Cardiac Calcium ATPase Dimerization Measured by Cross-Linking and Fluorescence Energy Transfer

Author:

Blackwell Daniel J.,Zak Taylor J.,Robia Seth L.

Publisher

Elsevier BV

Subject

Biophysics

Reference62 articles.

1. Correlation between calmodulin-dependent increase in the rate of calcium transport and calmodulin-dependent phosphorylation of cardiac sarcoplasmic reticulum. Characterization of calmodulin-dependent phosphorylation;Plank;Eur. J. Biochem.,1983

2. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains;Simmerman;J. Biol. Chem.,1986

3. Phosphorylation of a 22,000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase;Tada;J. Biol. Chem.,1975

4. Differential changes in cardiac phospholamban and sarcoplasmic reticular Ca2+-ATPase protein levels. Effects on Ca2+ transport and mechanics in compensated pressure-overload hypertrophy and congestive heart failure;Kiss;Circ. Res.,1995

5. Decreased expression of cardiac sarcoplasmic reticulum Ca2+-pump ATPase in congestive heart failure due to myocardial infarction;Zarain-Herzberg;Mol. Cell. Biochem.,1996

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