2022
Reversal of synapse loss in Alzheimer mouse models by targeting mGluR5 to prevent synaptic tagging by C1Q
Spurrier J, Nicholson L, Fang XT, Stoner AJ, Toyonaga T, Holden D, Siegert TR, Laird W, Allnutt MA, Chiasseu M, Brody AH, Takahashi H, Nies SH, Pérez-Cañamás A, Sadasivam P, Lee S, Li S, Zhang L, Huang YH, Carson RE, Cai Z, Strittmatter SM. Reversal of synapse loss in Alzheimer mouse models by targeting mGluR5 to prevent synaptic tagging by C1Q. Science Translational Medicine 2022, 14: eabi8593. PMID: 35648810, PMCID: PMC9554345, DOI: 10.1126/scitranslmed.abi8593.Peer-Reviewed Original ResearchMeSH KeywordsAlzheimer DiseaseAnimalsComplement C1qDisease Models, AnimalMiceReceptor, Metabotropic Glutamate 5SynapsesConceptsPositron emission tomographySilent allosteric modulatorsAlzheimer's diseaseMouse modelPhospho-tau accumulationAged mouse modelAlzheimer mouse modelImmune-mediated attackSAM treatmentMicroglial mediatorsSynaptic engulfmentSynaptic lossAD miceComplement component C1qSynapse lossGlutamate responseSynaptic densityDrug washoutSynaptic localizationTherapeutic benefitCognitive impairmentAllosteric modulatorsEmission tomographyNonhuman primatesComponent C1q
2013
Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model
Liu B, Wang Z, Zhang L, Ghosh S, Zheng H, Zhou Z. Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model. Nature Communications 2013, 4: 1868. PMID: 23695662, PMCID: PMC3674265, DOI: 10.1038/ncomms2885.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDisease Models, AnimalDNA DamageDNA RepairEnzyme StabilityFibroblastsHEK293 CellsHeterochromatinHistonesHumansLamin Type ALongevityLysineMethylationMethyltransferasesMiceNuclear ProteinsProgeriaProtein BindingProtein PrecursorsProtein Processing, Post-TranslationalRepressor ProteinsConceptsHutchinson-Gilford progeria syndromeBody weight lossBone mineral densityProgeria syndromeDNA repair capacityMineral densityMouse modelProgeria mouse modelG608G mutationSyndromeWeight lossProgeroid featuresRepair capacityH3K9me3 levelsPremature agingG mutationPotential strategyEpigenetic alterations
2011
Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice
Krishnan V, Chow MZ, Wang Z, Zhang L, Liu B, Liu X, Zhou Z. Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 12325-12330. PMID: 21746928, PMCID: PMC3145730, DOI: 10.1073/pnas.1102789108.Peer-Reviewed Original ResearchMeSH KeywordsAcetylationAgingAging, PrematureAnimalsCells, CulturedCellular SenescenceChromosomal Proteins, Non-HistoneDisease Models, AnimalDNA RepairDNA-Binding ProteinsHistone AcetyltransferasesHistone Deacetylase InhibitorsHistonesHumansLamin Type ALysineMembrane ProteinsMetalloendopeptidasesMiceMice, KnockoutNuclear MatrixNuclear ProteinsProtein PrecursorsRNA, Small InterferingTumor Suppressor p53-Binding Protein 1ConceptsDNA damage responseHutchinson-Gilford progeria syndromeDamage responseProgeria syndromeRepair protein recruitmentDNA damage sitesZmpste24-deficient miceAge-associated phenotypesDefective DNA repairChromatin modificationsProtein recruitmentEpigenetic marksHistone H4Histone acetyltransferaseNuclear matrixSpecific point mutationsDNA repairLamin AGenomic instabilityEpigenetic changesRepair proteinsHistone deacetylase inhibitorsCellular senescenceMOF overexpressionMolecular mechanisms