研究者業績
  1. 研究者検索結果一覧
  2. 金井 好克

金井 好克

カナイ ヨシカツ  (Yoshikatsu Kanai)

基本情報

所属
藤田医科大学 研究推進本部　産官学連携推進センター 特命教授
大阪大学 ヒューマン・メタバース疾患研究拠点（WPI-PRIMe） 特任教授
学位
医学士(1984年3月)
医学博士(1988年3月)
研究者番号
60204533
J-GLOBAL ID
200901003262194571
researchmap会員ID
1000305140
外部リンク

研究キーワード

 6

研究分野

 4

経歴

 10
もっとみる

学歴

 2

受賞

 12
もっとみる

論文

 470
  • Yunlong Sui, Norihiro Okamoto, Namiko Hoshi, Yuta Inoue, Yuna Ku, Misaki Agawa, Hirotaka Nakamura, Haruka Miyazaki, Daisuke Watanabe, Makoto Ooi, Yoshihiko Yano, Ryuichi Ohgaki, Yoshikatsu Kanai, Hui Yang, Yuzo Kodama
    International Immunopharmacology 172 116138-116138 2026年3月  
  • Kou Nishikubo, Ryuichi Ohgaki, Hiroki Okanishi, Minhui Xu, Yoshikatsu Kanai
    Cancer & Metabolism 13(1) 2025年12月2日  
  • Shinichi Sakamoto, Yukio Naya, Junryo Rii, Kazumi Taguchi, Masaaki Fujimura, Yasuhiro Shigeta, Arthit Chairoungdua, Motoi Nishimura, Ken Wakai, Yasutaka Yamada, Xue Zhao, Yusuke Imamura, Sawako Tajima, Natsumi Sato, Chiaki Hosaka, Mizuka Sekine, Takeshi Ueda, Shuzo Hamamoto, Takahiro Yasui, Yoshikatsu Kanai, Koichiro Akakura, Yuzuru Ikehara, Naohiko Anzai, Tomohiko Ichikawa
    Scientific Reports 15(1) 2025年9月26日  査読有り
  • Anzu Nishiwaki, Hiroki Okanishi, Yoshikatsu Kanai, Ryoji Masui
    FEBS Open Bio 2025年9月15日  査読有り
    In Thermus thermophilus, an aerobic Gram‐negative eubacterium used as a model organism, more than half of the phosphorylation sites identified by proteomic analysis are located near the ligand‐binding site, including the active site, of the enzyme in the three‐dimensional structure. We investigated the effect of these phosphorylation events on the activity of six enzymes (three nucleoside monophosphate kinases, isocitrate kinase, malate dehydrogenase and inorganic pyrophosphatase) by introducing phosphomimetic mutations, Glu, into the phosphorylation sites. All phosphomimetic mutants showed severely reduced activity compared with the wild‐type, particularly in the turnover number. The proteins analyzed in this study belong to different families and have various functions. This suggests that there is a widespread mechanism by which phosphorylation of amino acid residues near the active site reduces enzyme activity independent of the protein family and function.
  • Saki Kurinami, Kenji Fukui, Takeshi Murakawa, Seiki Baba, Takashi Kumasaka, Hiroki Okanishi, Yoshikatsu Kanai, Takato Yano, Ryoji Masui
    The Journal of Biochemistry 2025年5月29日  
    Abstract Zinc finger domains are important interaction modules for binding to nucleic acids, proteins, lipids and small molecules. Many small-sized zinc finger proteins are encoded in bacterial genomes, but most of them have not been functionally annotated. We focused on TTHA0897, ZifS, as a small zinc finger protein from the extremely thermophilic eubacterium Thermus thermophilus HB8. In vivo experiments suggested that the cellular function of ZifS is related to the growth transition of T. thermophilus from the lag to the exponential phase under nutritionally limited conditions. In vitro biochemical experiments, including electrophoretic mobility shift assay and pull-down assay, yielded no clues about molecular functions of ZifS. X-ray crystallographic analysis revealed that the dimeric ZifS globally forms a cylinder-like structure, although ZifS dimer has no overall structural similarity to other known zinc finger proteins. The zinc ion-binding manner of ZifS fitted the characteristics of the zinc ribbon fold, which are mostly found in domains from proteins involved in the transcriptional and translational machinery. The crystal structure of ZifS is the first experimental insight into the molecular structure of this protein family, revealing several conserved features that may be functionally relevant.
もっとみる

MISC

 434

書籍等出版物

 41
もっとみる

講演・口頭発表等

 38
もっとみる

所属学協会

 16
もっとみる

共同研究・競争的資金等の研究課題

 51
もっとみる

産業財産権

 68
もっとみる
一覧へ戻る