Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Takuya B. Hiyama"'
Autor:
Jun Abe1, Takuya B. Hiyama1, Atsushi Mukaiyama1,2, Seyoung Son3,4, Toshifumi Mori2,5, Shinji Saito1,2,5, Masato Osako3, Wolanin, Julie1,6, Eiki Yamashita7, Takao Kondo3, Shuji Akiyama1,2 akiyamas@ims.ac.jp
Publikováno v:
Science. 7/17/2015, Vol. 349 Issue 6245, p312-316. 5p.
Autor:
Masato Osako, Shinji Saito, Jun Abe, Shuji Akiyama, Eiki Yamashita, Toshifumi Mori, Takao Kondo, Takuya B. Hiyama, Atsushi Mukaiyama, Julie Wolanin, Se-Young Son
Publikováno v:
Science. 349:312-316
Biochemical basis of a 24-hour clock Circadian clocks keep organisms in synch with such daily cycles as illumination, activity, and food availability. The circadian clock in cyanobacteria has the necessary 24-hour period despite its three component p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4875ce10be1d8cf11295b22c7bb8282b
https://doi.org/10.1126/science.1261040
https://doi.org/10.1126/science.1261040
Autor:
Toshiaki Higo, Shigeyuki Yokoyama, Takashi Umehara, M. Takahashi, Kensaku Sakamoto, Kazuhiro Kashiwagi, Takuya B. Hiyama, Takuhiro Ito, Madoka Nishimoto
Publikováno v:
Nature. 531(7592)
Eukaryotic cells restrict protein synthesis under various stress conditions, by inhibiting the eukaryotic translation initiation factor 2B (eIF2B). eIF2B is the guanine nucleotide exchange factor for eIF2, a heterotrimeric G protein consisting of α-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60104b15ff118315aae0c2165bbeb5d1
https://pubmed.ncbi.nlm.nih.gov/26901872
https://pubmed.ncbi.nlm.nih.gov/26901872
Autor:
Mikako Shirouzu, Yu Kitago, Takuya B. Hiyama, Shun-ichi Sekine, John Rose, Bi-Cheng Wang, Isao Tanaka, Min Zhao, Seiki Kuramitsu, Min Yao, Chizu Kuroishi, Zhi-Jie Liu, Shigeyuki Yokoyama, Nobuhisa Watanabe, Takaho Terada
Publikováno v:
Journal of Structural and Functional Genomics. 7:119-129
The single-domain coenzyme A (CoA)-binding protein is conserved in bacteria, archaea, and a few eukaryal taxa. It consists of a Rossmann-fold domain, belonging to the FAD/NAD(P)-binding ;superfamily. The crystal structure of the Thermus thermophilus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45f8504062d159285b0844df3106d2d1
https://doi.org/10.1007/s10969-007-9015-6
https://doi.org/10.1007/s10969-007-9015-6
Autor:
Jun, Abe, Takuya B, Hiyama, Atsushi, Mukaiyama, Seyoung, Son, Toshifumi, Mori, Shinji, Saito, Masato, Osako, Julie, Wolanin, Eiki, Yamashita, Takao, Kondo, Shuji, Akiyama
Publikováno v:
Science (New York, N.Y.). 349(6245)
Circadian clocks generate slow and ordered cellular dynamics but consist of fast-moving bio-macromolecules; consequently, the origins of the overall slowness remain unclear. We identified the adenosine triphosphate (ATP) catalytic region [adenosine t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::57b7ce667c2f7501d6035164d1bfad04
https://pubmed.ncbi.nlm.nih.gov/26439342
https://pubmed.ncbi.nlm.nih.gov/26439342
Publikováno v:
Journal of molecular biology. 392(4)
Eukaryotic translation initiation factor 2B (eIF2B) is the heteropentameric guanine-nucleotide exchange factor specific for eukaryotic initiation factor 2 (eIF2). Under stressed conditions, guanine-nucleotide exchange is strongly inhibited by the tig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bceb4f12ed8b337bdb4185e0c06008ee
https://pubmed.ncbi.nlm.nih.gov/19631657
https://pubmed.ncbi.nlm.nih.gov/19631657