Zobrazeno 1 - 10
of 481
pro vyhledávání: '"Masasuke Yoshida"'
Autor:
Toshiharu Suzuki, Naoya Iida, Junko Suzuki, Yasunori Watanabe, Toshiya Endo, Toru Hisabori, Masasuke Yoshida
Publikováno v:
FEBS Open Bio, Vol 6, Iss 12, Pp 1267-1272 (2016)
F1‐ATPase (F1) is a multisubunit water‐soluble domain of FoF1‐ATP synthase and is a rotary enzyme by itself. Earlier genetic studies using yeast suggested that two factors, Atp11p and Atp12p, contribute to F1 assembly. Here, we show that their
Externí odkaz:
https://doaj.org/article/3f57093d0aa947c9950f0c160ce1e16f
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e52534 (2012)
Nano-scale alignment of several proteins with freedom of motion is equivalent to an enormous increase in effective local concentration of proteins and will enable otherwise impossible weak and/or cooperative associations between them or with their li
Externí odkaz:
https://doaj.org/article/75b44cbd918e4ea0a5650377130898ea
Autor:
Yasuto Todokoro, Su-Jin Kang, Toshiharu Suzuki, Takahisa Ikegami, Masatsune Kainosho, Masasuke Yoshida, Toshimichi Fujiwara, Hideo Akutsu
Publikováno v:
Journal of the American Chemical Society. 144:14132-14139
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a9f579b770e1c96c561308cb000011f7
https://doi.org/10.1021/jacs.2c03580
https://doi.org/10.1021/jacs.2c03580
Autor:
Kailiang Zhang, Rong Bao, Fengyuan Huang, Kevin Yang, Qinqiang Long, Lothar Lauterboeck, Qinglin Yang, Yishu Ding, Masasuke Yoshida
Publikováno v:
Laboratory Investigation. 102:69-79
Mitochondrial homeostasis is crucial for the function of pancreatic β-cells. ATP synthase inhibitory factor subunit 1 (IF1) is a mitochondrial protein interacting with ATP synthase to inhibit its enzyme activity. IF1 may also play a role in maintain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6c714daafda9fa526417f7e461fabd3
https://doi.org/10.1038/s41374-021-00670-x
https://doi.org/10.1038/s41374-021-00670-x
Autor:
Toshiharu Suzuki, Masasuke Yoshida, Su-Jin Kang, Suyeon Bak, Yasuto Todokoro, Hideo Akutsu, Toshimichi Fujiwara
Publikováno v:
Journal of Biomolecular NMR. 70:53-65
FoF1-ATP synthase catalyzes ATP hydrolysis/synthesis coupled with a transmembrane H+ translocation in membranes. The Fo c-subunit ring plays a major role in this reaction. We have developed an assignment strategy for solid-state 13C NMR (ssNMR) signa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c515c23a5980f5c922b0f92e23c77cd3
https://doi.org/10.1007/s10858-017-0158-x
https://doi.org/10.1007/s10858-017-0158-x
Publikováno v:
Proceedings of the National Academy of Sciences. 114:4960-4965
Significance Peter D. Mitchell, a Nobel awardee in 1978, proposed that F o F 1 -ATP synthase converts energy between electrochemical potential of H + across biological membrane ( Δ μ ∼ H + ), which is established by respiratory chain complexes, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a7d277843ae283e9fdf744fea2d04ace
https://doi.org/10.1073/pnas.1700801114
https://doi.org/10.1073/pnas.1700801114
Autor:
Naoya Iida, Yasunori Watanabe, Toshiya Endo, Junko Suzuki, Masasuke Yoshida, Toru Hisabori, Toshiharu Suzuki
Publikováno v:
FEBS Open Bio. 6:1267-1272
F1-ATPase (F1) is a multisubunit water-soluble domain of FoF1- ATP synthase and is a rotary enzyme by itself. Earlier genetic studies using yeast suggested that two factors, Atp11p and Atp12p, contribute to F1 assembly. Here, we show that their mamma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::026cec75f7bf845743887e9ccfc7c506
https://doi.org/10.1002/2211-5463.12143
https://doi.org/10.1002/2211-5463.12143
Autor:
Kevin Yang, Qinglin Yang, Yicheng Huang, K. Saja, Fengyuan Huang, Masasuke Yoshida, Qingqiang Long
Publikováno v:
Diabetes. 67
Mitochondrial ATP synthase catalyzes the coupling step of oxidative phosphorylation. Under pathologic conditions, ATP synthase hydrolyzes ATP to replenish protons from the matrix into the intermembrane space, sustaining mitochondrial membrane potenti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::03ad3709a9362d85b2d399e9964ef1dc
https://doi.org/10.2337/db18-1748-p
https://doi.org/10.2337/db18-1748-p
Autor:
Toshihiko Oka, Akira Kitamura, Michiro Otaka, Tomoya Okamoto, Masasuke Yoshida, Ewa Grave, Masataka Kinjo, Masako Tanabe, Hiroshi Kubota, Hiroki Takahashi, Ryuichi Ishida, Fumihiro Motojima, Hideaki Itoh
Publikováno v:
International Journal of Molecular Sciences; Volume 19; Issue 2; Pages: 489
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 19, Iss 2, p 489 (2018)
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 19, Iss 2, p 489 (2018)
The E. coli GroEL/GroES chaperonin complex acts as a folding cage by producing a bullet-like asymmetric complex, and GroEL exists as double rings regardless of the presence of adenosine triphosphate (ATP). Its mammalian chaperonin homolog, heat shock
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0779606761a5344d414642da1df3481
Autor:
Fumihiro Motojima, Masasuke Yoshida
Publikováno v:
Biochemical and Biophysical Research Communications. 466:72-75
Many proteins in bacterial cells fold in the chaperonin cage made of the central cavity of GroEL capped by GroES. Recent studies indicate that the polypeptide in the cage spends the most time as a state tethered dynamically to the GroEL/GroES interfa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79ea08fa4947a547c84f611322434a01
https://doi.org/10.1016/j.bbrc.2015.08.108
https://doi.org/10.1016/j.bbrc.2015.08.108