Zobrazeno 1 - 10
of 155
pro vyhledávání: '"Masatoshi, Murai"'
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:
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4c4379feb041d9e7162a80050673258
http://hdl.handle.net/2433/266256
http://hdl.handle.net/2433/266256
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,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f90a538d2d0a4ed72f9c314a3a37a1d
https://doi.org/10.1074/jbc.ra120.014229
https://doi.org/10.1074/jbc.ra120.014229
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef3c77ef52e406d09d23c5b5b88e1f52
https://doi.org/10.1074/jbc.ra120.013366
https://doi.org/10.1074/jbc.ra120.013366
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef7f4cd6b1302631ad5ca73710102396
https://doi.org/10.1074/jbc.ra119.012347
https://doi.org/10.1074/jbc.ra119.012347
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
Autor:
Kazunari Sakai, Katsuyuki Sakai, Aoi Kimishima, Satoshi Ōmura, Kazuro Shiomi, Kenichi Nonaka, Yukihiro Asami, Takumi Chinen, Yufu Unten, Hideto Miyoshi, Masato Iwatsuki, Masatoshi Murai, Takeo Usui
Publikováno v:
Journal of Industrial Microbiology and Biotechnology. 48
Two new tetramic acid derivatives, traminines A (1) and B (2), were isolated from a culture broth of Fusarium concentricum FKI-7550 by bioassay-guided fractionation using multidrug-sensitive Saccharomyces cerevisiae 12geneΔ0HSR-iERG6. The chemical s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f3bd1ce64f7f2d367c4ff95ef77796c
https://doi.org/10.1093/jimb/kuab051
https://doi.org/10.1093/jimb/kuab051
Publikováno v:
Journal of Biological Chemistry. 294:6550-6561
Site-specific suppressors of superoxide production (named S1QELs) in the quinone-reaction site in mitochondrial respiratory complex I during reverse electron transfer have been previously reported; however, their mechanism of action remains elusive.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::359b35e75539fe5284f8a3585d2a318d
https://doi.org/10.1074/jbc.ra119.007687
https://doi.org/10.1074/jbc.ra119.007687