Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Yayoi Kurokawa"'
Autor:
Masaya Nagao, Hideya Fukuzawa, Tokuji Tsuji, Yayoi Kurokawa, Jacques Pouysségur, Taiho Kambe, Johanna Chiche, Hiroshi Sato
Publikováno v:
Journal of Biological Chemistry. 292:2159-2173
Zinc-requiring ectoenzymes, including both secreted and membrane-bound enzymes, are considered to capture zinc in their active site for their activation in the early secretory pathway. This idea has been confirmed by our studies conducted using tissu
Autor:
Masaya Nagao, Kimimitsu Oda, Yayoi Kurokawa, Shuichi Enomoto, Seiji Masuda, Fumie Teranishi, Victor Faundez, M. Leigh Ackland, Makoto Hiromura, Israel Sekler, Ayako Fukunaka, Taiho Kambe
Publikováno v:
Journal of Biological Chemistry. 286:16363-16373
A number of enzymes become functional by binding to zinc during their journey through the early secretory pathway. The zinc transporters (ZnTs) located there play important roles in this step. We have previously shown that two zinc transport complexe
Autor:
Hitoshi Migaki, Katsuzumi Okumura, Kaori Ishihara, Tomohiro Yamazaki, Ayako Fukunaka, Taiho Kambe, Seiji Masuda, Naoko Fujiwara, Yuko Yamaguchi-Iwai, Yayoi Kurokawa, Masaya Nagao, Tomoyuki Suzuki
Publikováno v:
Journal of Biological Chemistry. 284:30798-30806
The majority of CDF/ZnT zinc transporters form homo-oligomers. However, ZnT5, ZnT6, and their orthologues form hetero-oligomers in the early secretory pathway where they load zinc onto zinc-requiring enzymes and maintain secretory pathway functions.
Autor:
Tokuji Tsuj1, Yayoi Kurokawa1, Chiche, Johanna2, Pouysségur, Jacques3,4, Hiroshi Sato5, Hideya Fukuzawa1, Masaya Nagao1, Taiho Kambe1 kambe1@kais.kyoto-u.ac.jp
Publikováno v:
Journal of Biological Chemistry. 2/10/2017, Vol. 292 Issue 6, p2159-2173. 15p.