Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Taiga Imai"'
Autor:
Yuuki Hayakawa, Masak Takaine, Kien Xuan Ngo, Taiga Imai, Yamada, Masafumi D., Behjat, Arash Badami, Kenichi Umeda, Keiko Hirose, Ayhan Yurtsever, Noriyuki Kodera, Kiyotaka Tokuraku, Osamu Numata, Takeshi Fukuma, Toshio Ando, Kentaro Nakano, Uyeda, Taro Q. P.
Publikováno v:
Life Science Alliance; Jan2023, Vol. 6 Issue 1, p1-18, 18p
Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II
Autor:
Yuuki Hayakawa, Masak Takaine, Kien Xuan Ngo, Taiga Imai, Masafumi D Yamada, Arash Badami Behjat, Kenichi Umeda, Keiko Hirose, Ayhan Yurtsever, Noriyuki Kodera, Kiyotaka Tokuraku, Osamu Numata, Takeshi Fukuma, Toshio Ando, Kentaro Nakano, Taro QP Uyeda
Publikováno v:
Life Science Alliance. 6:e202201469
We report a case in which sub-stoichiometric binding of an actin-binding protein has profound structural and functional consequences, providing an insight into the fundamental properties of actin regulation. Rng2 is an IQGAP contained in contractile
Actin binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II
Autor:
Yuuki Hayakawa, Masak Takaine, Kien Xuan Ngo, Taiga Imai, Masafumi D. Yamada, Arash Badami Behjat, Kenichi Umeda, Keiko Hirose, Ayhan Yurtsever, Noriyuki Kodera, Kiyotaka Tokuraku, Osamu Numata, Takeshi Fukuma, Toshio Ando, Kentaro Nakano, Taro Q.P. Uyeda
Substoichiometric binding of certain actin-binding proteins induces conformational changes in a disproportionally large number of actin protomers in actin filaments. Here, we report a case in which such conformational changes in actin filaments have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d20e9b24f576f8194dfdc137a6f24a30
https://doi.org/10.1101/2020.04.14.041046
https://doi.org/10.1101/2020.04.14.041046