1997
The Cytoplasmic Domain of Alzheimer’s Amyloid Precursor Protein Is Phosphorylated at Thr654, Ser655, and Thr668 in Adult Rat Brain and Cultured Cells
Oishi M, Nairn A, Czernik A, Lim G, Isohara T, Gandy S, Greengard P, Suzuki T. The Cytoplasmic Domain of Alzheimer’s Amyloid Precursor Protein Is Phosphorylated at Thr654, Ser655, and Thr668 in Adult Rat Brain and Cultured Cells. Molecular Medicine 1997, 3: 111-123. PMID: 9085254, PMCID: PMC2230054, DOI: 10.1007/bf03401803.Peer-Reviewed Original ResearchConceptsAlzheimer's disease amyloid precursor proteinCytoplasmic domainCultured cell linesCell cycle-dependent mannerAmyloid precursor proteinCultured cellsCycle-dependent mannerPhosphorylation state-specific antibodiesPhosphorylation-specific antibodiesPrecursor proteinCell linesProtein kinase C.Stoichiometric phosphorylationG2/M phaseAPP isoformsThr654Alzheimer amyloid precursor proteinOkadaic acidBiological functionsCell cycleKinase C.Intact cellsPhosphorylationHeLa cellsSpecific inhibitor
1993
Protein Phosphorylation Regulates the Cellular Trafficking and Processing of the Alzheimer Beta/A4 Amyloid Precursor Protein
Caporaso G, Gandy S, Buxbaum J, Suzuki T, Nordstedt C, Iverfeldt K, Ramabhadran T, Czernik A, Nairn A, Greengard P. Protein Phosphorylation Regulates the Cellular Trafficking and Processing of the Alzheimer Beta/A4 Amyloid Precursor Protein. NATO ASI Series 1993, 201-202. DOI: 10.1007/978-3-662-02928-2_42.Peer-Reviewed Original ResearchAmyloid precursor proteinBeta/A4 amyloid peptideAlzheimer's diseaseBeta/A4 amyloid precursor proteinA4 amyloid precursor proteinAlzheimer beta/A4 amyloid precursor proteinBeta/A4 peptideA4 amyloid peptidePrecursor proteinEarly-onset formAPP metabolismCerebral depositionA4 peptidePC12 cell lineAbnormal processingNeuroendocrine PC12 cell lineDiseaseCellular traffickingCell linesAmyloid peptidesNormal cellular traffickingTransmembrane glycoproteinProteolytic processingProtein phosphorylationPhosphorylation
1992
Characterization of the cystic fibrosis transmembrane conductance regulator in a colonocyte cell line.
Cohn J, Nairn A, Marino C, Melhus O, Kole J. Characterization of the cystic fibrosis transmembrane conductance regulator in a colonocyte cell line. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 2340-2344. PMID: 1372442, PMCID: PMC48653, DOI: 10.1073/pnas.89.6.2340.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorConductance regulatorTwo-dimensional phosphopeptide mappingT84 cellsProtein kinase ACell linesProtein kinase CSDS/PAGEPhosphopeptide mappingPhosphorylation sitesProminent substrateCFTR peptidesEquivalent proteinsKinase ASame proteinKinase CTerminal sequenceCell lysatesN-glycanaseProteinAnti-peptide antibodiesImmunoblot signalsCFTR immunoreactivity
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
1987
Nerve growth factor treatment or cAMP elevation reduces Ca2+/calmodulin-dependent protein kinase III activity in PC12 cells.
Nairn A, Nichols R, Brady M, Palfrey H. Nerve growth factor treatment or cAMP elevation reduces Ca2+/calmodulin-dependent protein kinase III activity in PC12 cells. Journal Of Biological Chemistry 1987, 262: 14265-14272. PMID: 2443502, DOI: 10.1016/s0021-9258(18)47933-1.Peer-Reviewed Original ResearchConceptsNerve growth factorEffect of forskolinIII activityPC12 cellsGrowth factorLong-term treatmentShort-term treatmentEffect of treatmentNerve growth factor treatmentGrowth factor treatmentAbility of forskolinAbility of NGFPhorbol esterEpidermal growth factorMaximal effectCytosolic extractsFactor treatmentForskolinCAMP elevationTreatmentCell linesProtein kinase CRemoval of forskolinImmunological techniquesDependent protein phosphorylation
1985
Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues.
Nairn A, Bhagat B, Palfrey H. Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 7939-7943. PMID: 3906654, PMCID: PMC390885, DOI: 10.1073/pnas.82.23.7939.Peer-Reviewed Original ResearchConceptsCaM-dependent protein kinaseCaM kinase IIIKinase IIIProtein kinaseMammalian tissuesCalmodulin-dependent protein kinase IIIProtein kinase IIIDependent protein kinaseProtein phosphorylation systemsWidespread tissue distributionTotal cytosolic proteinAnimal cellsPhosphorylation systemSubstrate specificityCytosolic proteinsMyosin light chainMajor substrateKinaseProteinSynapsin IPoor substrateCell linesPhosphorylase bMajor MrPolyclonal antibodies