2001
TARPP, a novel protein that accompanies TCR gene rearrangement and thymocyte education
Kisielow J, Nairn A, Karjalainen K. TARPP, a novel protein that accompanies TCR gene rearrangement and thymocyte education. European Journal Of Immunology 2001, 31: 1141-1149. PMID: 11298339, DOI: 10.1002/1521-4141(200104)31:4<1141::aid-immu1141>3.0.co;2-r.Peer-Reviewed Original ResearchAgingAmino Acid SequenceAnimalsAntibodiesBase SequenceCD3 ComplexCell DifferentiationCell LineageCells, CulturedCloning, MolecularDown-RegulationFlow CytometryGene Expression ProfilingGene Expression Regulation, DevelopmentalGene Rearrangement, T-LymphocyteMiceMice, Inbred C57BLMolecular Sequence DataMolecular WeightPhosphoproteinsProtein Phosphatase 1Receptors, Antigen, T-CellRNA, MessengerSignal TransductionThymus Gland
2000
NMDA receptor-mediated control of protein synthesis at developing synapses
Scheetz A, Nairn A, Constantine-Paton M. NMDA receptor-mediated control of protein synthesis at developing synapses. Nature Neuroscience 2000, 3: 211-216. PMID: 10700251, DOI: 10.1038/72915.Peer-Reviewed Original ResearchMeSH Keywords2-Amino-5-phosphonovalerateAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCycloheximideElectrophoresis, Gel, Two-DimensionalGlutamic AcidIsoelectric PointMolecular WeightN-MethylaspartatePeptide Elongation Factor 2PhosphorylationPrecipitin TestsProtein BiosynthesisProteinsRatsReceptors, N-Methyl-D-AspartateRetinal Ganglion CellsSuperior ColliculiSynapsesSynaptosomesTime FactorsConceptsNMDAR activationReceptor activationN-methyl-D-aspartate (NMDA) receptor activationActivity-dependent synaptic changesEukaryotic elongation factor 2Receptor-mediated controlSynaptic protein synthesisEEF2 phosphorylationProtein synthesisSuperior colliculiYoung ratsDependent kinase IISynaptic changesLow dosesTotal protein synthesisII synthesisFactor 2Overall protein synthesisActivationElongation factor 2Kinase IIPhosphorylation
1999
Characterization of the Inhibition of Protein Phosphatase-1 by DARPP-32 and Inhibitor-2*
Huang H, Horiuchi A, Watanabe T, Shih S, Tsay H, Li H, Greengard P, Nairn A. Characterization of the Inhibition of Protein Phosphatase-1 by DARPP-32 and Inhibitor-2*. Journal Of Biological Chemistry 1999, 274: 7870-7878. PMID: 10075680, DOI: 10.1074/jbc.274.12.7870.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAnimalsCatalytic DomainDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsHumansMolecular Sequence DataMolecular WeightMuscle ProteinsMutagenesis, Site-DirectedNerve Tissue ProteinsPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Phosphatase 1ProteinsRabbitsSerineThreonine
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 ResearchMeSH KeywordsAnimalsBrainCalcium-Calmodulin-Dependent Protein KinasesCattleIsoenzymesMolecular WeightPhosphorylationRatsRecombinant ProteinsCorrelation between protein kinase C binding proteins and substrates in REF52 cells.
Hyatt S, Liao L, Aderem A, Nairn A, Jaken S. Correlation between protein kinase C binding proteins and substrates in REF52 cells. Molecular Cancer Research 1994, 5: 495-502. PMID: 8049156.Peer-Reviewed Original ResearchMeSH KeywordsBlotting, WesternCalmodulin-Binding ProteinsCell LineCell Line, TransformedCell Transformation, NeoplasticDown-RegulationIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane ProteinsMolecular WeightMyristoylated Alanine-Rich C Kinase SubstratePhosphatidylserinesPhosphorylationProtein BindingProtein DenaturationProtein Kinase CProtein Kinase C-alphaProteinsSolubilityConceptsProtein kinase CREF52 cellsPKC substrateKinase CBinding proteinProperties of PKCCalmodulin-Sepharose chromatographyBlot overlay assaysProteins/substratesMajor PKC substrateMajor binding proteinPhosphorylation assaysBlot overlayOverlay assaysTarget proteinsBasal phosphorylationProteinCellsSufficient affinityMARCKSAssaysPhosphorylationSubstratePhenotypeSV40
1991
Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart.
Neumann J, Gupta R, Schmitz W, Scholz H, Nairn A, Watanabe A. Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart. Circulation Research 1991, 69: 1450-1457. PMID: 1659500, DOI: 10.1161/01.res.69.6.1450.Peer-Reviewed Original ResearchConceptsPhosphatase inhibitor-1Protein phosphatase inhibitor-1Type 1 phosphatase activityPhosphatase activityInhibitor-1Sodium dodecyl sulfate gelsDodecyl sulfate gelsIsoproterenol-induced phosphorylationSulfate gelsProteinRadioactive proteinsPhosphorylationPmol 32P/KdPhysiological bufferAntiserumActivityIndirect assayConcentrations of isoproterenolAgonist isoproterenolActivationAssaysVivoIntact heartCAMPIdentification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator.
