2001
Letter to the Editor: Backbone 1H, 15N, and 13C resonance assignments of ARPP-19
Huang H, Chen Y, Horiuchi A, Tsai L, Liu H, Chyan C, Hsieh M, Liu C, Lin F, Greengard P, Nairn A, Shiao M, Lin T. Letter to the Editor: Backbone 1H, 15N, and 13C resonance assignments of ARPP-19. Journal Of Biomolecular NMR 2001, 19: 383-384. PMID: 11370788, DOI: 10.1023/a:1011214512601.Peer-Reviewed Original Research
2000
Drugs of abuse modulate the phosphorylation of ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in the basal ganglia
Caporaso G, Bibb J, Snyder G, Valle C, Rakhilin S, Fienberg A, Hemmings H, Nairn A, Greengard P. Drugs of abuse modulate the phosphorylation of ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in the basal ganglia. Neuropharmacology 2000, 39: 1637-1644. PMID: 10854908, DOI: 10.1016/s0028-3908(99)00230-0.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalBasal GangliaCattleCocaineCorpus StriatumCyclosporineDopamine and cAMP-Regulated Phosphoprotein 32Dopamine Uptake InhibitorsEnzyme InhibitorsIllicit DrugsMarine ToxinsMethamphetamineMiceMice, Inbred C57BLMice, TransgenicNerve Tissue ProteinsOkadaic AcidOxazolesPhosphoproteinsPhosphorylationRats
1997
Characterization of novel calmodulin-binding peptides with distinct inhibitory effects on calmodulin-dependent enzymes
NEVALAINEN L, AOYAMA T, IKURA M, CRIVICI A, Hong Y, CHUA N, NAIRN A. Characterization of novel calmodulin-binding peptides with distinct inhibitory effects on calmodulin-dependent enzymes. Biochemical Journal 1997, 321: 107-115. PMID: 9003408, PMCID: PMC1218043, DOI: 10.1042/bj3210107.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCalmodulinCalmodulin-Binding ProteinsCattleCyclic Nucleotide Phosphodiesterases, Type 1Magnetic Resonance SpectroscopyMaleNeurosporaPeptide MappingPhosphoric Diester HydrolasesSpectrometry, FluorescenceTestis
1996
Inhibition of Tumor Necrosis Factor Signal Transduction in Endothelial Cells by Dimethylaminopurine*
Marino M, Dunbar J, Wu L, Ngaiza J, Han H, Guo D, Matsushita M, Nairn A, Zhang Y, Kolesnick R, Jaffe E, Donner D. Inhibition of Tumor Necrosis Factor Signal Transduction in Endothelial Cells by Dimethylaminopurine*. Journal Of Biological Chemistry 1996, 271: 28624-28629. PMID: 8910494, DOI: 10.1074/jbc.271.45.28624.Peer-Reviewed Original ResearchMeSH KeywordsAdenineAnimalsCattleEndothelium, VascularEnzyme InhibitorsEukaryotic Initiation Factor-4EHistaminePeptide Elongation Factor 2Peptide Elongation FactorsPeptide Initiation FactorsPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene Proteins c-rafSignal TransductionTumor Necrosis Factor-alphaConceptsBovine aortic endothelial cellsElongation factor 2Distinct signal transduction cascadesEukaryotic initiation factor 4ETNF signal transduction pathwayEF-2 phosphorylationC-Jun N-terminal kinaseSignal transduction cascadeInitiation factor 4EProtein kinase activitySignal transduction pathwaysEndothelial cellsN-terminal kinaseTNF actionPhosphorylation cascadeEIF-4ESignal transductionTransduction cascadeTransduction pathwaysResponse of BAECsJun-B expressionKinase activityProtein synthesisPhosphorylationCell types
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 regulatorImmunochemical localization of calcium/calmodulin‐dependent protein kinase I
Picciotto M, Zoli M, Bertuzzi G, Nairn A. Immunochemical localization of calcium/calmodulin‐dependent protein kinase I. Synapse 1995, 20: 75-84. PMID: 7624832, DOI: 10.1002/syn.890200111.Peer-Reviewed Original ResearchConceptsKinase IProtein kinase ICaM kinase INon-neuronal tissuesImmunoreactive speciesCalmodulin-dependent protein kinase IGlutathione S-transferase fusion proteinCalcium/calmodulin-dependent protein kinase IRat brainDependent protein kinase ISubcellular fractionation studiesRecombinant kinasesRat brain enzymeNeuronal cell bodiesCytosolic localizationProtein kinaseMultiple immunoreactive speciesMajor immunoreactive speciesFusion proteinMultiple neuronal processesWidespread cellMajor immunoreactive bandRat cDNAPrimary structureSynapsin I.Phosphorylation of DARPP-32, a Dopamine- and cAMP-regulated Phosphoprotein, by Casein Kinase I in Vitro and in Vivo *
