The Slippage of the Ca2+ Pump and Its Control by Anions and Curcumin in Skeletal and Cardiac Sarcoplasmic Reticulum
Open Access
- 1 April 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (16) , 13900-13906
- https://doi.org/10.1074/jbc.m111155200
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Curcumin, a Molecule That Inhibits the Ca2+-ATPase of Sarcoplasmic Reticulum but Increases the Rate of Accumulation of Ca2+Journal of Biological Chemistry, 2001
- Uncoupled ATPase Activity and Heat Production by the Sarcoplasmic Reticulum Ca2+-ATPaseJournal of Biological Chemistry, 2001
- Insight into the Uncoupling Mechanism of Sarcoplasmic Reticulum ATPase Using the Phosphorylating Substrate UTPJournal of Biological Chemistry, 2000
- Anionic phospholipids decrease the rate of slippage on the Ca2+-ATPase of sarcoplasmic reticulumBiochemical Journal, 1999
- Variable Stoichiometric Efficiency of Ca2+ and Sr2+ Transport by the Sarcoplasmic Reticulum ATPasePublished by Elsevier ,1995
- Adenosine 5'-triphosphate modulation of catalytic intermediates of calcium-adenosine triphosphatase of sarcoplasmic reticulum subsequent to enzyme phosphorylationBiochemistry, 1983
- Partial reactions in the catalytic and transport cycle of sarcoplasmic reticulum ATPaseBiochemistry, 1978
- Phosphorylation from Inorganic Phosphate and ATP Synthesis of Sarcoplasmic MembranesEuropean Journal of Biochemistry, 1977
- Demonstration of binding of triton X‐100 to amphiphilic proteins in crossed immunoelectrophoresisFEBS Letters, 1977
- Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate. Inhibition by calcium ionsBiochemistry, 1973