Properties of the 23,000-Da phosphoproteins in cardiac sarcolemma and sarcoplasmic reticulum
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference42 articles.
1. Phosphorylation of a 22,000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3':5'-monophosphate-dependent protein kinase.
2. Adenosine 3′:5′-Monophosphate-dependent Protein Kinase-catalyzed Phosphorylation Reaction and Its Relationship to Calcium Transport in Cardiac Sarcoplasmic Reticulum
3. Correlation between protein kinase-mediated stimulation of calcium transport by cardiac sarcoplasmic reticulum and phosphorylation of a 22 000 dalton protein
4. Effect of Myocardial Protein Kinase Modulator on Adenosine 3′: 5′-Monophosphate-Dependent Protein Kinase-Induced Stimulation of Calcium Transport by Cardiac Sarcoplasmic Reticulum1
5. Correlation between calmodulin-dependent increase in the rate of calcium transport and calmodulin-dependent phosphorylation of cardiac sarcoplasmic reticulum. Characterization of calmodulin-dependent phosphorylation
Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Phospholamban: Protein Structure, Mechanism of Action, and Role in Cardiac Function;Physiological Reviews;1998-10-01
2. Role of Ca2+-calmodulin dependent phospholamban phosphorylation on the relaxant effect of ?-adrenergic agonists;Molecular and Cellular Biochemistry;1993
3. Defective sarcolemmal phosphorylation associated with noninsulin-dependent diabetes;Biochimica et Biophysica Acta (BBA) - Biomembranes;1990-04
4. Immunoelectron microscopical localization of phospholamban in adult canine ventricular muscle.;The Journal of Cell Biology;1987-05-01
5. Identification of the calmodulin-binding components in canine cardiac sarcolemma;Cell Calcium;1987-02
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