Desdouits F, Cohen D, Nairn A, Greengard P, Girault J. Phosphorylation of DARPP-32, a Dopamine- and cAMP-regulated Phosphoprotein, by Casein Kinase I in Vitro and in Vivo *. Journal Of Biological Chemistry 1995, 270: 8772-8778. PMID: 7721783, DOI: 10.1074/jbc.270.15.8772.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCasein KinasesCattleCorpus StriatumCyclic AMPDNA PrimersDopamineDopamine and cAMP-Regulated Phosphoprotein 32Electrophoresis, Polyacrylamide GelHumansMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsNeuronsPeptide MappingPhosphoproteinsPhosphorylationProtein KinasesRabbitsRatsSubstantia NigraConceptsCasein kinase IProtein phosphatase 1Kinase ISer-137Phosphatase 1Ser-189DARPP-32CAMP-dependent protein kinasePhosphatase-1 inhibitorStoichiometry of phosphorylationSite-directed mutagenesisSpecific cell populationsProtein kinaseProtein sequencingSeryl residuesAcidic residuesThr-34PhosphorylationPhosphate/Presence of SDSChoroid plexus epithelial cellsResiduesCell populationsElectrophoretic mobilityEpithelial cells
1994
Ca2+/Calmodulin-Dependent Protein Kinase V and I May Form a Family of Isoforms
Ito T, Yokokura H, Nairn A, Nimura Y, Hidaka H. Ca2+/Calmodulin-Dependent Protein Kinase V and I May Form a Family of Isoforms. Biochemical And Biophysical Research Communications 1994, 201: 1561-1566. PMID: 8024601, DOI: 10.1006/bbrc.1994.1882.Peer-Reviewed Original Research
1993
Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas
Mitsui K, Brady M, Palfrey H, Nairn A. Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas. Journal Of Biological Chemistry 1993, 268: 13422-13433. PMID: 8514778, DOI: 10.1016/s0021-9258(19)38667-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesCalmodulinCattleChromatography, GelElectrophoresis, Polyacrylamide GelElongation Factor 2 KinaseHeat-Shock ProteinsMolecular Sequence DataPancreasPeptide Elongation Factor 2Peptide Elongation FactorsPeptide MappingPhosphoproteinsPhosphorylationProtein KinasesRabbitsRatsReticulocytesSubstrate SpecificityConceptsEukaryotic elongation factor 2CaM kinase IIICalmodulin-dependent protein kinase IIIProtein kinase IIIKinase IIIProtein kinaseRabbit reticulocytesCAMP-dependent protein kinaseYeast EF-2Heat shock protein Hsp90Novel protein kinaseElongation factor 2Amino acid sequencingPhosphopeptide mappingSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisProtein Hsp90Catalytic subunitSulfate-polyacrylamide gel electrophoresisSeryl residuesMajor polypeptidesSubstrate ATPHsp90Factor 2Gel electrophoresis
1992
MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium–calmodulin
Hartwig J, Thelen M, Resen A, Janmey P, Nairn A, Aderem A. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium–calmodulin. Nature 1992, 356: 618-622. PMID: 1560845, DOI: 10.1038/356618a0.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAmino Acid SequenceAnimalsBrainCalciumCalmodulinCattleCross-Linking ReagentsHomeostasisIntracellular Signaling Peptides and ProteinsKineticsMembrane ProteinsMicroscopy, ElectronMolecular Sequence DataMusclesMyristoylated Alanine-Rich C Kinase SubstratePhosphorylationProtein Kinase CProteinsRabbitsTime FactorsConceptsProtein kinase CPlasma membraneCalcium-calmodulinKinase CSignal transduction pathwaysPKC signal transduction pathwayActin filament crosslinking proteinActin cytoskeletonActin assemblyTransduction pathwaysMARCKS proteinFilamentous actinCrosslinking activitySpecific substratesSubstrates bindMARCKSCell morphologyProteinPhosphorylationActinMembraneCytoskeletonCalmodulinCytoplasmBinds
1990
Amiloride analogs induce the phosphorylation of elongation factor-2 in vascular endothelial cells.
