2025
Inflammaging, Neuroinflammation, and Synaptic Damage in Alzheimer's Disease
Carnevale L, Lipton S. Inflammaging, Neuroinflammation, and Synaptic Damage in Alzheimer's Disease. 2025, 303-314. DOI: 10.1016/b978-0-323-95702-1.00491-7.Peer-Reviewed Original ResearchAmyloid-betaAlzheimer's diseaseAmyloid-beta precursor proteinProteins amyloid-betaNeuronal healthDiscovery of mutationsAlzheimer's disease casesGenome sequencePresenilin-1Precursor proteinProtein functionAlzheimer's disease researchImmune signalingLipid transportProgressive neurodegenerative diseaseAlzheimer's disease patientsGenetic causeApolipoprotein E4Genes related to lipid transportSynaptic damageStress-mediated alterationsNeurodegenerative diseasesDisease pathologyProteinAlzheimer
2023
Integrative analysis reveals a conserved role for the amyloid precursor protein in proteostasis during aging
Nithianandam V, Bukhari H, Leventhal M, Battaglia R, Dong X, Fraenkel E, Feany M. Integrative analysis reveals a conserved role for the amyloid precursor protein in proteostasis during aging. Nature Communications 2023, 14: 7034. PMID: 37923712, PMCID: PMC10624868, DOI: 10.1038/s41467-023-42822-1.Peer-Reviewed Original ResearchConceptsAmyloid precursor proteinPrecursor proteinNormal function of APPFunction of amyloid precursor proteinPathogenesis of Alzheimer's diseaseRelevant to Alzheimer's diseaseAlzheimer's diseaseDrosophila orthologMutant fliesTauopathy modelGenetic screeningAB peptideCellular signalingCellular pathwaysProteomic studiesMitochondrial functionProteostasisNeurodegenerative diseasesIntegrated analysisLipid metabolismRegulating autophagyNucleic acidsSingle cellsAmyloidTGFB signaling
2022
Modulation of amyloid precursor protein cleavage by γ-secretase activating protein through phase separation
Jin C, Wang J, Wang Y, Jia B, Guo X, Yang G, Xu P, Greengard P, Zhou R, Shi Y. Modulation of amyloid precursor protein cleavage by γ-secretase activating protein through phase separation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2122292119. PMID: 35298330, PMCID: PMC8944281, DOI: 10.1073/pnas.2122292119.Peer-Reviewed Original ResearchConceptsAberrant cleavage of amyloid precursor proteinAssociated with Alzheimer's diseaseAPP-C99Cleavage of amyloid precursor proteinAmyloid precursor protein cleavageAmyloid precursor proteinPhase separation in vitroC-terminal fragmentDevelopment of potential therapeuticsSequence elementsPrecursor proteinAberrant cleavageProtein cleavageSubstrate sequestrationAlzheimer's diseaseGSAPProteinCleavagePotential therapeuticsC99SequenceAb42Increasing concentrationsCells
2021
Overlapping roles of JIP3 and JIP4 in promoting axonal transport of lysosomes in human iPSC-derived neurons
Gowrishankar S, Lyons L, Rafiq NM, Roczniak-Ferguson A, De Camilli P, Ferguson SM. Overlapping roles of JIP3 and JIP4 in promoting axonal transport of lysosomes in human iPSC-derived neurons. Molecular Biology Of The Cell 2021, 32: 1094-1103. PMID: 33788575, PMCID: PMC8351540, DOI: 10.1091/mbc.e20-06-0382.Peer-Reviewed Original ResearchConceptsAxonal transportAlzheimer's disease-related amyloid precursor proteinAmyloidogenic APP processingAmyloid precursor proteinDependence of neuronsHuman iPSCNeuronal cell biologyAPP processingAxonal lysosomesNeuronsLoss of JIP3Lysosome abundanceMovement of lysosomesPrecursor proteinCellular modelCritical regulatorStem cellsPluripotent stem cellsAβ42 peptideIPSCsLysosome transportLysosomesOverlapping rolePathology
2020
A Genetic Code Expansion‐Derived Molecular Beacon for the Detection of Intracellular Amyloid‐β Peptide Generation
Sappakhaw K, Jantarug K, Slavoff S, Israsena N, Uttamapinant C. A Genetic Code Expansion‐Derived Molecular Beacon for the Detection of Intracellular Amyloid‐β Peptide Generation. Angewandte Chemie 2020, 133: 3980-3985. PMID: 38504667, PMCID: PMC10946459, DOI: 10.1002/ange.202010703.Peer-Reviewed Original ResearchDiverse biological functionsAmyloid precursor proteinProteolytic proteoformsEndocytic pathwayGenetic taggingBiological functionsProtein precursorLiving cellsProteolytic processingMolecular beacon designPrecursor proteinCellular studiesLabeling strategyProteoformsMolecular beaconsAmyloid-β peptide generationBiogenesisImportant rolePeptide generationBeacon designPolypeptideReporterProteinAlzheimer's diseasePathwayAmyloid-β Precursor Protein APP Down-Regulation Alters Actin Cytoskeleton-Interacting Proteins in Endothelial Cells
