1997
Regulation of rat Na+-K+-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA
Cheng X, Höög J, Nairn A, Greengard P, Aperia A. Regulation of rat Na+-K+-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA. American Journal Of Physiology 1997, 273: c1981-c1986. PMID: 9435504, DOI: 10.1152/ajpcell.1997.273.6.c1981.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionAnimalsColforsinCOS CellsCyclic AMPCyclic AMP-Dependent Protein KinasesCytosolDichlororibofuranosylbenzimidazoleEnzyme ActivationHomeostasisIsoenzymesKineticsMutagenesis, Site-DirectedPhorbol 12,13-DibutyratePhosphorylationProtein Kinase CRatsRecombinant ProteinsSerineSodium-Potassium-Exchanging ATPaseThionucleotidesTransfectionConceptsProtein kinase AProtein kinase CATPase alpha 1State of phosphorylationEffect of PKCWild-type enzymeSpecific PKA activatorActivity of PKCEnzyme activityAlpha 1Direct phosphorylationCOS cellsATPase alphaKinase ASer-23Kinase CPKA activatorPhosphorylationPKA systemPhorbol esterATPase activityMutantsEffect of PDBuCellsInhibition
1979
PHOSPHORYLATION OF THE MYOFIBRILLAR PROTEINS
Perry S, Cole H, Frearson N, Moir A, Nairn A, Solaro R. PHOSPHORYLATION OF THE MYOFIBRILLAR PROTEINS. 1979, 147-159. DOI: 10.1016/b978-0-08-023178-5.50018-5.Peer-Reviewed Original ResearchCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseProtein kinaseSerine 20Covalent phosphateHalf-maximal ATPase activityMyofibrillar proteinsMaximal ATPase activityPhysiological functionsPhosphorylationATPase activityIntracellular ATPKinaseProteinIncorporation of 32pPhosphate groupsInorganic phosphateATPResiduesPhosphate contentPhosphate