2001
Mechanisms for Increased Levels of Phosphorylation of Elongation Factor-2 during Hibernation in Ground Squirrels †
Chen Y, Matsushita M, Nairn A, Damuni Z, Cai D, Frerichs K, Hallenbeck J. Mechanisms for Increased Levels of Phosphorylation of Elongation Factor-2 during Hibernation in Ground Squirrels †. Biochemistry 2001, 40: 11565-11570. PMID: 11560506, DOI: 10.1021/bi010649w.Peer-Reviewed Original ResearchConceptsEukaryotic elongation factor 2EEF-2 phosphorylationElongation factor 2Elongation phaseEEF-2 kinase activityProtein phosphatase 2AGround squirrelsLevel of phosphorylationFactor 2Phosphatase 2ACellular functionsCatalytic subunitUncharacterized mechanismKinase activityInhibitor 2Protein synthesisPhosphorylationPP2AHibernating animalsActive animalsHibernatorsReversible mechanismSevere reductionSquirrelsHibernation
1999
Modulation of GT-1 DNA-binding activity by calcium-dependent phosphorylation
Maréchal E, Hiratsuka K, Delgado J, Nairn A, Qin J, Chait B, Chua N. Modulation of GT-1 DNA-binding activity by calcium-dependent phosphorylation. Plant Molecular Biology 1999, 40: 373-386. PMID: 10437822, DOI: 10.1023/a:1006131330930.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsArabidopsisBase SequenceBinding SitesCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesDNA PrimersDNA-Binding ProteinsIn Vitro TechniquesMolecular Sequence DataNuclear ProteinsPhosphorylationPlants, ToxicRatsRecombinant ProteinsSequence Homology, Amino AcidSubstrate SpecificityTranscription FactorsConceptsDNA-binding activityCalcium-dependent phosphorylationGene expressionMolecular switchGT-1Analysis of mutantsDNA-binding proteinsLight-grown plantsPost-translational modificationsCalf intestine phosphataseCalcium/calmodulin kinasePhosphorylatable residuesCasein kinaseGene activationMass spectrometry analysisPromoter sequencesDNA bindingKinase activityBoxIICalmodulin kinasePhosphorylationHGT-1Novo synthesisDephosphorylationSpectrometry analysis
1996
Inhibition of Tumor Necrosis Factor Signal Transduction in Endothelial Cells by Dimethylaminopurine*
Marino M, Dunbar J, Wu L, Ngaiza J, Han H, Guo D, Matsushita M, Nairn A, Zhang Y, Kolesnick R, Jaffe E, Donner D. Inhibition of Tumor Necrosis Factor Signal Transduction in Endothelial Cells by Dimethylaminopurine*. Journal Of Biological Chemistry 1996, 271: 28624-28629. PMID: 8910494, DOI: 10.1074/jbc.271.45.28624.Peer-Reviewed Original ResearchMeSH KeywordsAdenineAnimalsCattleEndothelium, VascularEnzyme InhibitorsEukaryotic Initiation Factor-4EHistaminePeptide Elongation Factor 2Peptide Elongation FactorsPeptide Initiation FactorsPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene Proteins c-rafSignal TransductionTumor Necrosis Factor-alphaConceptsBovine aortic endothelial cellsElongation factor 2Distinct signal transduction cascadesEukaryotic initiation factor 4ETNF signal transduction pathwayEF-2 phosphorylationC-Jun N-terminal kinaseSignal transduction cascadeInitiation factor 4EProtein kinase activitySignal transduction pathwaysEndothelial cellsN-terminal kinaseTNF actionPhosphorylation cascadeEIF-4ESignal transductionTransduction cascadeTransduction pathwaysResponse of BAECsJun-B expressionKinase activityProtein synthesisPhosphorylationCell types
1992
Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase.
