Your browser doesn't support javascript.
loading
Structural and mutational analysis of Trypanosoma brucei prostaglandin H2 reductase provides insight into the catalytic mechanism of aldo-ketoreductases.
Kilunga, Kubata Bruno; Inoue, Tsuyoshi; Okano, Yousuke; Kabututu, Zakayi; Martin, Samuel K; Lazarus, Michael; Duszenko, Michael; Sumii, Yuichi; Kusakari, Yukiko; Matsumura, Hiroyoshi; Kai, Yasushi; Sugiyama, Shigeru; Inaka, Kouji; Inui, Takashi; Urade, Yoshihiro.
Affiliation
  • Kilunga KB; Department of Molecular Behavioral Biology, Osaka Bioscience Institute, 6-2-4 Furuedai, Suita, Osaka 565-0874, Japan. bkubata@nairobi.mimcom.net
J Biol Chem ; 280(28): 26371-82, 2005 Jul 15.
Article in En | MEDLINE | ID: mdl-15845552
Search on Google
Database: MEDLINE Main subject: Oxidoreductases / Trypanosoma brucei brucei / Hydroxyprostaglandin Dehydrogenases / Prostaglandin H2 Language: En Journal: J Biol Chem Year: 2005 Type: Article Affiliation country: Japan
Search on Google
Database: MEDLINE Main subject: Oxidoreductases / Trypanosoma brucei brucei / Hydroxyprostaglandin Dehydrogenases / Prostaglandin H2 Language: En Journal: J Biol Chem Year: 2005 Type: Article Affiliation country: Japan