2001
ARPP‐16/ARPP‐19: a highly conserved family of cAMP‐regulated phosphoproteins
Dulubova I, Horiuchi A, Snyder G, Girault J, Czernik A, Shao L, Ramabhadran R, Greengard P, Nairn A. ARPP‐16/ARPP‐19: a highly conserved family of cAMP‐regulated phosphoproteins. Journal Of Neurochemistry 2001, 77: 229-238. DOI: 10.1046/j.1471-4159.2001.00191.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCHO CellsConserved SequenceCorpus StriatumCricetinaeCyclic AMPCyclic AMP-Dependent Protein KinasesHumansIn Vitro TechniquesMaleMiceMultigene FamilyOrgan SpecificityPhosphoproteinsPhosphorylationProtein IsoformsRatsRats, Sprague-DawleyReceptors, Dopamine D1Receptors, Dopamine D2Sequence Homology, Amino AcidConceptsProtein kinase AARPP-19ARPP-16Family of cAMPImportant cellular functionsActivation of PKAIsoform-specific antibodiesYeast genomeD. melanogasterC. elegansProtein familyCellular functionsNon-neuronal cellsSignal transductionConsensus sitesKinase ARelated proteinsΑ-endosulfinePhosphorylated formIntact cellsIntracellular messengerBi-directional regulationDopamine receptorsFamily membersPhosphorylationARPP-16/ARPP-19: a highly conserved family of cAMP-regulated phosphoproteins.
Dulubova I, Horiuchi A, Snyder G, Girault J, Czernik A, Shao L, Ramabhadran R, Greengard P, Nairn A. ARPP-16/ARPP-19: a highly conserved family of cAMP-regulated phosphoproteins. Journal Of Neurochemistry 2001, 77: 229-38. PMID: 11279279, DOI: 10.1046/j.1471-4159.2001.t01-1-00191.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCHO CellsConserved SequenceCorpus StriatumCricetinaeCyclic AMPCyclic AMP-Dependent Protein KinasesHumansIn Vitro TechniquesMaleMiceMultigene FamilyOrgan SpecificityPhosphoproteinsPhosphorylationProtein IsoformsRatsRats, Sprague-DawleyReceptors, Dopamine D1Receptors, Dopamine D2Sequence Homology, Amino AcidConceptsProtein kinase AARPP-19ARPP-16Family of cAMPImportant cellular functionsActivation of PKAIsoform-specific antibodiesYeast genomeD. melanogasterC. elegansProtein familyCellular functionsNon-neuronal cellsSignal transductionConsensus sitesType dopamine receptorsKinase ARelated proteinsPhosphorylated formIntact cellsDopamine receptorsIntracellular messengerBi-directional regulationFamily membersPhosphorylation
1999
Role of Phosphorylation of Alzheimer’s Amyloid Precursor Protein during Neuronal Differentiation
Ando K, Oishi M, Takeda S, Iijima K, Isohara T, Nairn A, Kirino Y, Greengard P, Suzuki T. Role of Phosphorylation of Alzheimer’s Amyloid Precursor Protein during Neuronal Differentiation. Journal Of Neuroscience 1999, 19: 4421-4427. PMID: 10341243, PMCID: PMC6782598, DOI: 10.1523/jneurosci.19-11-04421.1999.Peer-Reviewed Original Research
1997
Phosphorylation of Connexin43 and the Regulation of Neonatal Rat Cardiac Myocyte Gap Junctions
Sáez J, Nairn A, Czernik A, Fishman G, Spray D, Hertzberg E. Phosphorylation of Connexin43 and the Regulation of Neonatal Rat Cardiac Myocyte Gap Junctions. Journal Of Molecular And Cellular Cardiology 1997, 29: 2131-2145. PMID: 9281445, DOI: 10.1006/jmcc.1997.0447.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornCalcium-Calmodulin-Dependent Protein KinasesCDC2 Protein KinaseCells, CulturedConnexin 43DNA, ComplementaryElectrophoresis, Gel, Two-DimensionalEnzyme InhibitorsGap JunctionsMyocardiumPatch-Clamp TechniquesPhosphorylationProtein Processing, Post-TranslationalRatsRecombinant Fusion ProteinsStaurosporineTetradecanoylphorbol AcetateConceptsProtein kinase CTwo-dimensional tryptic phosphopeptide mapsTryptic phosphopeptide mapsState of phosphorylationMyocyte gap junctionsProtein kinase inhibitorsGap junctionsMajor gap junction proteinPhosphorylation of connexin43Gap junction proteinPhosphopeptide mapsTryptic phosphopeptidesPKC-dependent mechanismFunctional couplingPhosphorylated formKinase CPhosphorylationNeonatal rat cardiocytesCx43 phosphorylationStaurosporineCellular distributionImmunoblot analysisRat cardiocytesJunction proteinsCx43
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