Factors that modify the molecular size of phospholamban, the 23,000-dalton cardiac sarcoplasmic reticulum phosphoprotein.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference25 articles.
1. Adenosine 3', 5'-Monophosphate-Dependent Membrane Phosphorylation
2. Cyclic Adenosine 3′,5′-Monophosphate-stimulated Protein Kinase and a Substrate Associated with Cardiac Sarcoplasmic Reticulum
3. Adenosine 3′:5′-Monophosphate-dependent Protein Kinase-catalyzed Phosphorylation Reaction and Its Relationship to Calcium Transport in Cardiac Sarcoplasmic Reticulum
4. Phosphorylation of a 22,000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3':5'-monophosphate-dependent protein kinase.
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4. Site-specific phosphorylation of a phospholamban peptide by cyclic nucleotide- and Ca2+/calmodulin-dependent protein kinases of cardiac sarcoplasmic reticulum;Alterations of Excitation-Contraction Coupling in the Failing Human Heart;1998
5. Site-specific phosphorylation of a phospholamban peptide by cyclic nucleotide- and Ca2+/calmodulin-dependent protein kinases of cardiac sarcoplasmic reticulum;Basic Research in Cardiology;1997
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