Zobrazeno 1 - 10
of 75
pro vyhledávání: '"Takeshi HIROMOTO"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Protein crystals are generally fragile and sensitive to subtle changes such as pH, ionic strength, and/or temperature in their crystallization mother liquor. Here, using T4 phage lysozyme as a model protein, the three-dimensional rigidification of pr
Externí odkaz:
https://doaj.org/article/3bea86c3731d41ef9f32ada0c29561fa
Autor:
Katsushiro Miyamoto, Hiroaki Kawano, Naoko Okai, Takeshi Hiromoto, Nao Miyano, Koji Tomoo, Takahiro Tsuchiya, Jun Komano, Tomotaka Tanabe, Tatsuya Funahashi, Hiroshi Tsujibo
Publikováno v:
Marine Drugs, Vol 19, Iss 12, p 710 (2021)
Vibrio vulnificus is a Gram-negative pathogenic bacterium that causes serious infections in humans and requires iron for growth. A clinical isolate, V. vulnificus M2799, secretes a catecholate siderophore, vulnibactin, that captures ferric ions from
Externí odkaz:
https://doaj.org/article/eeff6bc05c7d4f84bb65b5c2fb17d726
Autor:
Kentaro Kumoi, Tadashi Satoh, Kazuyoshi Murata, Takeshi Hiromoto, Tsunehiro Mizushima, Yukiko Kamiya, Masanori Noda, Susumu Uchiyama, Hirokazu Yagi, Koichi Kato
Publikováno v:
PLoS ONE, Vol 8, Iss 3, p e60294 (2013)
Assembly of the eukaryotic 20S proteasome is an ordered process involving several proteins operating as proteasome assembly factors including PAC1-PAC2 but archaeal 20S proteasome subunits can spontaneously assemble into an active cylindrical archite
Externí odkaz:
https://doaj.org/article/e35548a49f6b4841a655bc0e46d5b78f
Autor:
Taro, Tamada, Takeshi, Hiromoto
[NiFe]-ヒドロゲナーゼはNi-Fe活性部位、Mg中心、および鉄-硫黄クラスターを有し、水素の合成・分解を両方向に触媒できる。Desulfovibrio vulgaris Miyazaki F株由来[NiFe]-ヒドロゲナーゼのNi-Fe活性
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::d067e6cd483c79adb3d1ea85df6f0f71
https://repo.qst.go.jp/records/86315
https://repo.qst.go.jp/records/86315
Publikováno v:
Topics in Catalysis. 64:622-630
X-ray crystallography is the most powerful tool for obtaining structural information about protein molecules, affording accurate and precise positions for all of the atoms in the protein except for hydrogen. However, hydrogen species play crucial rol
Publikováno v:
Topics in Catalysis. 64:622-630
X-ray crystallography is the most powerful tool for obtaining structural information about protein molecules, affording accurate and precise positions for all of the atoms in the protein except for hydrogen. However, hydrogen species play crucial rol
Autor:
Toshiaki Nakano, Ken Akamatsu, Masataka Tsuda, Ayane Tujimoto, Ryoichi Hirayama, Takeshi Hiromoto, Taro Tamada, Hiroshi Ide, Naoya Shikazono
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Significance DNA damage causes loss of or alterations in genetic information, resulting in cell death or mutations. Ionizing radiations produce local, multiple DNA damage sites called clustered DNA damage. In this study, a complete protocol was estab
Autor:
Hiromoto, Takeshi, Nishikawa, Koji, Inoue, Seiya, Matsuura, Hiroaki, Hirano, Yu, Kurihara, Kazuo, Kusaka, Katsuhiro, Cuneo, Matthew, Coates, Leighton, Tamada, Taro, Higuchi, Yoshiki, Takeshi, Hiromoto, Yuu, Hirano, Kazuo, Kurihara, Taro, Tamada
Publikováno v:
Acta Crystallographica Section D. :946-953
A membrane-bound hydrogenase from Desulfovibrio vulgaris Miyazaki F is a metalloenzyme that contains a binuclear Ni–Fe complex in its active site and mainly catalyzes the oxidation of molecular hydrogen to generate a proton gradient in the bacteriu
Autor:
Tomitake Tsukihara, Takeshi Hiromoto, Ai Sasaki, Kyoko Shinzawa-Itoh, Kazumasa Muramoto, Atsuhiro Shimada, Yuki Etoh, Shinya Yoshikawa, Rika Kitoh-Fujisawa, Eiki Yamashita
Publikováno v:
Journal of Biological Chemistry. 295:5818-5833
Cytochrome c oxidase (CcO) reduces O2 to water, coupled with a proton-pumping process. The structure of the O2-reduction site of CcO contains two reducing equivalents, Fea32+ and CuB1+, and suggests that a peroxide-bound state (Fea33+–O−–O−
研究用原子炉JRR-3は約10年の運転停止期間を終え、2021年2月に再稼働を果たし、7月から供用運転を再開した。量研はJRR-3炉室に2台の生体高分子用中性子単結晶回折装置(BIX-3,4)を保有し
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::c5f20383194b589831246298e02b89e5
https://repo.qst.go.jp/records/83864
https://repo.qst.go.jp/records/83864