1993
Protein Phosphorylation Regulates Relative Utilization of Processing Pathways for Alzheimer β/A4 Amyloid Precursor Proteina
GANDY S, CAPORASO G, BUXBAUM J, DA CRUZ E SILVA O, IVERFELDT K, NORDSTEDT C, SUZUKI T, CZERNIK A, NAIRN A, GREENGARD P. Protein Phosphorylation Regulates Relative Utilization of Processing Pathways for Alzheimer β/A4 Amyloid Precursor Proteina. Annals Of The New York Academy Of Sciences 1993, 695: 117-121. PMID: 8239268, DOI: 10.1111/j.1749-6632.1993.tb23038.x.Peer-Reviewed Original ResearchConceptsOkadaic acid-sensitive proteinAlzheimer amyloid precursor proteinAcid-sensitive proteinProtein kinase CProtein phosphorylationKinase CCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinase IISignal transductionPhosphorylation stateModulation of betaKinase IISecretory cleavageSubstrate redistributionPrecursor proteinCurrent experimental evidenceAmyloid precursor proteinProteinCleavage pathwayPhosphorylationProcessing pathwaysSubstrate activationSer655APP metabolism
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
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. DOI: 10.1007/bf02918897.Peer-Reviewed Original ResearchCalcium/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 sitesMultisite 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