Associated Papers
Deception in simplicity: hereditary phospholamban mutations in dilated cardiomyopathy.
Young HS et al.
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire, 2015
Phospholamban interactome in cardiac contractility and survival: A new vision of an old friend.
Haghighi K et al.
Journal of Molecular and Cellular Cardiology, 2014
The role of CaMKII regulation of phospholamban activity in heart disease.
Mattiazzi A et al.
Frontiers in Pharmacology, 2014
Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy.
Ceholski DK et al.
The Journal of Biological Chemistry, 2012
Ryanodine receptor-mediated arrhythmias and sudden cardiac death.
Blayney LM et al.
Pharmacology & Therapeutics, 2009
Threonine-17 phosphorylation of phospholamban: a key determinant of frequency-dependent increase of cardiac contractility.
Zhao W et al.
Journal of Molecular and Cellular Cardiology, 2004
Phospholamban: a crucial regulator of cardiac contractility.
MacLennan DH et al.
Nature Reviews. Molecular Cell Biology, 2003
A single site (Ser16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac responses to beta -agonists.
Chu G et al.
The Journal of Biological Chemistry, 2000
Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulum.
Kimura Y et al.
The Journal of Biological Chemistry, 1998
Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum.
Toyofuku T et al.
The Journal of Biological Chemistry, 1994
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