2000
Overexpression of Human Amyloid Precursor Protein in Drosophila
Yagi Y, Tomita S, Nakamura M, Suzuki T. Overexpression of Human Amyloid Precursor Protein in Drosophila. Archives Of Biochemistry And Biophysics 2000, 4: 43-49. PMID: 11152627, DOI: 10.1006/mcbr.2000.0248.Peer-Reviewed Original ResearchMeSH KeywordsAmyloid beta-Protein PrecursorAnimalsAnimals, Genetically ModifiedDrosophilaHumansPhenotypeConceptsHuman APPHuman amyloid precursor proteinAPP expression levelsExpression of APPPrecursor proteinAmyloid precursor proteinBeta-amyloid peptideSynaptic terminalsHuman neuronsAlzheimer's diseaseNeural cellsApp functionsExpression levelsDiseasePhysiological functionsProtein transport systemWing blister phenotypePhenotypeWing phenotypeImaginal discsCuticle secretionNeuronsWing tissueProteinSecretionRegulation of X11L-dependent Amyloid Precursor Protein Metabolism by XB51, a Novel X11L-binding Protein*
Lee D, Tomita S, Kirino Y, Suzuki T. Regulation of X11L-dependent Amyloid Precursor Protein Metabolism by XB51, a Novel X11L-binding Protein*. Journal Of Biological Chemistry 2000, 275: 23134-23138. PMID: 10833507, DOI: 10.1074/jbc.c000302200.Peer-Reviewed Original Research
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 compartmentAlphaCellsMetabolismcDNA isolation of Alzheimer's amyloid precursor protein from cholinergic nerve terminals of the electric organ of the electric ray
IIJIMA K, LEE D, OKUTSU J, TOMITA S, HIRASHIMA N, KIRINO Y, SUZUKI T. cDNA isolation of Alzheimer's amyloid precursor protein from cholinergic nerve terminals of the electric organ of the electric ray. Biochemical Journal 1998, 330: 29-33. PMID: 9461486, PMCID: PMC1219103, DOI: 10.1042/bj3300029.Peer-Reviewed Original ResearchConceptsAlzheimer amyloid precursor proteinAmyloid precursor proteinNerve terminalsCholinergic nerve terminalsPrecursor proteinBeta-amyloid domainAPP695 isoformCholinergic neuronsElectric ray electric organCell bodiesElectric organNeuronsRay electric organPresent studyElectric lobePhosphorylation sitesCytoplasmic domainOrgansPhosphorylated formPhosphorylationProtein