Countaway J, Nairn A, Davis R. Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase. Journal Of Biological Chemistry 1992, 267: 1129-1140. PMID: 1309762, DOI: 10.1016/s0021-9258(18)48406-2.Peer-Reviewed Original ResearchConceptsProtein tyrosine kinase activityKinase activityEGF receptorIntrinsic protein tyrosine kinase activityGrowth factor receptor protein tyrosine kinaseSrc homology 2 (SH2) regionsEpidermal growth factor receptor protein tyrosine kinaseEGF receptor protein tyrosine kinase activityReceptor protein tyrosine kinaseRegulatory phosphorylation sitesEGF-stimulated phosphorylationCalmodulin-dependent protein kinase IIProtein tyrosine kinasesEGF-stimulated endocytosisProtein kinase IICell surface receptorsEpidermal growth factor receptorPhosphorylation sitesBinding of EGFSignal transductionGrowth factor receptorCarboxyl terminusSer1046/7Kinase IIEGF treatment
1990
Nerve Growth Factor‐Induced Down‐Regulation of Calmodulin‐Dependent Protein Kinase III in PC12 Cells Involves Cyclic AMP‐Dependent Protein Kinase
Brady M, Nairn A, Wagner J, Palfrey H. Nerve Growth Factor‐Induced Down‐Regulation of Calmodulin‐Dependent Protein Kinase III in PC12 Cells Involves Cyclic AMP‐Dependent Protein Kinase. Journal Of Neurochemistry 1990, 54: 1034-1039. PMID: 1689374, DOI: 10.1111/j.1471-4159.1990.tb02354.x.Peer-Reviewed Original ResearchConceptsWild-type cellsCalmodulin-dependent protein kinase IIICAMP-dependent protein kinase activityProtein kinase IIIProtein kinase activityEpidermal growth factorKinase IIIKinase activityA126-1B2 cellsCyclic AMP-dependent protein kinaseAMP-dependent protein kinasePC12 cellsNerve growth factorMutant PC12 cell lineElongation factor 2Growth factorAbility of NGFPC12 cell lineEffects of NGFProtein kinaseNGF additionA126-1B2Down regulationCell linesFactor 2
1988
Protein kinases 1988: a current perspective
Blackshear P, Nairn A, Kuo J. Protein kinases 1988: a current perspective. The FASEB Journal 1988, 2: 2957-2969. PMID: 2972578, DOI: 10.1096/fasebj.2.14.2972578.Peer-Reviewed Original ResearchConceptsProtein tyrosine kinasesProtein kinaseIntrinsic protein tyrosine kinase activityProtein serine/threonine kinaseKinase activityTyrosine kinaseCalcium/calmodulin-dependent protein kinaseSerine/threonine kinaseCalmodulin-dependent protein kinaseProtein tyrosine kinase activityPhosphatidylinositol kinase activityNew enzyme speciesTyrosine kinase activityMyosin light chain kinaseCalmodulin kinase IIPseudosubstrate prototopeKinase IIIThreonine kinaseSignal transductionLight chain kinaseConstitutive inhibitorGrowth factor receptorKinase autophosphorylationSubstrate specificityCalcium-calmodulin kinase II
1987
The 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
1986
Protein phosphorylation in cultured endothelial cells
Mackie K, Lai Y, Nairn A, Greengard P, Pitt B, Lazo J. Protein phosphorylation in cultured endothelial cells. Journal Of Cellular Physiology 1986, 128: 367-374. PMID: 3745280, DOI: 10.1002/jcp.1041280304.Peer-Reviewed Original ResearchConceptsCalcium/calmodulin-dependent protein kinaseCalmodulin-dependent protein kinaseCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseProtein kinase activityProtein kinaseKinase activityCyclic GMP-dependent protein kinase activityRespective substrate proteinsProtein phosphorylation systemsProtein kinase CSubstrate proteinsProtein phosphorylationPhosphorylation systemEndothelial cellsNumerous substratesTyrosine kinaseKinase CPulmonary artery endothelial cellsKinaseCultured endothelial cellsArtery endothelial cellsSimilar culture conditionsCulture conditionsCells