Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Yukako Miyata"'
Autor:
Chunlai Tam, Mutsuko Kukimoto-Niino, Yukako Miyata-Yabuki, Kengo Tsuda, Chiemi Mishima-Tsumagari, Kentaro Ihara, Mio Inoue, Mayumi Yonemochi, Kazuharu Hanada, Takehisa Matsumoto, Mikako Shirouzu, Kam Y. J. Zhang
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-11 (2023)
Structural analysis of the Ras-binding domain (RBD) of ELMO1 alone and in complex with the activator RhoG enables rational engineering and validation of a nanobody targeting ELMO1 RBD.
Externí odkaz:
https://doaj.org/article/57ffcbf5665046feb62686a925bac3cb
Autor:
Kento Kasahara, Suyong Re, Grzegorz Nawrocki, Hiraku Oshima, Chiemi Mishima-Tsumagari, Yukako Miyata-Yabuki, Mutsuko Kukimoto-Niino, Isseki Yu, Mikako Shirouzu, Michael Feig, Yuji Sugita
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
The intracellular compartment is a crowded environment. Here, the authors use molecular dynamics (MD) simulations to assess inhibitor binding to c-Src kinase and show how ligand binding pathways differ in crowded and dilute protein solutions, highlig
Externí odkaz:
https://doaj.org/article/8d675a4370724533a2e4806e520bcb66
Autor:
Mikako Shirouzu, Chiemi Mishima-Tsumagari, Isseki Yu, Kento Kasahara, Mutsuko Kukimoto-Niino, Grzegorz Nawrocki, Michael Feig, Yuji Sugita, Suyong Re, Yukako Miyata-Yabuki, Hiraku Oshima
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
The inside of a cell is highly crowded with proteins and other biomolecules. How proteins express their specific functions together with many off-target proteins in crowded cellular environments is largely unknown. Here, we investigate an inhibitor b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cb3efa8a102a08a297bd3e3d7e210b8
https://pubmed.ncbi.nlm.nih.gov/34215742
https://pubmed.ncbi.nlm.nih.gov/34215742
Autor:
Shuji Sonezaki, Yasuhiko Kato, Fumio Amano, Yukako Miyata, Yoshiyuki Ishii, Kazumi Akita, Yasushi Iwasaki
Publikováno v:
Journal of Biochemistry. 127:837-844
The SulA protein is a cell division inhibitor in Escherichia coli, and is specifically degraded by Lon protease. To study the recognition site of SulA for Lon, we prepared a mutant SulA protein lacking the C-terminal 8 amino acid residues (SA8). This
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ec6922253ad2925fdbb37c3e1b1a355
https://doi.org/10.1093/oxfordjournals.jbchem.a022677
https://doi.org/10.1093/oxfordjournals.jbchem.a022677
Autor:
Yasuko Tomo, Yukako Miyata, Takayoshi Matsuda, Makoto Inoue, Shigeyuki Yokoyama, Masaaki Aoki, Takanori Kigawa
Publikováno v:
Protein expression and purification. 68(2)
High-throughput protein production systems have become an important issue, because protein production is one of the bottleneck steps in large-scale structural and functional analyses of proteins. We have developed a dialysis reactor and a fully autom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::023693a4417431cb682ceca78785a112
https://pubmed.ncbi.nlm.nih.gov/19664715
https://pubmed.ncbi.nlm.nih.gov/19664715
Autor:
Makoto Inoue, Masaaki Aoki, Takaho Terada, Akiko Tanaka, Manabu Nakayama, Emi Nunokawa, Shigeyuki Yokoyama, Takahiro Nagase, Tetsuo Takagi, Kazuo Sato, Reiko Kikuno, Mikako Shirouzu, Noriko Hirakawa, Yo Matsuo, Takanori Kigawa, Takashi Yabuki, Seizo Koshiba, Yukako Miyata, Takayoshi Matsuda, Eiko Seki, Osamu Ohara, Ayako Sakamoto, Kohei Saito
Publikováno v:
Structure (London, England : 1993). 12(9)
CYLD was originally identified as the human familial cylindromatosis tumor suppressor. Recently, it was reported that CYLD directly interacts with NEMO/IKKgamma and TRAF2 in the NF-kappaB signaling pathway. The two proteins bind to a region of CYLD t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12690721cb4f3bedf2b7c78b84e8f001
https://pubmed.ncbi.nlm.nih.gov/15341735
https://pubmed.ncbi.nlm.nih.gov/15341735