1999
Molecular identification of human G-substrate, a possible downstream component of the cGMP-dependent protein kinase cascade in cerebellar Purkinje cells
Endo S, Suzuki M, Sumi M, Nairn A, Morita R, Yamakawa K, Greengard P, Ito M. Molecular identification of human G-substrate, a possible downstream component of the cGMP-dependent protein kinase cascade in cerebellar Purkinje cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 2467-2472. PMID: 10051666, PMCID: PMC26808, DOI: 10.1073/pnas.96.5.2467.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainCerebellumCloning, MolecularCyclic GMP-Dependent Protein KinasesDatabases as TopicExpressed Sequence TagsHumansMolecular Sequence DataNerve Tissue ProteinsPurkinje CellsRabbitsRecombinant ProteinsRNA, MessengerSequence AlignmentSequence Homology, Amino AcidTranscription, GeneticConceptsAmino acid sequenceProtein phosphatase 1G-substrateAcid sequencePhosphatase 1Deduced amino acid sequenceRadiation hybrid panel analysisProtein phosphatase 2APutative phosphorylation sitesCGMP-dependent protein kinaseProtein kinase cascadeProtein phosphatase inhibitorSequence tag databaseSites of phosphorylationVitro translation productsHuman brain libraryCGMP-dependent proteinAcid-soluble proteinsApparent molecular massSDS/PAGEPhosphatase 2AThr-35Kinase cascadePhosphorylation sitesTag databaseRegulation of CFTR Cl- ion channels by phosphorylation and dephosphorylation.
Gadsby D, Nairn A. Regulation of CFTR Cl- ion channels by phosphorylation and dephosphorylation. Advances In Second Messenger And Phosphoprotein Research 1999, 33: 79-106. PMID: 10218115, DOI: 10.1016/s1040-7952(99)80006-8.Peer-Reviewed Original ResearchAdenosine TriphosphateBinding SitesCalcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesCyclic GMP-Dependent Protein KinasesCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorHumansIon Channel GatingModels, MolecularPhosphoprotein PhosphatasesPhosphorylationProtein Kinase C
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