2025
The Roles of the Numb Protein in Synaptic Development and Plasticity
Sukhanova T, Renkemeyer M, Pritchett N, Berke B, Keshishian H. The Roles of the Numb Protein in Synaptic Development and Plasticity. Developmental Neurobiology 2025, 85: e22988. PMID: 40620134, PMCID: PMC12258135, DOI: 10.1002/dneu.22988.Peer-Reviewed Original ResearchConceptsLarval neuromuscular junctionGrowth factor signalingEndocytic processRNAi knockdownNumb proteinFactor signalingDrosophila neuromuscular junctionSynaptic developmentKnockdown of NumbGrowth factor receptor signalingNeuromuscular junctionGenetic interactionsAdaptor proteinGrowth plasticityLoss of functionPresynaptic sidePresynaptic boutonsReceptor signalingGrowth factor receptorProteinFactor receptorLarvalGrowthAdaptorRNAi
2022
KIF2C regulates synaptic plasticity and cognition in mice through dynamic microtubule depolymerization
Zheng R, Du Y, Wang X, Liao T, Zhang Z, Wang N, Li X, Shen Y, Shi L, Luo J, Xia J, Wang Z, Xu J. KIF2C regulates synaptic plasticity and cognition in mice through dynamic microtubule depolymerization. ELife 2022, 11: e72483. PMID: 35138249, PMCID: PMC8828051, DOI: 10.7554/elife.72483.Peer-Reviewed Original ResearchConceptsDynamic microtubulesFunctional plasticity of synapsesRegulate synaptic developmentConditional knockout approachFunction of KIF2CNervous systemNeuronal activity-dependent mannerPlasticity of synapsesProtein traffickingActivity-dependent mannerDepolymerizing proteinsRNAi knockdownSynaptic plasticityExpression of AMPA receptorsMicrotubule dynamicsMicrotubule invasionMicrotubule depolymerizationImpaired excitatory transmissionKnockout approachRegulatory mechanismsKIF2CDepolymerization capabilityLong-term potentiationSynaptic developmentMicrotubules
2018
Extracellular anti-angiogenic proteins augment an endosomal protein trafficking pathway to reach mitochondria and execute apoptosis in HUVECs
Chen M, Qiu T, Wu J, Yang Y, Wright GD, Wu M, Ge R. Extracellular anti-angiogenic proteins augment an endosomal protein trafficking pathway to reach mitochondria and execute apoptosis in HUVECs. Cell Death & Differentiation 2018, 25: 1905-1920. PMID: 29523874, PMCID: PMC6219483, DOI: 10.1038/s41418-018-0092-9.Peer-Reviewed Original ResearchMeSH KeywordsAngiostatinsApoptosisCell MembraneEndocytosisEndoplasmic Reticulum Chaperone BiPEndosomesFibronectinsFluorescence Recovery After PhotobleachingHeat-Shock ProteinsHuman Umbilical Vein Endothelial CellsHumansMicroscopy, FluorescenceMitochondriaNeovascularization, PhysiologicPhosphoproteinsProtein TransportRecombinant ProteinsRNA InterferenceRNA, Small InterferingSodium-Hydrogen ExchangersSynaptosomal-Associated Protein 25ThrombospondinsConceptsLate endosomesEndosomal proteinExtracellular proteinsT-SNARE proteinsCytosolic scaffold proteinsTotal internal reflection fluorescent microscopyPro-apoptotic functionFluorescent microscopyRegulatory factor 1Recycling endosomesRNAi knockdownCargo degradationScaffold proteinSuper-resolution fluorescent microscopyMitochondrial traffickingCell fractionationPlasma membraneIsthminProximity ligationMitochondriaProtein 25ProteinBiochemical analysisAnti-angiogenic proteinFactor 1
2012
Nature and function of insulator protein binding sites in the Drosophila genome
Schwartz Y, Linder-Basso D, Kharchenko P, Tolstorukov M, Kim M, Li H, Gorchakov A, Minoda A, Shanower G, Alekseyenko A, Riddle N, Jung Y, Gu T, Plachetka A, Elgin S, Kuroda M, Park P, Savitsky M, Karpen G, Pirrotta V. Nature and function of insulator protein binding sites in the Drosophila genome. Genome Research 2012, 22: 2188-2198. PMID: 22767387, PMCID: PMC3483548, DOI: 10.1101/gr.138156.112.Peer-Reviewed Original ResearchConceptsInsulator proteinsQuantitative genome-wide analysisInsulator elementsGenome-wide analysisEnhancer-blocking assaysRepressive histone methylationDrosophila chromatinDrosophila genomeEukaryotic genomesCombinatorial bindingH3K27me3 marksHistone methylationRNAi knockdownAdjacent genesGenome expressionFunctional characterizationAssociated proteinsGenomeCultured cellsProteinSpecific regulationGenesMajor alterationsDifferent classesChromatin
2006
ATP Synthase Is Responsible for Maintaining Mitochondrial Membrane Potential in Bloodstream Form Trypanosoma brucei
Brown SV, Hosking P, Li J, Williams N. ATP Synthase Is Responsible for Maintaining Mitochondrial Membrane Potential in Bloodstream Form Trypanosoma brucei. MSphere 2006, 5: 45-53. PMID: 16400167, PMCID: PMC1360250, DOI: 10.1128/ec.5.1.45-53.2006.Peer-Reviewed Original ResearchConceptsMitochondrial membrane potentialATP synthaseRNA interferenceBeta subunitProtein levelsAlpha subunitMembrane potentialBloodstream form T. bruceiSteady-state transcript levelsF1-ATPase alphaInduction of RNAiMitochondrion of TrypanosomaWild-type cellsBloodstream form TrypanosomaAlpha subunit transcriptsRNAi knockdownRNAi cellsT. bruceiTranscript levelsUninduced cellsBloodstream formsBeta subunit transcriptsSubunitsKrebs cycleFluorescence microscopy
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