2023
Mass spectrometry in cerebrospinal fluid uncovers association of glycolysis biomarkers with Alzheimer’s disease in a large clinical sample
de Geus M, Leslie S, Lam T, Wang W, Roux-Dalvai F, Droit A, Kivisakk P, Nairn A, Arnold S, Carlyle B. Mass spectrometry in cerebrospinal fluid uncovers association of glycolysis biomarkers with Alzheimer’s disease in a large clinical sample. Scientific Reports 2023, 13: 22406. PMID: 38104170, PMCID: PMC10725469, DOI: 10.1038/s41598-023-49440-3.Peer-Reviewed Original Research
2001
Auto‐inhibition of Ca2+/calmodulin‐dependent protein kinase II by its ATP‐binding domain
Lengyel I, Nairn A, McCluskey A, Tóth G, Penke B, Rostas J. Auto‐inhibition of Ca2+/calmodulin‐dependent protein kinase II by its ATP‐binding domain. Journal Of Neurochemistry 2001, 76: 1066-1072. PMID: 11181826, DOI: 10.1046/j.1471-4159.2001.00139.x.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBinding SitesCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesDose-Response Relationship, DrugEnzyme ActivationEnzyme InhibitorsPeptide FragmentsPeptidesProtein Structure, TertiaryRatsSubstrate SpecificityConceptsATP-binding domainDependent protein kinase IIProtein kinase IIProtein kinaseCaMPK-IIKinase IICAMP-dependent protein kinaseDependent protein kinaseSubstitution of phenylalaninePhysiological processesKey enzymeAutocamtide-2Position 25Phenylalanine 25Molecular interactionsKinasePeptide fragmentsDependent activityIndependent activityATPEnzymeCrucial roleIntramolecular interactionsDomainInhibition
2000
Letter to the Editor: Backbone 1H, 15N, and 13C resonance assignments of inhibitor-2 – a protein inhibitor of protein phosphatase-1
Huang H, Chen Y, Tsai L, Wang H, Lin F, Horiuchi A, Greengard P, Nairn A, Shiao M, Lin T. Letter to the Editor: Backbone 1H, 15N, and 13C resonance assignments of inhibitor-2 – a protein inhibitor of protein phosphatase-1. Journal Of Biomolecular NMR 2000, 17: 359-360. PMID: 11014604, DOI: 10.1023/a:1008355428294.Peer-Reviewed Original ResearchSevered Molecules Functionally Define the Boundaries of the Cystic Fibrosis Transmembrane Conductance Regulator's Nh2-Terminal Nucleotide Binding Domain
Chan K, Csanády L, Seto-Young D, Nairn A, Gadsby D. Severed Molecules Functionally Define the Boundaries of the Cystic Fibrosis Transmembrane Conductance Regulator's Nh2-Terminal Nucleotide Binding Domain. The Journal Of General Physiology 2000, 116: 163-180. PMID: 10919864, PMCID: PMC2229491, DOI: 10.1085/jgp.116.2.163.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine MonophosphateAnimalsCystic Fibrosis Transmembrane Conductance RegulatorEndoplasmic ReticulumEpitopesFemaleGene DeletionGene ExpressionIon Channel GatingKineticsMembrane PotentialsMolecular Sequence DataMutagenesisOligopeptidesOocytesPatch-Clamp TechniquesPeptide FragmentsPeptidesPrecipitin TestsProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidTransfectionXenopus laevisConceptsR domainCFTR channelsCOOH terminusMature formFull-length CFTRCystic fibrosis transmembrane conductance regulatorAmino acids 590Nucleotide Binding DomainFibrosis transmembrane conductance regulatorExcised patch recordingsChannel activityFamily of ATPRequirement of phosphorylationCFTR channel activityTransmembrane conductance regulatorNBD1 domainSmaller single-channel conductanceCFTR polypeptideTransmembrane domainATP bindingRegulatory domainCassette proteinNBD structuresNBD1Binding domains
1999
Regulation of Neurabin I Interaction with Protein Phosphatase 1 by Phosphorylation †
