2000
PDZ Domain-dependent Suppression of NF-κB/p65-induced Aβ42 Production by a Neuron-specific X11-like Protein*
Tomita S, Fujita T, Kirino Y, Suzuki T. PDZ Domain-dependent Suppression of NF-κB/p65-induced Aβ42 Production by a Neuron-specific X11-like Protein*. Journal Of Biological Chemistry 2000, 275: 13056-13060. PMID: 10777610, DOI: 10.1074/jbc.c000019200.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAlzheimer DiseaseAmyloid beta-PeptidesAnimalsBrainCell LineCOS CellsDNA, ComplementaryGene Expression RegulationGene LibraryHumansLuciferasesNerve Tissue ProteinsNeuronsNF-kappa BNF-kappa B p50 SubunitPeptide FragmentsPrecipitin TestsProtein BindingProtein IsoformsProtein Structure, TertiaryTranscription Factor RelATranscription, GeneticTransfectionTwo-Hybrid System TechniquesConceptsNF-kappaB/p65X11-like proteinsAlzheimer's diseaseNF-kappaB/p50Progression of ADAmyloid precursor proteinSpecific therapyAbeta productionAβ42 productionAbeta42 productionNF-kappaBP65Neuronal cellsAmino acids 161Precursor proteinX11LAbeta42DiseaseRel homology domainSecretionX11L.P50LIN-10Transcription factorsTherapy
1998
A Basic Amino Acid in the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein (APP) Is Essential for Cleavage of APP at the α-Site*
Tomita S, Kirino Y, Suzuki T. A Basic Amino Acid in the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein (APP) Is Essential for Cleavage of APP at the α-Site*. Journal Of Biological Chemistry 1998, 273: 19304-19310. PMID: 9668120, DOI: 10.1074/jbc.273.30.19304.Peer-Reviewed Original ResearchConceptsAlzheimer's β-Amyloid Precursor ProteinΒ-amyloid precursor proteinAlzheimer's diseaseSecretion of Abeta40Beta-amyloid precursor proteinFamilial AD mutationsPrecursor proteinAPP cytoplasmic domainBeta-amyloid peptideAPP metabolismAD mutationsSporadic typeAbeta productionAberrant metabolismCTFbetaIntracellular accumulationBasic amino acidsAmino acid mutationsAmino acidsDiseaseSingle amino acid mutationNon-basic amino acidsMetabolismAcid mutationsCytoplasmic domainCleavage of Alzheimer's Amyloid Precursor Protein (APP) by Secretases Occurs after O-Glycosylation of APP in the Protein Secretory Pathway IDENTIFICATION OF INTRACELLULAR COMPARTMENTS IN WHICH APP CLEAVAGE OCCURS WITHOUT USING TOXIC AGENTS THAT INTERFERE WITH PROTEIN METABOLISM*
Tomita S, Kirino Y, Suzuki T. Cleavage of Alzheimer's Amyloid Precursor Protein (APP) by Secretases Occurs after O-Glycosylation of APP in the Protein Secretory Pathway IDENTIFICATION OF INTRACELLULAR COMPARTMENTS IN WHICH APP CLEAVAGE OCCURS WITHOUT USING TOXIC AGENTS THAT INTERFERE WITH PROTEIN METABOLISM*. Journal Of Biological Chemistry 1998, 273: 6277-6284. PMID: 9497354, DOI: 10.1074/jbc.273.11.6277.Peer-Reviewed Original ResearchConceptsAlzheimer amyloid precursor proteinAmyloid precursor proteinAPP cleavageParenchymal amyloid depositsAPP carboxyl-terminal fragmentsPrecursor proteinBeta-amyloid peptideProtein metabolismNormal protein metabolismPossible intracellular siteAbeta generationAmyloid depositsAlzheimer's diseaseCarboxyl-terminal fragmentDefective O-glycosylationToxic agentsIntracellular secretory pathwayDiseasePresent studyIntracellular sitesBetaReticular compartmentAlphaCellsMetabolism