2024
3-Hydroxykynurenine targets kainate receptors to promote defense against infection
Parada-Kusz M, Clatworthy A, Goering E, Blackwood S, Shigeta J, Mashin E, Salm E, Choi C, Combs S, Lee J, Rodriguez-Osorio C, Clish C, Tomita S, Hung D. 3-Hydroxykynurenine targets kainate receptors to promote defense against infection. Nature Chemical Biology 2024, 1-11. PMID: 38898166, DOI: 10.1038/s41589-024-01635-z.Peer-Reviewed Original ResearchKainate-sensitive glutamate receptorsHost tryptophan metabolismHost survivalBacterial infectionsPromote host survivalGlutamate receptorsLethal bacterial infectionHost-pathogenIn vivo chemical screeningTryptophan metabolismPromote defenseBacterial expansionOutcome of infectionChemical screeningZebrafish embryosAntibacterial activityKainate receptorsPathogen eradicationPathogensHostModulate immunityNervous systemInfectionMetabolismReceptors
2000
Regulation 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
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