Ristori E, Cicaloni V, Salvini L, Tinti L, Tinti C, Simons M, Corti F, Donnini S, Ziche M. Amyloid-β Precursor Protein APP Down-Regulation Alters Actin Cytoskeleton-Interacting Proteins in Endothelial Cells. Cells 2020, 9: 2506. PMID: 33228083, PMCID: PMC7699411, DOI: 10.3390/cells9112506.Peer-Reviewed Original ResearchConceptsAmyloid-β precursor proteinCerebral amyloid angiopathyUbiquitous membrane proteinsFocal adhesion stabilityEndothelial cellsMajor cellular targetInteracting proteinActin cytoskeletonProteomic approachMembrane proteinsAlzheimer's diseaseMolecular mechanismsCellular responsesCellular targetsPhysiological roleRole of APPEndothelial cell proliferationPrecursor proteinCell proliferationNormal endothelial functionProteinNeuronal tissueGrowth factorExogenous stimuliExpressionNew Insights Into Blood-Brain Barrier Maintenance: The Homeostatic Role of β-Amyloid Precursor Protein in Cerebral Vasculature
Ristori E, Donnini S, Ziche M. New Insights Into Blood-Brain Barrier Maintenance: The Homeostatic Role of β-Amyloid Precursor Protein in Cerebral Vasculature. Frontiers In Physiology 2020, 11: 1056. PMID: 32973564, PMCID: PMC7481479, DOI: 10.3389/fphys.2020.01056.Peer-Reviewed Original ResearchCerebral amyloid angiopathyΒ-amyloid precursor proteinBlood-brain barrierCentral nervous systemAlzheimer's diseaseBlood-brain barrier maintenanceΒ-amyloid accumulationPeripheral blood circulationPrecursor proteinEndothelial cell homeostasisCAA pathogenesisBBB dysfunctionBBB functionAmyloid angiopathyVascular dysfunctionAD onsetCerebrovascular homeostasisCerebral vasculatureVascular endotheliumPathological outcomesNervous systemHomeostatic roleBrain vasculatureNeurodegenerative disordersBarrier maintenance
2014
Quantitative analysis and modeling of katanin function in flagellar length control
Kannegaard E, Rego E, Schuck S, Feldman J, Marshall W. Quantitative analysis and modeling of katanin function in flagellar length control. Molecular Biology Of The Cell 2014, 25: 3686-3698. PMID: 25143397, PMCID: PMC4230626, DOI: 10.1091/mbc.e14-06-1116.Peer-Reviewed Original ResearchConceptsFlagellar length controlFlagellar lengthCytoplasmic microtubulesFull-length flagellaHalf-length flagellaLength controlPools of tubulinFlagellar assemblyTranscriptional regulationKatanin functionKatanin-mediated severingOrganelle sizeRegulatory subunitChlamydomonas reinhardtiiCandidate genesMicrotubule severingPreexisting poolFlagellaRegulatory systemPrecursor proteinModel systemGenesSimple model systemMicrotubulesMutations
2013
Cerebrospinal Fluid and Neuroimaging Biomarker Abnormalities Suggest Early Neurological Injury in a Subset of Individuals During Primary HIV Infection
Peluso MJ, Meyerhoff DJ, Price RW, Peterson J, Lee E, Young AC, Walter R, Fuchs D, Brew BJ, Cinque P, Robertson K, Hagberg L, Zetterberg H, Gisslén M, Spudich S. Cerebrospinal Fluid and Neuroimaging Biomarker Abnormalities Suggest Early Neurological Injury in a Subset of Individuals During Primary HIV Infection. The Journal Of Infectious Diseases 2013, 207: 1703-1712. PMID: 23460748, PMCID: PMC3636785, DOI: 10.1093/infdis/jit088.Peer-Reviewed Original ResearchConceptsPrimary HIV infectionNeurofilament light chainHIV infectionAmyloid precursor proteinCerebrospinal fluidNeuronal injuryT-tauCSF/plasma albumin ratioPrimary human immunodeficiency virus (HIV) infectionCentral nervous system inflammationHuman immunodeficiency virus (HIV) infectionSoluble amyloid precursor proteinGamma-induced protein 10Primary infection groupNervous system inflammationImmunodeficiency virus infectionEarly neuronal injuryPlasma albumin ratioParietal gray matterGlutamate/creatineLight chainPrecursor proteinProton magnetic resonance spectroscopyFrontal white matterWhite blood cellsProteomics and the Analysis of Proteomic Data: 2013 Overview of Current Protein‐Profiling Technologies
Bruce C, Stone K, Gulcicek E, Williams K. Proteomics and the Analysis of Proteomic Data: 2013 Overview of Current Protein‐Profiling Technologies. Current Protocols In Bioinformatics 2013, 41: 13.21.1-13.21.17. PMID: 23504934, PMCID: PMC3688054, DOI: 10.1002/0471250953.bi1321s41.Peer-Reviewed Original ResearchConceptsMore post-translational modificationsStudy of proteomesPost-translational modificationsFragment ionsChemical structureProtein profiling technologiesMass spectrometryProteolytic peptidesCharge ratioProteomic dataProtein sequencesSpectral dataPrecursor proteinProteomeProteomicsProteinQuantitationSpectrometryIons
