin-containing diterpenoid pyrenes production by e
Externí odkaz:
https://doaj.org/article/b8d5d9bdb0c848689511d663ed7160bb
Autor:
Masatoshi Murai, Hideto Miyoshi
Publikováno v:
Bio-Protocol, Vol 9, Iss 17 (2019)
The architecture of quinone/inhibitor-access channel in proton-translocating NADH-quinone oxidoreductase (respiratory complex I) was modeled by X-ray crystallography and cryo-EM, however, it remains debatable whether the channel model reflects the ph
Externí odkaz:
https://doaj.org/article/26ad391bed1144c78e90fd891a948bf3
Autor:
Yukihiro Asami, Katsuyuki Sakai, Takahiro Masuya, Takenori Yamamoto, Masatoshi Murai, Yufu Unten, Hideto Miyoshi
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 85(12):2368-2377
The mitochondrial machineries presiding over ATP synthesis via oxidative phosphorylation are promising druggable targets. Fusaramin, a 3-acyl tetramic acid isolated from Fusarium concentricum FKI-7550, is an inhibitor of oxidative phosphorylation in
Autor:
Sayo Kodama, Junya Ishizuka, Ito Miyashita, Takaaki Ishii, Takumi Nishiuchi, Hideto Miyoshi, Yasuyuki Kubo
Publikováno v:
PLoS Pathogens, Vol 13, Iss 2, p e1006189 (2017)
Plant infection by pathogenic fungi involves the differentiation of appressoria, specialized infection structures, initiated by fungal sensing and responding to plant surface signals. How plant fungal pathogens control infection-related morphogenesis
Externí odkaz:
https://doaj.org/article/7ee1037cf2924fa48d7858c8056b6c8c
Autor:
Yuki Sano, Tatsuhiko Tosaki, Nicole L. Butler, Takahiro Masuya, Blanca Barquera, H. Tanaka, Hideto Miyoshi, Takeshi Ito, Joel E. Morgan, Masatoshi Murai
Publikováno v:
J Biol Chem
The Na(+)-pumping NADH-ubiquinone (UQ) oxidoreductase (Na(+)-NQR) is present in the respiratory chain of many pathogenic bacteria and is thought to be a promising antibiotic target. Whereas many details of Na(+)-NQR structure and function are known,
Publikováno v:
J Biol Chem
The small molecule IACS-010759 has been reported to potently inhibit the proliferation of glycolysis-deficient hypoxic tumor cells by interfering with the functions of mitochondrial NADH-ubiquinone oxidoreductase (complex I) without exhibiting cytoto
Autor:
Tomoo Shiba, Takahiro Masuya, Daniel Ken Inaoka, Vivek Sharma, Masatoshi Murai, Outi Haapanen, Shinpei Uno, Kyoko Shinzawa-Itoh, Jonathan Lasham, Hideto Miyoshi
Publikováno v:
J Biol Chem
NADH-quinone oxidoreductase (complex I) couples electron transfer from NADH to quinone with proton translocation across the membrane. Quinone reduction is a key step for energy transmission from the site of quinone reduction to the remotely located p
Autor:
Daniel N. Grba, James N. Blaza, Hannah R. Bridges, Ahmed-Noor A. Agip, Zhan Yin, Masatoshi Murai, Hideto Miyoshi, Judy Hirst
Mitochondrial complex I (NADH:ubiquinone oxidoreductase), a crucial enzyme in energy metabolism, captures the redox potential energy from NADH oxidation/ubiquinone reduction to create the proton motive force used to drive ATP synthesis in oxidative p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d83bbc154910aed6724e673f1307b07
https://eprints.whiterose.ac.uk/184520/1/1_s2.0_S0021925822000424_main.pdf
https://eprints.whiterose.ac.uk/184520/1/1_s2.0_S0021925822000424_main.pdf