2000
Severed Channels Probe Regulation of Gating of Cystic Fibrosis Transmembrane Conductance Regulator by Its Cytoplasmic Domains
Csanády L, Chan K, Seto-Young D, Kopsco D, Nairn A, Gadsby D. Severed Channels Probe Regulation of Gating of Cystic Fibrosis Transmembrane Conductance Regulator by Its Cytoplasmic Domains. The Journal Of General Physiology 2000, 116: 477-500. PMID: 10962022, PMCID: PMC2233695, DOI: 10.1085/jgp.116.3.477.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAdenylyl ImidodiphosphateAnimalsBase SequenceCyclic AMP-Dependent Protein KinasesCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDNA PrimersFemaleHumansIn Vitro TechniquesIon Channel GatingModels, BiologicalMutationOocytesPhosphorylationProtein Structure, TertiaryRecombinant ProteinsXenopusConceptsR domainCFTR channelsPhosphorylated R domainWild-type CFTR channelsCytoplasmic regulatory domainCystic fibrosis transmembrane conductance regulatorNucleotide Binding DomainFibrosis transmembrane conductance regulatorDetailed functional characteristicsWT channelsApparent ATP affinityTransmembrane conductance regulatorCFTR Cl- channelPresence of PKANonhydrolyzable ATP analogue AMPPNPATP analogue AMPPNPATP bindingRegulatory domainCytoplasmic domainWt-CFTRBinding domainsGating eventsConductance regulatorATP affinityFunctional interaction
1999
Requirement for DARPP‐32 in mediating effect of dopamine D2 receptor activation
Nishi A, Snyder G, Fienberg A, Fisone G, Aperia A, Nairn A, Greengard P. Requirement for DARPP‐32 in mediating effect of dopamine D2 receptor activation. European Journal Of Neuroscience 1999, 11: 2589-2592. PMID: 10383649, DOI: 10.1046/j.1460-9568.1999.00724.x.Peer-Reviewed Original ResearchConceptsDopamine D2 agonistD1 agonistDopamine D1 agonistDARPP-32D2 agonistDopamine D2 receptor activationDopamine D2 receptor agonistD2 receptor activationD2 receptor agonistBiological effectsReceptor agonistD1 receptorsD2 receptorsMouse neostriatumProtein phosphatase-1 inhibitorReceptor activationAgonistsPhosphatase-1 inhibitorDopamine signalingObligatory roleRole of Phosphorylation of Alzheimer’s Amyloid Precursor Protein during Neuronal Differentiation
Ando K, Oishi M, Takeda S, Iijima K, Isohara T, Nairn A, Kirino Y, Greengard P, Suzuki T. Role of Phosphorylation of Alzheimer’s Amyloid Precursor Protein during Neuronal Differentiation. Journal Of Neuroscience 1999, 19: 4421-4427. PMID: 10341243, PMCID: PMC6782598, DOI: 10.1523/jneurosci.19-11-04421.1999.Peer-Reviewed Original Research
1997
Widespread Neuronal Ectopia Associated with Secondary Defects in Cerebrocortical Chondroitin Sulfate Proteoglycans and Basal Lamina in MARCKS-Deficient Mice
Blackshear P, Silver J, Nairn A, Sulik K, Squier M, Stumpo D, Tuttle J. Widespread Neuronal Ectopia Associated with Secondary Defects in Cerebrocortical Chondroitin Sulfate Proteoglycans and Basal Lamina in MARCKS-Deficient Mice. Experimental Neurology 1997, 145: 46-61. PMID: 9184108, DOI: 10.1006/exnr.1997.6475.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalBasement MembraneCerebral CortexChondroitin SulfatesFemaleGene Expression Regulation, DevelopmentalIntracellular Signaling Peptides and ProteinsLamininMaleMembrane ProteinsMiceMice, Mutant StrainsMicroscopy, Electron, ScanningMutationMyristoylated Alanine-Rich C Kinase SubstrateNeurogliaNeuronsPia MaterPregnancyProteinsProteoglycansReticulinSynaptophysinConceptsChondroitin sulfate proteoglycanNeuronal ectopiaBasal laminaSulfate proteoglycanProtein kinase CEmbryonic day 13Basal lamina proteinsReticulin stainingSubarachnoid spaceForebrain commissuresPial membraneDay 13EctopiaGross abnormalitiesRetinal laminationMiceMARCKS deficiencyAbnormalitiesPotential mechanismsNeural substratesMarginal zoneProteolytic destructionKinase CProteoglycansLaminaSite-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding
Huang H, Horiuchi A, Goldberg J, Greengard P, Nairn A. Site-directed mutagenesis of amino acid residues of protein phosphatase 1 involved in catalysis and inhibitor binding. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 3530-3535. PMID: 9108010, PMCID: PMC20473, DOI: 10.1073/pnas.94.8.3530.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1Site-directed mutagenesisActive site residuesOkadaic acidPhosphatase 1Calyculin AMammalian protein phosphatase 1PP-1Site residuesEnzyme activityMutation of residuesAmino acid residuesMechanism of catalysisActive siteInhibitor bindingAcid residuesInhibitory proteinMutationsResiduesMutagenesisDivalent cationsToxinY272Large lossesR221
1992
Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase.
Countaway J, Nairn A, Davis R. Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase. Journal Of Biological Chemistry 1992, 267: 1129-1140. PMID: 1309762, DOI: 10.1016/s0021-9258(18)48406-2.Peer-Reviewed Original ResearchConceptsProtein tyrosine kinase activityKinase activityEGF receptorIntrinsic protein tyrosine kinase activityGrowth factor receptor protein tyrosine kinaseSrc homology 2 (SH2) regionsEpidermal growth factor receptor protein tyrosine kinaseEGF receptor protein tyrosine kinase activityReceptor protein tyrosine kinaseRegulatory phosphorylation sitesEGF-stimulated phosphorylationCalmodulin-dependent protein kinase IIProtein tyrosine kinasesEGF-stimulated endocytosisProtein kinase IICell surface receptorsEpidermal growth factor receptorPhosphorylation sitesBinding of EGFSignal transductionGrowth factor receptorCarboxyl terminusSer1046/7Kinase IIEGF treatment