Zobrazeno 1 - 10
of 97
pro vyhledávání: '"Reiko, Urade"'
Autor:
Masahiro Shimizu, Aya Okuda, Ken Morishima, Rintaro Inoue, Nobuhiro Sato, Yasuhiro Yunoki, Reiko Urade, Masaaki Sugiyama
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-13 (2022)
Abstract Solving structural ensembles of flexible biomolecules is a challenging research area. Here, we propose a method to obtain possible structural ensembles of a biomolecule based on small-angle X-ray scattering (SAXS) and molecular dynamics simu
Externí odkaz:
https://doaj.org/article/cebe6a6661b54da3ae5c417ca4a47856
Autor:
Yasuhiro Yunoki, Atsushi Matsumoto, Ken Morishima, Anne Martel, Lionel Porcar, Nobuhiro Sato, Rina Yogo, Taiki Tominaga, Rintaro Inoue, Maho Yagi-Utsumi, Aya Okuda, Masahiro Shimizu, Reiko Urade, Kazuki Terauchi, Hidetoshi Kono, Hirokazu Yagi, Koichi Kato, Masaaki Sugiyama
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-12 (2022)
The revealed full KaiA12B6C6 complex is assembled including the dynamic and asynchronous KaiA N-terminal domains that have been missing in cryo-EM structures.
Externí odkaz:
https://doaj.org/article/190270aaeb514b6fbcb5c9982c22b4e8
Autor:
Aya Okuda, Masahiro Shimizu, Ken Morishima, Rintaro Inoue, Nobuhiro Sato, Reiko Urade, Masaaki Sugiyama
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
Abstract Multi-domain proteins (MDPs) show a variety of domain conformations under physiological conditions, regulating their functions through such conformational changes. One of the typical MDPs, ER-60 which is a protein folding enzyme, has a U-sha
Externí odkaz:
https://doaj.org/article/ad41e2aa6cd3420e869018a7efea4c15
Autor:
Rintaro Inoue, Yusuke Sakamaki, Takumi Takata, Kathleen Wood, Ken Morishima, Nobuhiro Sato, Aya Okuda, Masahiro Shimizu, Reiko Urade, Noriko Fujii, Masaaki Sugiyama
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
Abstract AlphaB crystallin (αB-crystallin) is a key protein for maintaining the long-term transparency of the eye lens. In the eye lens, αB-crystallin is a “dynamical” oligomer regulated by subunit exchange between the oligomers. To elucidate t
Externí odkaz:
https://doaj.org/article/b8a425ab410945a6aa125ea5bc530606
Autor:
Rintaro Inoue, Takashi Oda, Hiroshi Nakagawa, Taiki Tominaga, Tomohide Saio, Yukinobu Kawakita, Masahiro Shimizu, Aya Okuda, Ken Morishima, Nobuhiro Sato, Reiko Urade, Mamoru Sato, Masaaki Sugiyama
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-10 (2020)
Abstract Incoherent quasielastic neutron scattering (iQENS) is a fascinating technique for investigating the internal dynamics of protein. However, low flux of neutron beam, low signal to noise ratio of QENS spectrometers and unavailability of well-e
Externí odkaz:
https://doaj.org/article/802927b816be4ad28bcef6152cb0aa14
Autor:
Aya Okuda, Rintaro Inoue, Ken Morishima, Tomohide Saio, Yasuhiro Yunoki, Maho Yagi-Utsumi, Hirokazu Yagi, Masahiro Shimizu, Nobuhiro Sato, Reiko Urade, Koichi Kato, Masaaki Sugiyama
Publikováno v:
Biophysics and Physicobiology, Vol 18 (2021)
The distinguished feature of neutron as a scattering probe is an isotope effect, especially the large difference in neutron scattering length between hydrogen and deuterium. The difference renders the different visibility between hydrogenated and deu
Externí odkaz:
https://doaj.org/article/0a53650e2a0d439485807c25220b9695
Publikováno v:
Angewandte Chemie (International ed. in English). 62(1)
Three domain fragments of a multi-domain protein, ER-60, were ligated in two short linker regions using asparaginyl endopeptidase not involving denaturation. To identify appropriate ligation sites, by selecting several potential ligation sites with f
Autor:
Hirokazu Yagi, Koichi Kato, Masahiro Shimizu, Yasuhiro Yunoki, Maho Yagi-Utsumi, Reiko Urade, Ken Morishima, Aya Okuda, Nobuhiro Sato, Rintaro Inoue, Tomohide Saio, Masaaki Sugiyama
Publikováno v:
Biophysics and Physicobiology
Biophysics and Physicobiology, Vol 18 (2021)
Biophysics and Physicobiology, Vol 18 (2021)
The distinguished feature of neutron as a scattering probe is an isotope effect, especially the large difference in neutron scattering length between hydrogen and deuterium. The difference renders the different visibility between hydrogenated and deu
Autor:
Reiko Urade
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 83:781-793
For most of the proteins synthesized in the endoplasmic reticulum (ER), disulfide bond formation accompanies protein folding in a process called oxidative folding. Oxidative folding is catalyzed by a number of enzymes, including the family of protein
Autor:
Reiko Urade, Nobuhiro Sato, Masaaki Sugiyama, Takumi Takata, Yusuke Sakamaki, Noriko Fujii, Kathleen Wood, Ken Morishima, Aya Okuda, Rintaro Inoue, Masahiro Shimizu
Publikováno v:
Scientific Reports
Scientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
Scientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
AlphaB crystallin (αB-crystallin) is a key protein for maintaining the long-term transparency of the eye lens. In the eye lens, αB-crystallin is a “dynamical” oligomer regulated by subunit exchange between the oligomers. To elucidate the unsett