2012
Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells
Lang S, Benedix J, Fedeles SV, Schorr S, Schirra C, Schäuble N, Jalal C, Greiner M, Haßdenteufel S, Tatzelt J, Kreutzer B, Edelmann L, Krause E, Rettig J, Somlo S, Zimmermann R, Dudek J. Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells. Journal Of Cell Science 2012, 125: 1958-1969. PMID: 22375059, PMCID: PMC4074215, DOI: 10.1242/jcs.096727.Peer-Reviewed Original ResearchConceptsPost-translational transportTail-anchored proteinsSEC61A1 geneEndoplasmic reticulumTransport of polypeptidesCo-translational transportSemi-permeabilized cellsPrecursor proteinSEC62 geneSec61 channelPresecretory proteinsMembrane integrationProtein transportMammalian cellsKnockdown approachHuman cellsGenesHeLa cellsProteinPolypeptideReticulumCellsSec63pSec61αSec63
2009
Structural Characterization of the E2 Domain of APL-1, a Caenorhabditis elegans Homolog of Human Amyloid Precursor Protein, and Its Heparin Binding Site*
Hoopes JT, Liu X, Xu X, Demeler B, Folta-Stogniew E, Li C, Ha Y. Structural Characterization of the E2 Domain of APL-1, a Caenorhabditis elegans Homolog of Human Amyloid Precursor Protein, and Its Heparin Binding Site*. Journal Of Biological Chemistry 2009, 285: 2165-2173. PMID: 19906646, PMCID: PMC2804372, DOI: 10.1074/jbc.m109.018432.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmyloid beta-Protein PrecursorAnimalsBinding SitesCaenorhabditis elegansCaenorhabditis elegans ProteinsCrystallography, X-RayHeparinHumansHydrogen-Ion ConcentrationMembrane ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein StabilityProtein Structure, TertiarySequence Homology, Amino AcidSolutionsSucrose
2006
Presenilin-1 uses phospholipase D1 as a negative regulator of β-amyloid formation
Cai D, Netzer WJ, Zhong M, Lin Y, Du G, Frohman M, Foster DA, Sisodia SS, Xu H, Gorelick FS, Greengard P. Presenilin-1 uses phospholipase D1 as a negative regulator of β-amyloid formation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 1941-1946. PMID: 16449386, PMCID: PMC1413665, DOI: 10.1073/pnas.0510708103.Peer-Reviewed Original ResearchMeSH KeywordsAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAnimalsAspartic Acid EndopeptidasesCell LineEndopeptidasesGene Expression RegulationHumansMembrane ProteinsMiceMice, KnockoutPhospholipase DPresenilin-1Protein BindingProtein Processing, Post-TranslationalProtein Transporttrans-Golgi NetworkConceptsBeta-amyloid precursor proteinPrecursor proteinΒ-amyloid formationAbeta productionAbeta generationPresenilin 1Phospholipase D1 corrects impaired βAPP trafficking and neurite outgrowth in familial Alzheimer’s disease-linked presenilin-1 mutant neurons
Cai D, Zhong M, Wang R, Netzer WJ, Shields D, Zheng H, Sisodia SS, Foster DA, Gorelick FS, Xu H, Greengard P. Phospholipase D1 corrects impaired βAPP trafficking and neurite outgrowth in familial Alzheimer’s disease-linked presenilin-1 mutant neurons. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 1936-1940. PMID: 16449385, PMCID: PMC1413666, DOI: 10.1073/pnas.0510710103.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkOverexpression of PLD1Mutant neuronsPhospholipase D1Beta-amyloid precursor proteinIntracellular traffickingPS1-deficient cellsPLD enzymatic activityTherapeutic targetNeuronal functionPS1 mutationsOverexpression of WTBetaAPPPrecursor proteinMutant cellsSubcellular localizationNeurite outgrowthPLD1 activitySurface deliveryNeuronsOutgrowth capacityCellsTraffickingEnzymatic activityOverexpression
2001
17 First trimester thrombus precursor protein (TPP) predicts adverse pregnancy outcome in thrombophilic patients
Paidas M, Urban G, Ku W, Arkel Y, Dilley A, Andrei R, Kuczynski E, Jeanine M, Mignosa M, Khan S, Schoenfeld J, Lockwood C. 17 First trimester thrombus precursor protein (TPP) predicts adverse pregnancy outcome in thrombophilic patients. American Journal Of Obstetrics And Gynecology 2001, 185: s76. DOI: 10.1016/s0002-9378(01)80027-2.Peer-Reviewed Original Research
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 ResearchConceptsHuman 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 ResearchPDZ 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
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
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