A. D. Wegener

High molecular weight proteins in cardiac and skeletal muscle junctional sarcoplasmic reticulum vesicles bind calmodulin, are phosphorylated, and are degraded by Ca2+-activated protease.

D. Hathaway, L. Jones, S. Seiler, 1984, The Journal of biological chemistry.

Phospholamban phosphorylation in intact ventricles. Phosphorylation of serine 16 and threonine 17 in response to beta-adrenergic stimulation.

L. Jones, L R Jones, A D Wegener, 1989, The Journal of biological chemistry.

Purification and characterization of phospholamban from canine cardiac sarcoplasmic reticulum.

F. Gurd, W. Wilson, L. Jones, 1985, The Journal of biological chemistry.

Purification of phospholamban from canine cardiac sarcoplasmic reticulum vesicles by use of sulfhydryl group affinity chromatography.

L. Jones, H. Simmerman, A. Wegener, 1988, Methods in enzymology.

Proteolytic cleavage of phospholamban purified from canine cardiac sarcoplasmic reticulum vesicles. Generation of a low resolution model of phospholamban structure.

J. Liepnieks, L. Jones, H. Simmerman, 1986, The Journal of biological chemistry.