McAvoy T, Allen P, Obaishi H, Nakanishi H, Takai Y, Greengard P, Nairn A, Hemmings H. Regulation of Neurabin I Interaction with Protein Phosphatase 1 by Phosphorylation †. Biochemistry 1999, 38: 12943-12949. PMID: 10504266, DOI: 10.1021/bi991227d.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1Neurabin IPP1 activityPhosphatase 1Two-hybrid interaction analysisActin-binding proteinsCo-immunoprecipitation experimentsMimic phosphorylationSerine 461Phosphorylated residuesGlutathione S-transferaseOverlay assaysFusion proteinSignaling mechanismGamma isoformsCAMP pathwayPhosphorylationS-transferaseProteinTryptic digestPKARegulationHPLC-MS analysisInteraction analysisS461Characterization of the Neuronal Targeting Protein Spinophilin and Its Interactions with Protein Phosphatase-1 †
Hsieh-Wilson L, Allen P, Watanabe T, Nairn A, Greengard P. Characterization of the Neuronal Targeting Protein Spinophilin and Its Interactions with Protein Phosphatase-1 †. Biochemistry 1999, 38: 4365-4373. PMID: 10194355, DOI: 10.1021/bi982900m.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCell LineDopamine and cAMP-Regulated Phosphoprotein 32HumansMicrofilament ProteinsNerve Tissue ProteinsNeuronsPeptide FragmentsPeptidesPhosphoprotein PhosphatasesPhosphoproteinsProtein Phosphatase 1Protein Structure, TertiaryProteinsRabbitsSequence Homology, Amino AcidConceptsProtein phosphatase 1Ability of spinophilinPhosphatase 1PP1 regulatory subunitClass of proteinsAmino acids 447Cell cycle progressionPP1 activityPentapeptide motifRegulatory subunitCellular processesDeletion analysisDistinct subdomainsSubstrate specificityBinding domainsPhysiological substratesMutational analysisNeuronal proteinsProtein spinophilinCompetition binding assaysHigh-affinity binding domainsDARPP-32SpinophilinPostsynaptic densityBinding assays
1996
Amyloid β Peptide Formation in Cell-free Preparations REGULATION BY PROTEIN KINASE C, CALMODULIN, AND CALCINEURIN*
Desdouits F, Buxbaum J, Desdouits-Magnen J, Nairn A, Greengard P. Amyloid β Peptide Formation in Cell-free Preparations REGULATION BY PROTEIN KINASE C, CALMODULIN, AND CALCINEURIN*. Journal Of Biological Chemistry 1996, 271: 24670-24674. PMID: 8798734, DOI: 10.1074/jbc.271.40.24670.Peer-Reviewed Original ResearchConceptsProtein kinase CAction of PKCCell-free systemIntact cellsKinase CProtein phosphatase calcineurinCell-permeant inhibitorStimulation of PKCSpecific peptide inhibitorPhosphatase calcineurinMolecular mechanismsCalcineurinPeptide inhibitorRegulationShort peptidesCalmodulinCellsBeta peptideInhibitorsPeptide formationPeptidesMajor constituentsPronounced inhibitionCyclosporin ASingle substrate
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
1992
The nature and metabolism of potentially amyloidogenic carboxyl-terminal fragments of the Alzheimer βA4-amyloid precursor protein: Some technical notes
Gandy S, Buxbaum J, Suzuki T, Ramabhadran T, Caporaso G, Nairn A, Greengard P. The nature and metabolism of potentially amyloidogenic carboxyl-terminal fragments of the Alzheimer βA4-amyloid precursor protein: Some technical notes. Neurobiology Of Aging 1992, 13: 601-603. PMID: 1461349, DOI: 10.1016/0197-4580(92)90063-4.Peer-Reviewed Original Research
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
1988
Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity.
Thiel G, Czernik AJ, Gorelick F, Nairn AC, Greengard P. Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 6337-6341. PMID: 2842767, PMCID: PMC281965, DOI: 10.1073/pnas.85.17.6337.Peer-Reviewed Original ResearchConceptsBeta/beta' subunitsAlpha subunitThr-286Beta subunitDependent protein kinase IIProtein kinase IIAutophosphorylation sitesThreonine residuesMajor phosphopeptideNaDodSO4/PAGEPhosphorylated residuesCyanogen bromide peptidesConsensus sequenceKinase IIIndependent activityThermolytic phosphopeptidesPrimary structureGas-phase Edman degradationGeneration of Ca2Edman degradationAutophosphorylationSubunitsThreonine-286Amino acidsAsp-Xaa