Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Stefania, Danko"'
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
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
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
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
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
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
Publikováno v:
Scientific Reports
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
Autor:
Stefania Danko, Hiroshi Suzuki
Publikováno v:
P-Type ATPases ISBN: 9781493931781
The membrane-bound protein family, P-type ATPases, couples ATP hydrolysis with substrate transport across the membrane and forms an obligatory auto-phosphorylated intermediate in the transport cycle. The metal fluoride compounds, BeF x , AlF x , and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91adb12029ad526bca834d79df3470b2
https://doi.org/10.1007/978-1-4939-3179-8_19
https://doi.org/10.1007/978-1-4939-3179-8_19
Publikováno v:
YAKUGAKU ZASSHI. 130:179-189
Sarco(endo)plasmic reticulum Ca(2+)-ATPase is a representative member of P-type cation transporting ATPases and catalyzes Ca(2+) transport coupled with ATP hydrolysis. The ATPase possesses three cytoplasmic domains (N, P, and A) and ten transmembrane