Marshall J, Martin K, Picciotto M, Hockfield S, Nairn A, Kaczmarek L. Identification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator. Journal Of Biological Chemistry 1991, 266: 22749-22754. PMID: 1718999, DOI: 10.1016/s0021-9258(18)54631-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCell MembraneCloning, MolecularCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDNADogfishHumansImmunoenzyme TechniquesMembrane ProteinsMolecular Sequence DataMolecular WeightProtein KinasesRectumSebaceous GlandsSequence Homology, Nucleic AcidSubstrate SpecificityConceptsCystic fibrosis transmembrane conductance regulatorHuman cystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorDogfish proteinRectal glandConductance regulatorPutative substrate sitesCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseMajor phosphorylation siteCyclic AMP-dependent protein phosphorylationApical plasma membraneAmino acid sequenceStudy of regulationPhosphorylation sitesProtein phosphorylationCDNA clonesProtein kinaseSimilar molecular massCFTR sequencePlasma membraneAcid sequenceImmunolocalization studiesMolecular mass
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
1987
Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2.
Nairn A, Palfrey H. Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2. Journal Of Biological Chemistry 1987, 262: 17299-17303. PMID: 3693353, DOI: 10.1016/s0021-9258(18)45377-x.Peer-Reviewed Original ResearchConceptsProtein kinase IIIElongation factor 2Kinase IIIMammalian cellsThreonine residuesCalmodulin-dependent protein kinase IIIDependent protein kinase IIIPhosphorylated EF-2Endogenous GTPase activityAmino acid sequencingSpecies of MrFactor 2Inhibits protein synthesisTryptic phosphopeptidesGTPase activityNucleic acid sequencingCytoplasmic localizationMajor substrateN-terminalPeptidyl-tRNATerminal sequenceSalt-washed ribosomesProtein synthesisEF-1Thr-AspCa2+/calmodulin-dependent protein kinase II: identification of autophosphorylation sites responsible for generation of Ca2+/calmodulin-independence.
Lai Y, Nairn AC, Gorelick F, Greengard P. Ca2+/calmodulin-dependent protein kinase II: identification of autophosphorylation sites responsible for generation of Ca2+/calmodulin-independence. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 5710-5714. PMID: 3475699, PMCID: PMC298932, DOI: 10.1073/pnas.84.16.5710.Peer-Reviewed Original ResearchRapid activation of calmodulin-dependent protein kinase III in mitogen-stimulated human fibroblasts. Correlation with intracellular Ca2+ transients.
Palfrey H, Nairn A, Muldoon L, Villereal M. Rapid activation of calmodulin-dependent protein kinase III in mitogen-stimulated human fibroblasts. Correlation with intracellular Ca2+ transients. Journal Of Biological Chemistry 1987, 262: 9785-9792. PMID: 3496338, DOI: 10.1016/s0021-9258(18)48002-7.Peer-Reviewed Original ResearchThe cyclic nucleotide-dependent phosphorylation of aortic smooth muscle membrane proteins
Parks T, Nairn A, Greengard P, Jamieson J. The cyclic nucleotide-dependent phosphorylation of aortic smooth muscle membrane proteins. Archives Of Biochemistry And Biophysics 1987, 255: 361-371. PMID: 3036005, DOI: 10.1016/0003-9861(87)90404-8.Peer-Reviewed Original ResearchConceptsG-kinaseA-kinaseGs proteinMembrane proteinsCyclic nucleotide-dependent phosphorylationCAMP-dependent protein kinase activityCGMP-dependent protein kinaseKinase catalytic subunitEndogenous A-kinaseProtein kinase activityPeptide mappingTwo-dimensional peptide mappingMembrane-bound formCyclic nucleotidesHigh-salt washMuscle membrane proteinsCatalytic subunitFunctional homologyProtein kinasePhosphorylation stateCytosolic formKinase activitySalt washIntracellular concentrationSoluble form
1985
Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues.
Nairn A, Bhagat B, Palfrey H. Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 7939-7943. PMID: 3906654, PMCID: PMC390885, DOI: 10.1073/pnas.82.23.7939.Peer-Reviewed Original ResearchConceptsCaM-dependent protein kinaseCaM kinase IIIKinase IIIProtein kinaseMammalian tissuesCalmodulin-dependent protein kinase IIIProtein kinase IIIDependent protein kinaseProtein phosphorylation systemsWidespread tissue distributionTotal cytosolic proteinAnimal cellsPhosphorylation systemSubstrate specificityCytosolic proteinsMyosin light chainMajor substrateKinaseProteinSynapsin IPoor substrateCell linesPhosphorylase bMajor MrPolyclonal antibodies
1983
Cyclic Nucleotide‐Dependent Protein Kinases and Some Major Substrates in the Rat Cerebellum After Neonatal X‐Irradiation
Dolphin A, Detre J, Schlichter D, Nairn A, Yeh H, Woodward D, Greengard P. Cyclic Nucleotide‐Dependent Protein Kinases and Some Major Substrates in the Rat Cerebellum After Neonatal X‐Irradiation. Journal Of Neurochemistry 1983, 40: 577-581. PMID: 6296321, DOI: 10.1111/j.1471-4159.1983.tb11321.x.Peer-Reviewed Original Research
1980
THE RELATIONSHIP OF THE STRUCTURE TO THE FUNCTION OF CALMODULIN IN THE MYOSIN LIGHT CHAIN KINASE SYSTEM
Nairn A, Grand R, Wall C, Perry S. THE RELATIONSHIP OF THE STRUCTURE TO THE FUNCTION OF CALMODULIN IN THE MYOSIN LIGHT CHAIN KINASE SYSTEM. Annals Of The New York Academy Of Sciences 1980, 356: 413-414. PMID: 6940506, DOI: 10.1111/j.1749-6632.1980.tb29653.x.Peer-Reviewed Original Research