Phosphorylation of the Thr17 residue of phospholamban. New insights into the physiological role of the CaMK-II pathway of phospholamban phosphorylation.
Mattiazzi
A
A
Centro de Investigaciones Cardiovasculares, Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Argentina. cicme@isis.unlp.edu.ar
Vittone
L
L
Mundiña-Weilenmann
C
C
Said
M
M
D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D009206:Myocardium / Q000378:metabolism*; D019319:Okadaic Acid / Q000494:pharmacology; D010766:Phosphorylation; D010769:Phosphothreonine; D051381:Rats; D017208:Rats, Wistar; D013912:Threonine; D000099211:Phospholamban
D002135:Calcium-Binding Proteins; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D019319:Okadaic Acid; D010769:Phosphothreonine; D013912:Threonine; D000099211:Phospholamban