Reexamination of the Role of the Leucine/Isoleucine Zipper Residues of Phospholamban in Inhibition of the Ca2+ Pump of Cardiac Sarcoplasmic Reticulum
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference25 articles.
1. Phosphorylation of a 22,000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3':5'-monophosphate-dependent protein kinase.
2. Phospholamban: Protein Structure, Mechanism of Action, and Role in Cardiac Function
3. Comparative studies of cardiac and skeletal sarcoplasmic reticulum ATPases. Effect of a phospholamban antibody on enzyme activation by Ca2+
4. The max of the Ca2+-ATPase of Cardiac Sarcoplasmic Reticulum (SERCA2a) Is Not Altered by Ca2+/Calmodulin-dependent Phosphorylation or by Interaction with Phospholamban
5. Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels. Evidence for a protein structure consisting of multiple identical phosphorylatable subunits.
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