Maximal Inhibition of SERCA2 Ca2+ Affinity by Phospholamban in Transgenic Hearts Overexpressing a Non-phosphorylatable Form of Phospholamban
Open Access
- 1 April 2000
- journal article
- Published by Elsevier
- Vol. 275 (16), 12129-12135
- https://doi.org/10.1074/jbc.275.16.12129
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Differential regulation of inotropy and lusitropy in overexpressed Gsα myocytes through cAMP and Ca2+ channel pathwaysJournal of Clinical Investigation, 1999
- Reduced Ca2+-Sensitivity of SERCA 2a in Failing Human Myocardium due to Reduced Serin-16 Phospholamban PhoshorylationJournal of Molecular and Cellular Cardiology, 1999
- Depolymerization of Phospholamban in the Presence of Calcium Pump: A Fluorescence Energy Transfer StudyBiochemistry, 1999
- Mutation and Phosphorylation Change the Oligomeric Structure of Phospholamban in Lipid BilayersBiochemistry, 1997
- Increased Expression of Cardiac Phosphatases in Patients with End-stage Heart FailureJournal of Molecular and Cellular Cardiology, 1997
- Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice.Journal of Clinical Investigation, 1996
- Alterations of Sarcoplasmic Reticulum Proteins in Failing Human Dilated CardiomyopathyCirculation, 1995
- Effects of cyclic nucleotide dependent protein kinases on the endoplasmic reticulum Ca2+ pump of bovine pulmonary arteryCell Calcium, 1990
- Regulation of Ca2+ transport by cyclic 3′,5′-AMP-dependent and calcium-calmodulin-dependent phosphorylation of cardiac sarcoplasmic reticulumBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1985
- Phosphorylation of the Sarcoplasmic Reticulum and SarcolemmaAnnual Review of Physiology, 1982