Zobrazeno 1 - 10
of 95
pro vyhledávání: '"Tatsuya Niwa"'
Autor:
Yuhei Chadani, Takashi Kanamori, Tatsuya Niwa, Kazuya Ichihara, Keiichi I. Nakayama, Akinobu Matsumoto, Hideki Taguchi
Publikováno v:
Cell Reports, Vol 42, Iss 12, Pp 113569- (2023)
Summary: Ribosomes polymerize nascent peptides through repeated inter-subunit rearrangements between the classic and hybrid states. The peptidyl-tRNA, the intermediate species during translation elongation, stabilizes the translating ribosome to ensu
Externí odkaz:
https://doaj.org/article/6d2d154c3c4741b6810cd8dfc85eb9a0
Publikováno v:
FEBS Open Bio, Vol 13, Iss 4, Pp 779-794 (2023)
Molecular chaperones are indispensable proteins that assist the folding of aggregation‐prone proteins into their functional native states, thereby maintaining organized cellular systems. Two of the best‐characterized chaperones are the Escherichi
Externí odkaz:
https://doaj.org/article/0e47f1adccc94d0e85de3682ec39ba70
Autor:
Yosuke Ito, Yuhei Chadani, Tatsuya Niwa, Ayako Yamakawa, Kodai Machida, Hiroaki Imataka, Hideki Taguchi
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
Here the authors find that nascent chains enriched in acidic amino acids destabilize the translating ribosome, eventually leading to stochastic premature termination in eukaryotes as in bacteria. Such risk of premature termination influences the amin
Externí odkaz:
https://doaj.org/article/916d1174a4b24e219937c6f63becb21d
Autor:
Hitoki Nanaura, Honoka Kawamukai, Ayano Fujiwara, Takeru Uehara, Yuichiro Aiba, Mari Nakanishi, Tomo Shiota, Masaki Hibino, Pattama Wiriyasermkul, Sotaro Kikuchi, Riko Nagata, Masaya Matsubayashi, Yoichi Shinkai, Tatsuya Niwa, Taro Mannen, Naritaka Morikawa, Naohiko Iguchi, Takao Kiriyama, Ken Morishima, Rintaro Inoue, Masaaki Sugiyama, Takashi Oda, Noriyuki Kodera, Sachiko Toma-Fukai, Mamoru Sato, Hideki Taguchi, Shushi Nagamori, Osami Shoji, Koichiro Ishimori, Hiroyoshi Matsumura, Kazuma Sugie, Tomohide Saio, Takuya Yoshizawa, Eiichiro Mori
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nuclear import receptors (NIRs) regulate self-association of RNA-binding proteins as phase modifiers, while C9orf72-derived arginine-rich polydipeptides lead to aberrant phase transitions. Here the authors show in molecular basis how arginine-rich po
Externí odkaz:
https://doaj.org/article/84769c6bce8f47bf9553e2e7438eb8a6
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Co-translational protein folding is one of the central topics in molecular biology. In Escherichia coli, trigger factor (TF) is a primary chaperone that facilitates co-translational folding by directly interacting with nascent polypeptide chains on t
Externí odkaz:
https://doaj.org/article/a35bc38aa070429c99112ac4cf31b346
Publikováno v:
Biochemistry and Biophysics Reports, Vol 17, Iss , Pp 27-31 (2019)
We tested whether a short model peptide derived from a group 3 late embryogenesis abundant (G3LEA) protein is able to maintain the fluorescence activity of a red fluorescent protein, mKate2, in the dry state. The fluorescence intensity of mKate2 alon
Externí odkaz:
https://doaj.org/article/94939aa212ce4eb99dd024ac22398a89
Publikováno v:
Molecules, Vol 27, Iss 12, p 3772 (2022)
The Escherichia coli chaperonin GroEL/ES (GroE) is one of the most extensively studied molecular chaperones. So far, ~80 proteins in E. coli are identified as GroE substrates that obligately require GroE for folding in vivo. In GroE-depleted cells, t
Externí odkaz:
https://doaj.org/article/44fff113d7034b7aa46f3e29098d0d39
Autor:
Mai Duy Luu Trinh, Daichi Miyazaki, Sumire Ono, Jiro Nomata, Masaru Kono, Hiroyuki Mino, Tatsuya Niwa, Yuki Okegawa, Ken Motohashi, Hideki Taguchi, Toru Hisabori, Shinji Masuda
Publikováno v:
iScience, Vol 24, Iss 2, Pp 102059- (2021)
Summary: In natural habitats, plants have developed sophisticated regulatory mechanisms to optimize the photosynthetic electron transfer rate at the maximum efficiency and cope with the changing environments. Maintaining proper P700 oxidation at phot
Externí odkaz:
https://doaj.org/article/fc916f74bb9f4395afb4a608762ddd39
Autor:
Hao K. Shen, Kiyoshi Morishita, P. K. Hashim, Kou Okuro, Daiki Kashiwagi, Ayumi Kimura, Haruaki Yanagisawa, Masahide Kikkawa, Tatsuya Niwa, Hideki Taguchi, Takuzo Aida
Publikováno v:
Angewandte Chemie.
Autor:
Keigo Hirai, Hiroko Yamashita, Shusuke Tomoshige, Yugo Mishima, Tatsuya Niwa, Kenji Ohgane, Mayumi Ishii, Kayoko Kanamitsu, Yui Ikemi, Shinsaku Nakagawa, Hideki Taguchi, Shinichi Sato, Yuichi Hashimoto, Minoru Ishikawa
Publikováno v:
ACS Med Chem Lett
[Image: see text] The onset of neurodegenerative disorders (NDs), such as Alzheimer’s disease, is associated with the accumulation of aggregates of misfolded proteins. We previously showed that chemical knockdown of ND-related aggregation-prone pro