Zobrazeno 1 - 10
of 247
pro vyhledávání: '"Ryota, Iino"'
Autor:
Yoshimi MATSUMOTO, Seiji YAMASAKI, Kouhei HAYAMA, Ryota IINO, Hiroyuki NOJI, Akihito YAMAGUCHI, Kunihiko NISHINO
Publikováno v:
Proceedings of the Japan Academy. Series B, Physical and Biological Sciences, Vol 100, Iss 1, Pp 57-67 (2024)
Changes in expression levels of drug efflux pump genes, mexB and mexY, and porin gene oprD in Pseudomonas aeruginosa were investigated in this study. Fifty-five multidrug-resistant P. aeruginosa (MDRP) strains were compared with 26 drug-sensitive str
Externí odkaz:
https://doaj.org/article/c848b6dbb03745449f524ddfd03f1bd8
Autor:
Raymond N. Burton-Smith, Chihong Song, Hiroshi Ueno, Takeshi Murata, Ryota Iino, Kazuyoshi Murata
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-13 (2023)
Abstract The vacuolar-type ATPase from Enterococcus hirae (EhV-ATPase) is a thus-far unique adaptation of V-ATPases, as it performs Na+ transport and demonstrates an off-axis rotor assembly. Recent single molecule studies of the isolated V1 domain ha
Externí odkaz:
https://doaj.org/article/23b83a07a51b43048838f3bc0e38a0dd
Publikováno v:
ACS Omega, Vol 5, Iss 41, Pp 26807-26816 (2020)
Externí odkaz:
https://doaj.org/article/a51e9120bc8744c088802733e73b8425
Publikováno v:
Biophysics and Physicobiology, Vol 17 (2020)
Motor proteins are essential units of life and are well-designed nanomachines working under thermal fluctuations. These proteins control moving direction by consuming chemical energy or by dissipating electrochemical potentials. Chitinase A from bact
Externí odkaz:
https://doaj.org/article/98f491edcda64534aaaaa359ffee3efb
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Processive chitinase is a linear molecular motor which moves on the surface of crystalline chitin. Here authors use single-molecule imaging, X-ray crystallography and simulations on chitinase A (SmChiA) and show that Brownian motion along the single
Externí odkaz:
https://doaj.org/article/44bbc30a869946569170e33c85207248
Publikováno v:
ACS Omega, Vol 3, Iss 7, Pp 7715-7726 (2018)
Externí odkaz:
https://doaj.org/article/a06a71b44b9b4fcb903b524ff28f196c
Autor:
Takayuki Uchihashi, Yo-hei Watanabe, Yosuke Nakazaki, Takashi Yamasaki, Hiroki Watanabe, Takahiro Maruno, Kentaro Ishii, Susumu Uchiyama, Chihong Song, Kazuyoshi Murata, Ryota Iino, Toshio Ando
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
The bacterial protein disaggregation machine ClpB uses ATP to generate mechanical force to unfold and thread its protein substrates. Here authors visualize the ClpB ring using high-speed atomic force microscopy and capture conformational changes of t
Externí odkaz:
https://doaj.org/article/f10a7d63f3934077acd63c3f83c2cc21
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(42)
V-ATPases are rotary motor proteins that convert the chemical energy of ATP into the electrochemical potential of ions across cell membranes. V-ATPases consist of two rotary motors, V
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4c7f82c336b78490d86238238b835007
https://pubmed.ncbi.nlm.nih.gov/36215468
https://pubmed.ncbi.nlm.nih.gov/36215468
Autor:
Raymond N. Burton-Smith, Chihong Song, Hiroshi Ueno, Takeshi Murata, Ryota Iino, Kazuyoshi Murata
SummaryThe vacuolar-type ATPase from Enterococcus hirae (EhV-ATPase) is a thus-far unique adaptation of V-ATPases, as it performs Na+ transport and demonstrates an off-axis rotor assembly. Recent single molecular studies of the isolated V1 domain hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ae5956a9de8b1d33bd1d037a81eadf52
https://doi.org/10.1101/2022.08.09.503272
https://doi.org/10.1101/2022.08.09.503272
Publikováno v:
ACS Catalysis. 11:8550-8564
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e5d50d424bce534ce87d9ea562d42ea
https://doi.org/10.1021/acscatal.1c01204
https://doi.org/10.1021/acscatal.1c01204