Zobrazeno 1 - 10
of 384
pro vyhledávání: '"Kazuo Yamasaki"'
Autor:
Kazuo Yamasaki, Takashi Daiho, Satoshi Yasuda, Stefania Danko, Jun-ichi Kawabe, Hiroshi Suzuki
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-12 (2022)
Abstract Arg324 of sarcoplasmic reticulum Ca2+-ATPase forms electrostatic interactions with the phosphate moiety of phospholipids in most reaction states, and a hydrogen bond with Tyr122 in other states. Using site-directed mutagenesis, we explored t
Externí odkaz:
https://doaj.org/article/cde8cc0e189a45628f84d8db218ab550
Autor:
Takanobu A. Katoh, Takashi Daiho, Kazuo Yamasaki, Stefania Danko, Shoko Fujimura, Hiroshi Suzuki
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
Abstract The sarcoendoplasmic reticulum Ca2+-ATPase (SERCA) transports Ca2+ ions across the membrane coupled with ATP hydrolysis. Crystal structures of ligand-stabilized molecules indicate that the movement of actuator (A) domain plays a crucial role
Externí odkaz:
https://doaj.org/article/42b4be887568440d87720bad745fb185
Autor:
Katsuji Hattori, Naoe Sukenobu, Tomo Sasaki, Shunsuke Takasuga, Takeo Hayashi, Ryoji Kasai, Kazuo Yamasaki, Osamu Hazeki
Publikováno v:
Journal of Pharmacological Sciences, Vol 93, Iss 1, Pp 69-73 (2003)
ABSTRACT: Lagerstroemin, an ellagitannin isolated from the leaves of Lagerstroemia speciosa (L.) Pers. (Lythraceae), was examined for its biological activities. In rat adipocytes, the compound increased the rate of glucose uptake and decreased the is
Externí odkaz:
https://doaj.org/article/4f403d98abe74f24911c0c3f37b4eba2
Publikováno v:
Pharmacological Research on Traditional Herbal Medicines
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::26a5b71d89e64bb2e4eb80c39bc06781
https://doi.org/10.1201/9781003072867-7
https://doi.org/10.1201/9781003072867-7
Publikováno v:
Journal of Biological Chemistry. 292:20218-20227
Sarco(endo)plasmic reticulum Ca2+-ATPase catalyzes ATP-driven Ca2+ transport from the cytoplasm to the lumen and is critical for a range of cell functions, including muscle relaxation. Here, we investigated the effects of the headgroups of the 1-palm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1051e1c8ce86a525631a740af0a822d4
https://doi.org/10.1074/jbc.m117.816702
https://doi.org/10.1074/jbc.m117.816702
Autor:
Hiroshi Ueta, Ryutaro Seo, Norifumi Sugo, Kazuma Yunoki, Kazuo Yamasaki, Takahiro Shimozono, Hiroyuki Mima
Publikováno v:
Nihon Shuchu Chiryo Igakukai zasshi. 22:27-32
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5669cdb08d3d52f165748d20eae274e0
https://doi.org/10.3918/jsicm.22.27
https://doi.org/10.3918/jsicm.22.27
Publikováno v:
The Journal of biological chemistry. 292(49)
Sarco(endo)plasmic reticulum Ca2+-ATPase catalyzes ATP-driven Ca2+ transport from the cytoplasm to the lumen and is critical for a range of cell functions, including muscle relaxation. Here, we investigated the effects of the headgroups of the 1-palm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fe3d3d77897f1b3b2be8a8cca57f5c05
https://pubmed.ncbi.nlm.nih.gov/29032359
https://pubmed.ncbi.nlm.nih.gov/29032359
Publikováno v:
Scientific Reports. 7
Ca2+ transport by sarcoplasmic reticulum Ca2+-ATPase involves ATP-dependent phosphorylation of a catalytic aspartic acid residue. The key process, luminal Ca2+ release occurs upon phosphoenzyme isomerization, abbreviated as E1PCa2 (reactive to ADP re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7eda5447083aeb64b1e79576762cb678
https://doi.org/10.1038/srep41172
https://doi.org/10.1038/srep41172
Publikováno v:
Journal of Biological Chemistry. 289:31241-31252
The actuator (A) domain of sarco(endo)plasmic reticulum Ca2+-ATPase not only plays a catalytic role but also undergoes large rotational movements that influence the distant transport sites through connections with transmembrane helices M1 and M2. Her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::06754baccc39b45d604f15fdbef92b2e
https://doi.org/10.1074/jbc.m114.584086
https://doi.org/10.1074/jbc.m114.584086
Publikováno v:
Journal of Biological Chemistry. 288:20646-20657
Sarcoplasmic reticulum Ca(2+)-ATPase couples the motions and rearrangements of three cytoplasmic domains (A, P, and N) with Ca(2+) transport. We explored the role of electrostatic force in the domain dynamics in a rate-limiting phosphoenzyme (EP) tra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec0536bbb6ee21f16d0c7d9ee70682e8
https://doi.org/10.1074/jbc.m113.482711
https://doi.org/10.1074/jbc.m113.482711