2006
2‐Deoxyglucose and NMDA inhibit protein synthesis in neurons and regulate phosphorylation of elongation factor‐2 by distinct mechanisms
Maus M, Torrens Y, Gauchy C, Bretin S, Nairn A, Glowinski J, Premont J. 2‐Deoxyglucose and NMDA inhibit protein synthesis in neurons and regulate phosphorylation of elongation factor‐2 by distinct mechanisms. Journal Of Neurochemistry 2006, 96: 815-824. PMID: 16405506, DOI: 10.1111/j.1471-4159.2005.03601.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntimetabolitesBlotting, WesternCalciumCarbonyl Cyanide m-Chlorophenyl HydrazoneCells, CulturedCerebral CortexDeoxyglucoseDose-Response Relationship, DrugDrug InteractionsEmbryo, MammalianEnzyme InhibitorsExcitatory Amino Acid AgonistsIonophoresLeucineMiceModels, BiologicalNeuronsN-MethylaspartateOligomycinsPeptide Elongation Factor 2PhosphorylationProtein KinasesProtein Synthesis InhibitorsPyruvic AcidSodium AzideTime FactorsTOR Serine-Threonine KinasesTritiumConceptsCortical neuronsExcitatory amino acid releaseImine hydrogen maleateNMDA receptor antagonistAMP kinaseAmino acid releaseNeuronal protein synthesisCytosolic free Ca2Protein synthesisCerebral ischaemiaReceptor antagonistBrain damageNeuronal metabolismMetabolic impairmentNMDADistinct mechanismsCytosolic Ca2NeuronsMetabolic deprivationAcid releaseSecondary releaseProtein synthesis inhibitionSynthesis inhibitionElongation factor eEF-2ATP levels
1999
The expression of Ca2+/calmodulin-dependent protein kinase I in rat retina is regulated by light stimulation
Tsumura T, Murata A, Yamaguchi F, Sugimoto K, Hasegawa E, Hatase O, Nairn A, Tokuda M. The expression of Ca2+/calmodulin-dependent protein kinase I in rat retina is regulated by light stimulation. Vision Research 1999, 39: 3165-3173. PMID: 10615488, DOI: 10.1016/s0042-6989(99)00063-2.Peer-Reviewed Original Research
1995
Cystic Fibrosis Transmembrane Conductance Regulator Is Found Within Brain Ventricular Epithelium and Choroid Plexus
Hincke M, Nairn A, Staines W. Cystic Fibrosis Transmembrane Conductance Regulator Is Found Within Brain Ventricular Epithelium and Choroid Plexus. Journal Of Neurochemistry 1995, 64: 1662-1668. PMID: 7534334, DOI: 10.1046/j.1471-4159.1995.64041662.x.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorConductance regulatorCystic fibrosis gene productBrain Ventricular EpitheliumCyclic AMP-dependent phosphorylationGene productsCFTR proteinFine punctaChloride transportersCl- channelsCyclic AMP-elevating agentsEpendymal functionWestern blottingRegulatorVentricular epitheliumPhosphorylationChoroid plexusProteinTransportersRodent brainPunctaRegulationMicrodissection
1994
Correlation 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
1992
Increased phosphorylation of elongation factor 2 in Alzheimer's disease
Johnson G, Gotlib J, Haroutunian V, Bierer L, Nairn A, Merril C, Wallace W. Increased phosphorylation of elongation factor 2 in Alzheimer's disease. Brain Research 1992, 15: 319-326. PMID: 1331687, DOI: 10.1016/0169-328x(92)90124-t.Peer-Reviewed Original ResearchConceptsDisease brainAlzheimer's diseaseAlzheimer's disease brainFactor 2AD homogenatesAD tissueElongation factor 2Brain homogenatesSame brainDiseaseVariant isoformsProtein synthesisPhosphorylated formInhibits protein synthesisBrainUnaffected areasHomogenatesAcidic isoformsPhosphorylationGene expressionEF-2
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 heartCAMP
1989
Insulin rapidly induces the biosynthesis of elongation factor 2
Levenson R, Nairn A, Blackshear P. Insulin rapidly induces the biosynthesis of elongation factor 2. Journal Of Biological Chemistry 1989, 264: 11904-11911. PMID: 2663845, DOI: 10.1016/s0021-9258(18)80152-1.Peer-Reviewed Original ResearchConceptsElongation factor 2EF-2Overall protein synthesisProtein synthesisProtein translation apparatusEukaryotic elongation factor 2Two-dimensional gel electrophoresisHuman insulin receptorNIH 3T3 cellsFactor 2Translation apparatusMature speciesMRNA translationActinomycin D. ThusRNA transcription inhibitorSuch proteinsIndividual proteinsInsulin inductionPreferential expressionPrecursor formInsulin receptorSerum deprivationProteinGel autoradiographsGel electrophoresis