Demolle D, Lecomte M, Boutherin-Falson O, Cragoe E, Nairn A, Boeynaems J. Amiloride analogs induce the phosphorylation of elongation factor-2 in vascular endothelial cells. Molecular Pharmacology 1990, 37: 827-32. PMID: 2359404.Peer-Reviewed Original ResearchConceptsElongation factor 2Protein synthesisFactor 2Rabbit reticulocyte lysateCell-free systemBovine aortic endothelial cellsDependent phosphorylationReticulocyte lysateEndothelial cellsAmiloride analoguesPhosphorylationSimilar MrCytosolic pHVascular endothelial cellsProteinAnalogues of amilorideAortic endothelial cellsPotent inhibitorInhibitory effectAntiportCellsEIPAAmilorideATPLysates
1988
Purification and characterization of PCPP‐260: A Purkinje cell‐enriched cyclic amp‐regulated membrane phosphoprotein of Mr 260,000
Weeks G, Picciotto M, Nairn A, Walaas S, Greengard P. Purification and characterization of PCPP‐260: A Purkinje cell‐enriched cyclic amp‐regulated membrane phosphoprotein of Mr 260,000. Synapse 1988, 2: 89-96. PMID: 2844000, DOI: 10.1002/syn.890020112.Peer-Reviewed Original ResearchConceptsCAMP-dependent protein kinaseMembrane proteinsProtein kinaseN-lauryl sarcosineIntegral membrane proteinsMajor tryptic phosphopeptidesPhosphoamino acid analysisTotal membrane proteinSodium dodecyl sulfate-polyacrylamide gel electrophoresisMembrane phosphoproteinDodecyl sulfate-polyacrylamide gel electrophoresisTryptic phosphopeptidesSulfate-polyacrylamide gel electrophoresisPossible functional roleProminent proteinsAlpha-methyl mannosideParticulate fractionMammalian cerebellumFunctional roleProteinPeptide mappingConcanavalin A-agaroseGel electrophoresisAcid analysisA-agarose
1986
Protein phosphorylation in cultured endothelial cells
Mackie K, Lai Y, Nairn A, Greengard P, Pitt B, Lazo J. Protein phosphorylation in cultured endothelial cells. Journal Of Cellular Physiology 1986, 128: 367-374. PMID: 3745280, DOI: 10.1002/jcp.1041280304.Peer-Reviewed Original ResearchConceptsCalcium/calmodulin-dependent protein kinaseCalmodulin-dependent protein kinaseCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseProtein kinase activityProtein kinaseKinase activityCyclic GMP-dependent protein kinase activityRespective substrate proteinsProtein phosphorylation systemsProtein kinase CSubstrate proteinsProtein phosphorylationPhosphorylation systemEndothelial cellsNumerous substratesTyrosine kinaseKinase CPulmonary artery endothelial cellsKinaseCultured endothelial cellsArtery endothelial cellsSimilar culture conditionsCulture conditionsCells