1999
Interaction of a Neuron-specific Protein Containing PDZ Domains with Alzheimer's Amyloid Precursor Protein*
Tomita S, Ozaki T, Taru H, Oguchi S, Takeda S, Yagi Y, Sakiyama S, Kirino Y, Suzuki T. Interaction of a Neuron-specific Protein Containing PDZ Domains with Alzheimer's Amyloid Precursor Protein*. Journal Of Biological Chemistry 1999, 274: 2243-2254. PMID: 9890987, DOI: 10.1074/jbc.274.4.2243.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAlzheimer DiseaseAmino Acid SequenceAmyloid beta-Protein PrecursorAnimalsChromosome MappingChromosomes, Human, Pair 9Cloning, MolecularDNA, ComplementaryHumansMolecular Sequence DataNerve Tissue ProteinsNeuronsProtein BindingProtein Processing, Post-TranslationalSequence Homology, Amino Acid
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 ResearchMeSH KeywordsAlanineAlzheimer DiseaseAmino Acid SubstitutionAmyloid beta-Protein PrecursorBinding SitesCells, CulturedCytoplasmHumansMutagenesis, Site-DirectedPeptide FragmentsProtein Processing, Post-TranslationalConceptsAlzheimer'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