Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Johannes D. Clausen"'
Publikováno v:
Clausen, J D, Holdensen, A N & Andersen, J P 2014, ' Critical Roles of Interdomain Interactions for Modulatory ATP Binding to Sarcoplasmic Reticulum Ca2+-ATPase ', Journal of Biological Chemistry . https://doi.org/10.1074/jbc.M114.571687
ATP has dual roles in the reaction cycle of sarcoplasmic reticulum Ca(2+)-ATPase. Upon binding to the Ca2E1 state, ATP phosphorylates the enzyme, and by binding to other conformational states in a non-phosphorylating modulatory mode ATP stimulates th
Publikováno v:
Anthonisen, A N, Clausen, J D & Andersen, J P 2006, ' Mutational analysis of the conserved TGES loop of sarcoplasmic reticulum Ca 2+-ATPase. ', Journal of Biological Chemistry, vol. 281, pp. 31572-31582 .
Aarhus University
Aarhus University
Crystal structures have shown that the conserved TGES loop of the Ca2+-ATPase is isolated in the Ca2E1 state but becomes inserted in the catalytic site in E2 states. Here, we have examined the kinetics of the partial reaction steps of the transport c
Autor:
Bente Vilsen, David B. McIntosh, Johannes D. Clausen, David H. MacLennan, Jens Peter Andersen, David G. Woolley
Publikováno v:
The Journal of Biological Chemistry
32515-32523
32515-32523
Residues in conserved motifs (625)TGD, (676)FARXXPXXK, and (701)TGDGVND in domain P of sarcoplasmic reticulum Ca(2+)-ATPase, as well as in motifs (601)DPPR and (359)NQR(/K)MSV in the hinge segments connecting domains N and P, were examined by mutagen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6815355f0643bf917a418bd98a786d79
http://hdl.handle.net/11427/35009
http://hdl.handle.net/11427/35009