2018
N 6 -methyladenine DNA Modification in Glioblastoma
Xie Q, Wu TP, Gimple RC, Li Z, Prager BC, Wu Q, Yu Y, Wang P, Wang Y, Gorkin DU, Zhang C, Dowiak AV, Lin K, Zeng C, Sui Y, Kim LJY, Miller TE, Jiang L, Lee-Poturalski C, Huang Z, Fang X, Zhai K, Mack SC, Sander M, Bao S, Kerstetter-Fogle AE, Sloan AE, Xiao AZ, Rich JN. N 6 -methyladenine DNA Modification in Glioblastoma. Cell 2018, 175: 1228-1243.e20. PMID: 30392959, PMCID: PMC6433469, DOI: 10.1016/j.cell.2018.10.006.Peer-Reviewed Original ResearchMeSH KeywordsAdenineAdultAgedAlkB Homolog 1, Histone H2a DioxygenaseAnimalsAstrocytesBrain NeoplasmsCell HypoxiaChildDNA MethylationEpigenomicsFemaleGlioblastomaHeterochromatinHistonesHumansKaplan-Meier EstimateMaleMiceMiddle AgedNeoplastic Stem CellsRNA InterferenceRNA, Small InterferingTumor Suppressor Protein p53ConceptsDNA modificationsHeterochromatic histone modificationsRegulation of transcriptionNovel DNA modificationChromatin accessibilityEpigenetic marksHistone modificationsTranscriptional silencingEpigenetic modificationsGenetic driversHuman diseasesOncogenic pathwaysTumor cell proliferationPotential therapeutic targetALKBH1Cell proliferationTumor-bearing miceCritical roleTherapeutic targetDNAHuman tissuesHuman glioblastoma modelGlioblastoma modelGlioblastomaSilencing
2008
Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity
Zhao X, Jankovic V, Gural A, Huang G, Pardanani A, Menendez S, Zhang J, Dunne R, Xiao A, Erdjument-Bromage H, Allis CD, Tempst P, Nimer SD. Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity. Genes & Development 2008, 22: 640-653. PMID: 18316480, PMCID: PMC2259033, DOI: 10.1101/gad.1632608.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, CD34ArginineCell Line, TumorCore Binding Factor Alpha 2 SubunitDNA-Binding ProteinsGene Expression RegulationHematopoiesisHumansMethylationMutationPlatelet Membrane Glycoprotein IIbProtein-Arginine N-MethyltransferasesProto-Oncogene ProteinsRepressor ProteinsRNA, Small InterferingRUNX1 Translocation Partner 1 ProteinSin3 Histone Deacetylase and Corepressor ComplexTrans-ActivatorsTranscription FactorsTranscription, GeneticConceptsRUNX1 functionArginine residuesRUNX1-ETO fusion proteinArginine methyltransferase PRMT1Arginine methylation sitesPRMT1-dependent methylationRUNX1 target genesProtein-protein interactionsPost-translational modificationsRUNX1/AML1Dominant inhibitory activityDefinitive hematopoiesisMethyltransferase PRMT1Corepressor Sin3ATranscriptional coactivatorPRMT1Target genesMethylation sitesDynamic regulationTranscriptional activityCorepressor bindingHuman acute leukemiaFusion proteinChromosome translocationRUNX1