A. Wegener

Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains.

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

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.

Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels. Evidence for a protein structure consisting of multiple identical phosphorylatable subunits.

L. Jones, A. Wegener, Adam D. WegenerS, 1984, 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.

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.

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.

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.