1995
Isotype-specific Activation of Cystic Fibrosis Transmembrane Conductance Regulator-Chloride Channels by cGMP-dependent Protein Kinase II (∗)
French P, Bijman J, Edixhoven M, Vaandrager A, Scholte B, Lohmann S, Nairn A, de Jonge H. Isotype-specific Activation of Cystic Fibrosis Transmembrane Conductance Regulator-Chloride Channels by cGMP-dependent Protein Kinase II (∗). Journal Of Biological Chemistry 1995, 270: 26626-26631. PMID: 7592887, DOI: 10.1074/jbc.270.44.26626.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCattleCell LineCell MembraneChloride ChannelsCyclic GMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorEnzyme InhibitorsIntestinesIsoenzymesKineticsLungMacromolecular SubstancesMarine ToxinsMembrane PotentialsMicrovilliOxazolesPeptide FragmentsPhosphopeptidesPhosphorylationProtein Phosphatase 1Protein Tyrosine PhosphatasesRatsRecombinant ProteinsSwineTransfectionConceptsProtein kinaseType II cGMP-dependent protein kinaseCGMP-dependent protein kinase IICAMP-dependent protein kinaseCystic fibrosis transmembrane conductance regulator (CFTR) chloride channelCGMP-dependent protein kinaseCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorProtein kinase IINIH 3T3 fibroblastsRat intestinal cell lineRecombinant CFTRCF 2Presence of cGMPProtein phosphatasePresence of ATPCAK activationPhosphatase 1Phosphopeptide mapsCatalytic subunitCalyculin ACatalytic fragmentKinase IIConductance regulator
1992
Calmodulin and Protein Kinase C Cross‐Talk: The MARCKS Protein is an Actin Filament and Plasma Membrane Cross‐Linking Protein Regulated by Protein Kinase C Phosphorylation and by Calmodulin
Nairn A, Aderem A. Calmodulin and Protein Kinase C Cross‐Talk: The MARCKS Protein is an Actin Filament and Plasma Membrane Cross‐Linking Protein Regulated by Protein Kinase C Phosphorylation and by Calmodulin. Novartis Foundation Symposia 1992, 164: 145-161. PMID: 1395931, DOI: 10.1002/9780470514207.ch10.Peer-Reviewed Original ResearchConceptsCross-linking proteinsPlasma membraneF-actin cross-linking proteinsActin filamentsProtein kinase C phosphorylationAlanine-rich C kinase substrateKinase C phosphorylationGrowth factor-dependent mitogenesisSignal transduction pathwaysC kinase substrateActin-binding propertiesKinase substrateActivation of PKCTransduction pathwaysC phosphorylationMARCKS proteinInhibits phosphorylationMARCKSMembrane interactionsCycles of releaseSpecific substratesPhosphorylationPKCProteinCalmodulin
1988
Autophosphorylation and activation of Ca2+/calmodulin-dependent protein kinase II in intact nerve terminals.
Gorelick FS, Wang JK, Lai Y, Nairn AC, Greengard P. Autophosphorylation and activation of Ca2+/calmodulin-dependent protein kinase II in intact nerve terminals. Journal Of Biological Chemistry 1988, 263: 17209-17212. PMID: 2846557, DOI: 10.1016/s0021-9258(19)77816-8.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCerebral CortexEnzyme ActivationKineticsMacromolecular SubstancesPhosphorylationProtein KinasesSynaptosomesConceptsDependent protein kinase IIKinase IIAlpha subunitProtein kinase IIKinase II activityTwo-dimensional phosphopeptide mapsII activityState of phosphorylationAutophosphorylation mechanismThreonine residuesPhosphothreonine contentPhosphopeptide mapsTransient phosphorylationIndependent speciesPhosphoserine contentIntact nerve terminalsBeta subunitEnhanced phosphorylationSubunitsPhosphorylationAutophosphorylationIntact synaptosomesBasal incubation conditionsPhosphopeptidesDepolarization of synaptosomes
1979
The Role of Calmodulin in the Structure and Regulation of Phosphorylase Kinase from Rabbit Skeletal Muscle
SHENOLIKAR S, COHEN P, COHEN P, NAIRN A, PERRY S. The Role of Calmodulin in the Structure and Regulation of Phosphorylase Kinase from Rabbit Skeletal Muscle. The FEBS Journal 1979, 100: 329-337. PMID: 159817, DOI: 10.1111/j.1432-1033.1979.tb04175.x.Peer-Reviewed Original Research