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: 229-38. 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 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: 229-238. 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 membersPhosphorylation
1989
Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms
Ivar Walaas S, Nairn A. Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms. Journal Of Molecular Neuroscience 1989, 1: 117-127. PMID: 2561875, DOI: 10.1007/bf02896895.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino AcidsAnimalsBrainCalcium-Calmodulin-Dependent Protein KinasesElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelMicrotubule-Associated ProteinsOrgan SpecificityPeptide MappingPhosphopeptidesPhosphorylationProtein Kinase CProtein KinasesRatsConceptsCalcium/phospholipid-dependent protein kinasePhospholipid-dependent protein kinaseCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinaseCalcium/calmodulinProtein kinase IIKinase IICyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCommon phosphorylation sitesOnly serine residuesProtein 2Cyclic AMPMultisite phosphorylationThreonine residuesPhosphorylation sitesSerine residuesPhosphorylation systemPhosphorylation mechanismCytoskeletal proteinsMAP-2KinasePeptide mapsDistinct sites