1995
Immunochemical 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
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
1991
[23] Production of phosphorylation state-specific antibodies
Jczernik A, Girault J, Nairn A, Chen J, Snyder G, Kebabian J, Greengard P. [23] Production of phosphorylation state-specific antibodies. Methods In Enzymology 1991, 201: 264-283. PMID: 1943769, DOI: 10.1016/0076-6879(91)01025-w.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodiesAntibodies, MonoclonalAntibody SpecificityCross ReactionsElectrophoresis, Polyacrylamide GelEnzyme-Linked Immunosorbent AssayGTP-Binding ProteinsImmunoblottingKineticsMolecular Sequence DataPeptidesPhosphopeptidesPhosphoproteinsPhosphorylationRabbitsRecombinant ProteinsSynapsins
1990
Phosphorylation of connexin 32, a hepatocyte gap‐junction protein, by cAMP‐dependent protein kinase, protein kinase C and Ca2+/calmodulin‐dependent protein kinase II
SAEZ J, NAIRN A, CZERNIK A, SPRAY D, HERTZBERG E, GREENGARD P, BENNETT M. Phosphorylation of connexin 32, a hepatocyte gap‐junction protein, by cAMP‐dependent protein kinase, protein kinase C and Ca2+/calmodulin‐dependent protein kinase II. The FEBS Journal 1990, 192: 263-273. PMID: 2170122, DOI: 10.1111/j.1432-1033.1990.tb19223.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesConnexinsElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelFemaleLiverMembrane ProteinsMolecular Sequence DataPeptide FragmentsPeptidesPhosphopeptidesPhosphorylationProtein Kinase CProtein KinasesRatsRats, Inbred StrainsConceptsProtein kinase CCAMP-dependent protein kinaseDependent protein kinase IIGap junction proteinPhosphopeptide mappingProtein kinaseSeryl residuesProtein kinase IICAMP-PKKinase IIKinase CCell typesConnexin 32PK IIPhosphoamino acid analysisDifferent gap junction proteinsSites of phosphorylationPhosphorylated synthetic peptideCAMP-PK activityGap junctionsAmino acid sequencingActivation of PKCDifferent cell typesPhysiological substratesSynthetic peptides
1989
Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms
Ivar Walaas S, Nairn A. Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms. Journal Of Molecular Neuroscience 1989, 1: 117-127. PMID: 2561875, DOI: 10.1007/bf02896895.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino AcidsAnimalsBrainCalcium-Calmodulin-Dependent Protein KinasesElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelMicrotubule-Associated ProteinsOrgan SpecificityPeptide MappingPhosphopeptidesPhosphorylationProtein Kinase CProtein KinasesRatsConceptsCalcium/phospholipid-dependent protein kinasePhospholipid-dependent protein kinaseCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinaseCalcium/calmodulinProtein kinase IIKinase IICyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCommon phosphorylation sitesOnly serine residuesProtein 2Cyclic AMPMultisite phosphorylationThreonine residuesPhosphorylation sitesSerine residuesPhosphorylation systemPhosphorylation mechanismCytoskeletal proteinsMAP-2KinasePeptide mapsDistinct sites
1988
DARPP‐32 and Phosphatase Inhibitor‐1, Two Structurally Related Inhibitors of Protein Phosphatase‐1, Are Both Present in Striatonigral Neurons
Nairn A, Hemmings H, Walaas S, Greengard P. DARPP‐32 and Phosphatase Inhibitor‐1, Two Structurally Related Inhibitors of Protein Phosphatase‐1, Are Both Present in Striatonigral Neurons. Journal Of Neurochemistry 1988, 50: 257-262. PMID: 3335843, DOI: 10.1111/j.1471-4159.1988.tb13258.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBasal GangliaCarrier ProteinsCorpus StriatumDopamine and cAMP-Regulated Phosphoprotein 32Electrophoresis, Polyacrylamide GelIntracellular Signaling Peptides and ProteinsKainic AcidMaleMusclesNerve Tissue ProteinsNeuronsPhosphoproteinsPhosphorylationProteinsRatsRats, Inbred StrainsSubstantia NigraConceptsPhosphatase inhibitor-1Protein phosphatase 1Phosphatase 1DARPP-32Inhibitor-1Striatonigral neuronsSubstantia nigraKainic acidStriatonigral fibersBiochemical propertiesRelated inhibitorsSpecific neuronal subpopulationsIpsilateral substantia nigraBovine caudate nucleusSpecific activityStriatal neuronsNeuronal localizationRat neostriatumNeuronal subpopulationsRat brainCaudate nucleusLesioned neostriatumNeostriatumNeuronsInhibitors
1980
The preparation of calmodulins from barley (Hordeum sp.) and basidiomycete fungi
Grand R, Nairn A, Perry S. The preparation of calmodulins from barley (Hordeum sp.) and basidiomycete fungi. Biochemical Journal 1980, 185: 755-760. PMID: 6248033, PMCID: PMC1161454, DOI: 10.1042/bj1850755.Peer-Reviewed Original ResearchMeSH Keywords3',5'-Cyclic-AMP PhosphodiesterasesAmino AcidsBasidiomycotaCalcium-Binding ProteinsCalmodulinElectrophoresis, Polyacrylamide GelEnzyme ActivationHordeumMyosin-Light-Chain KinasePlantsProtein KinasesTroponinConceptsRabbit skeletal muscle troponin ICalmodulin-like proteinPresence of Ca2Myosin light chain kinaseSkeletal muscle troponin IMammalian proteinsFungal calmodulinsLight chain kinaseMammalian calmodulinBovine brain calmodulinHigher fungiAmino acid analysisEscherichia coliCalmodulinProteinFungiE. coliAcid analysisBrain calmodulinElectrophoretic mobilityBarleyPolyacrylamide gelsM ureaColiNumber of differences