2023
Mass spectrometry in cerebrospinal fluid uncovers association of glycolysis biomarkers with Alzheimer’s disease in a large clinical sample
de Geus M, Leslie S, Lam T, Wang W, Roux-Dalvai F, Droit A, Kivisakk P, Nairn A, Arnold S, Carlyle B. Mass spectrometry in cerebrospinal fluid uncovers association of glycolysis biomarkers with Alzheimer’s disease in a large clinical sample. Scientific Reports 2023, 13: 22406. PMID: 38104170, PMCID: PMC10725469, DOI: 10.1038/s41598-023-49440-3.Peer-Reviewed Original Research
2022
Performance of a fully-automated Lumipulse plasma phospho-tau181 assay for Alzheimer’s disease
Wilson E, Young C, Ramos Benitez J, Swarovski M, Feinstein I, Vandijck M, Le Guen Y, Kasireddy N, Shahid M, Corso N, Wang Q, Kennedy G, Trelle A, Lind B, Channappa D, Belnap M, Ramirez V, Skylar-Scott I, Younes K, Yutsis M, Le Bastard N, Quinn J, van Dyck C, Nairn A, Fredericks C, Tian L, Kerchner G, Montine T, Sha S, Davidzon G, Henderson V, Longo F, Greicius M, Wagner A, Wyss-Coray T, Poston K, Mormino E, Andreasson K. Performance of a fully-automated Lumipulse plasma phospho-tau181 assay for Alzheimer’s disease. Alzheimer's Research & Therapy 2022, 14: 172. PMID: 36371232, PMCID: PMC9652927, DOI: 10.1186/s13195-022-01116-2.Peer-Reviewed Original ResearchMeSH KeywordsAlzheimer DiseaseAmyloid beta-PeptidesBiomarkersCognitive DysfunctionHumansTau ProteinsConceptsPlasma p-tau181Alzheimer's Disease Research CenterP-tau181Disease Research CenterAlzheimer's diseasePositron emission tomographyAD dementiaBlood-based biomarker assaysAmyloid positron emission tomographyTreatment monitoringNovel blood-based biomarkersCSF p-tau181P-tau181 concentrationsDisease-modifying therapiesAβ42/Aβ40 ratioBlood-based biomarkersClinical AD diagnosisDetection of ADMild cognitive impairmentStudy cohortCSF biomarkersPlasma levelsAD groupPrognostic performanceCDR sum
2001
Decreased levels of ARPP-19 and PKA in brains of Down syndrome and Alzheimer’s disease
Kim S, Nairn A, Cairns N, Lubec G. Decreased levels of ARPP-19 and PKA in brains of Down syndrome and Alzheimer’s disease. Journal Of Neural Transmission. Supplementa 2001, 263-272. PMID: 11771749, DOI: 10.1007/978-3-7091-6262-0_21.Peer-Reviewed Original ResearchConceptsARPP-19Protein kinaseDifferential display polymerase chain reactionAlzheimer's diseaseDown syndromeCAMP-dependent protein kinaseTemporal cortexActivity of PKASignal transductionDownregulated sequenceBrain regionsNeurodegenerative disordersDiseaseImpaired mechanismsProtein levelsDecreased activityChain reactionFirst evidenceSignificant reductionSyndromeCortexDisordersTransductionHomologyKinase
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 ResearchPhosphorylation of the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein at Ser655 by a Novel Protein Kinase
Isohara T, Horiuchi A, Watanabe T, Ando K, Czernik A, Uno I, Greengard P, Nairn A, Suzuki T. Phosphorylation of the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein at Ser655 by a Novel Protein Kinase. Biochemical And Biophysical Research Communications 1999, 258: 300-305. PMID: 10329382, DOI: 10.1006/bbrc.1999.0637.Peer-Reviewed Original ResearchConceptsNovel protein kinaseAlzheimer's beta-amyloid precursor proteinProtein kinase CExtracellular signal-regulated kinaseProtein kinaseCytoplasmic domainCalmodulin-dependent protein kinase IIΒ-amyloid precursor proteinPrecursor proteinAlzheimer's β-Amyloid Precursor ProteinSignal-regulated kinaseProtein kinase IIBeta-amyloid precursor proteinKinase IUnidentified proteinsKinase IIKinase CKinaseSer655ProteinAlzheimer's diseaseThr654Rat brainPhosphorylationDomain
1997
Phosphorylation of Alzheimer β-Amyloid Precursor-like Proteins †
Suzuki T, Ando K, Isohara T, Oishi M, Lim G, Satoh Y, Wasco W, Tanzi R, Nairn A, Greengard P, Gandy S, Kirino Y. Phosphorylation of Alzheimer β-Amyloid Precursor-like Proteins †. Biochemistry 1997, 36: 4643-4649. PMID: 9109675, DOI: 10.1021/bi962618k.Peer-Reviewed Original ResearchConceptsAlzheimer's beta-amyloid precursor proteinCytoplasmic domain peptidePrecursor-like proteinsProtein kinase CCytoplasmic domainCultured cellsCell cycle-dependent mannerKinase CDomain peptideCycle-dependent mannerAmino acid sequenceHomologous amino acid sequencesGene familyKinase siteAcid sequenceExtracellular domainIntact cellsAPLP2Proteolytic processingAPLP1PhosphorylationPrecursor proteinProteinBeta-amyloid precursor proteinCdc2The 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
1992
Characterization of Alternative Routes for Processing of the Alzheimer β/A4‐Amyloid Precursor Protein
GANDY S, CAPORASO G, RAMABHADRAN T, SUZUKI T, BUXBAUM J, NORDSTEDT C, IVERFELDT K, CZERNIK A, NAIRN A, GREENGARD P. Characterization of Alternative Routes for Processing of the Alzheimer β/A4‐Amyloid Precursor Protein. Annals Of The New York Academy Of Sciences 1992, 674: 203-217. PMID: 1363189, DOI: 10.1111/j.1749-6632.1992.tb27489.x.Peer-Reviewed Original ResearchIncreased 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