Zobrazeno 1 - 4
of 4
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:
Clausen, J D, McIntosh, D B, Woolley, D G & Andersen, J P 2008, ' Critical Interaction of Actuator Domain Residues Arginine 174, Isoleucine 188, and Lysine 205 with Modulatory Nucleotide in Sarcoplasmic Reticulum Ca 2+-ATPase ', Journal of Biological Chemistry, vol. 283, no. 51, pp. 35703-14 . https://doi.org/10.1074/jbc.M806795200
Udgivelsesdato: 2008-Dec-19 ATP plays dual roles in the reaction cycle of the sarcoplasmic reticulum Ca(2+)-ATPase by acting as the phosphorylating substrate as well as in nonphosphorylating (modulatory) modes accelerating conformational transitions
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
Publikováno v:
Journal of Biological Chemistry. 279:54426-54437
Point mutants with alterations to amino acid residues Thr(247), Pro(248), Glu(340), Asp(813), Arg(819), and Arg(822) of sarcoplasmic reticulum Ca(2+)-ATPase were analyzed by transient kinetic measurements. In the Ca(2+)-ATPase crystal structures, mos