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
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 interactionsDomainInhibitionInhibition of protein synthesis in cortical neurons during exposure to hydrogen peroxide
Alirezaei M, Marin P, Nairn A, Glowinski J, Prémont J. Inhibition of protein synthesis in cortical neurons during exposure to hydrogen peroxide. Journal Of Neurochemistry 2001, 76: 1080-1088. PMID: 11181828, DOI: 10.1046/j.1471-4159.2001.00105.x.Peer-Reviewed Original ResearchMeSH KeywordsAniline CompoundsAnimalsCalciumCells, CulturedCerebral CortexDose-Response Relationship, DrugEukaryotic Initiation Factor-2Fluorescent DyesHydrogen PeroxideIntracellular FluidMiceNeuronsPeptide Chain Elongation, TranslationalPeptide Elongation Factor 2PhosphorylationProtein BiosynthesisProtein Synthesis InhibitorsProteinsThapsigarginXanthenesConceptsCortical neuronsGlutamate-induced increaseTransient cerebral ischemiaDose-dependent mannerEffects of thapsigarginProtein synthesisCerebral ischemiaReperfusion periodCommon intracellularEEF-2BlockadeTreatmentNeuronsInhibitionThapsigarginIntracellularPhosphorylationSustained releaseIschemiaEIF-2alphaSlow increaseProtein translation
1999
Arginine vasopressin stimulates phosphorylation of aquaporin-2 in rat renal tissue
Nishimoto G, Zelenina M, Li D, Yasui M, Aperia A, Nielsen S, Nairn A. Arginine vasopressin stimulates phosphorylation of aquaporin-2 in rat renal tissue. American Journal Of Physiology 1999, 276: f254-f259. PMID: 9950956, DOI: 10.1152/ajprenal.1999.276.2.f254.Peer-Reviewed Original ResearchConceptsPhosphorylation of AQP2Protein kinase AAquaporin-2Two-dimensional phosphopeptide mappingCAMP-dependent protein kinase AConsensus phosphorylation sitesActivation of PKAPhosphopeptide mappingPhosphorylation sitesMaximal phosphorylationAQP2 phosphorylationKinase APhosphorylationSer256Immunoblot analysis