Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Masashi Kajiro"'
Autor:
Masashi Kajiro, Mai Tsuchiya, Yoh-Ichi Kawabe, Ryohei Furumai, Naoya Iwasaki, Yuki Hayashi, Miyuki Katano, Yuka Nakajima, Natsuka Goto, Tatsuya Watanabe, Akiko Murayama, Hisashi Oishi, Masatsugu Ema, Satoru Takahashi, Hiroyuki Kishimoto, Junn Yanagisawa
Publikováno v:
PLoS ONE, Vol 6, Iss 10, p e25871 (2011)
Protein ubiquitination is a post-translational protein modification that regulates many biological conditions. Trip12 is a HECT-type E3 ubiquitin ligase that ubiquitinates ARF and APP-BP1. However, the significance of Trip12 in vivo is largely unknow
Externí odkaz:
https://doaj.org/article/03f823a97dad474ba8cd3be68901be9c
Autor:
Masashi Kajiro, Keiji Kimura, Yuka Nakajima, Shohei Kawasaki, Mitsutoshi Wayama, Yoko Komatsu, Takeshi Imamura, Aki Hanyu, Ichiaki Ito, Yoko Katsuno, Natsuka Goto, Junn Yanagisawa, Akiko Fujimura, Ryuichi Hirota, Akiko Murayama
Publikováno v:
Journal of Biological Chemistry. 285:14747-14755
Estrogen is a growth factor that stimulates cell proliferation. The effects of estrogen are mediated through the estrogen receptors, ERalpha and ERbeta, which function as ligand-induced transcription factors and belong to the nuclear receptor superfa
Autor:
Hiroyuki Takei, Sho Hei Ohie, Shin Ichi Hayashi, Yuko Seino, Yuka Nakajima, Yoh ichi Kawabe, Kaori Kawanowa, Keiji Kimura, Yasuhito Kobayashi, Akiko Murayama, Junn Yanagisawa, Ryuichi Hirota, Kae So-Ma, Miwako Kawano, Masashi Kajiro, Ichiaki Ito, Yuri Yamaguchi, Masafumi Kurosumi
Publikováno v:
Nature Cell Biology. 11:312-319
CHIP is a U-box-type ubiquitin ligase that induces ubiquitylation and degradation of its substrates, which include several oncogenic proteins. The relationship between CHIP and tumour progression, however, has not been elucidated. Here, we show that
Autor:
Natsuka Goto, Yuka Nakajima, Satoru Takahashi, Yoh-ichi Kawabe, Yuki Hayashi, Naoya Iwasaki, Tatsuya Watanabe, Ryohei Furumai, Masashi Kajiro, Masatsugu Ema, Hiroyuki Kishimoto, Akiko Murayama, Mai Tsuchiya, Miyuki Katano, Hisashi Oishi, Junn Yanagisawa
Publikováno v:
PLoS ONE
PLoS ONE, Vol 6, Iss 10, p e25871 (2011)
PLoS ONE, Vol 6, Iss 10, p e25871 (2011)
Protein ubiquitination is a post-translational protein modification that regulates many biological conditions [1], [2], [3], [4]. Trip12 is a HECT-type E3 ubiquitin ligase that ubiquitinates ARF and APP-BP1 [5], [6]. However, the significance of Trip