A Single Site (Ser16) Phosphorylation in Phospholamban Is Sufficient in Mediating Its Maximal Cardiac Responses to β-Agonists
Open Access
- 1 December 2000
- journal article
- Published by Elsevier
- Vol. 275 (49), 38938-38943
- https://doi.org/10.1074/jbc.m004079200
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Frequency-encoding Thr17 Phospholamban Phosphorylation Is Independent of Ser16 Phosphorylation in Cardiac MyocytesJournal of Biological Chemistry, 2000
- Pentameric Assembly of Phospholamban Facilitates Inhibition of Cardiac Function in VivoPublished by Elsevier ,1998
- Phosphorylation States of PhospholambanaAnnals of the New York Academy of Sciences, 1998
- Sites of Regulatory Interaction between Calcium ATPases and PhospholambanaAnnals of the New York Academy of Sciences, 1998
- Immunodetection of Phosphorylation Sites Gives New Insights into the Mechanisms Underlying Phospholamban Phosphorylation in the Intact HeartJournal of Biological Chemistry, 1996
- Phospholamban Regulates the Ca2+-ATPase through Intramembrane InteractionsJournal of Biological Chemistry, 1996
- Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice.Journal of Clinical Investigation, 1996
- In Vivo Echocardiographic Detection of Enhanced Left Ventricular Function in Gene-Targeted Mice With Phospholamban DeficiencyCirculation Research, 1995
- 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
- Concerted regulation of cardiac sarcoplasmic reticulum calcium transport by cyclic adenosine monophosphate dependent and calcium-calmodulin-dependent phosphorylationsBiochemistry, 1979