2020
RNA-based CRISPR-Mediated Loss-of-Function Mutagenesis in Human Pluripotent Stem Cells
Leung AW, Broton C, Bogacheva MS, Xiao AZ, Garcia-Castro MI, Lou YR. RNA-based CRISPR-Mediated Loss-of-Function Mutagenesis in Human Pluripotent Stem Cells. Journal Of Molecular Biology 2020, 432: 3956-3964. PMID: 32339532, DOI: 10.1016/j.jmb.2020.04.017.Peer-Reviewed Original ResearchConceptsHuman pluripotent stem cellsPluripotent stem cellsTargeting efficiencyShelf cell productsTransfection protocolShort palindromic repeatsStem cellsSelection markerGenome editingPS cell linesFunction mutagenesisImproved protocolBroad applicationsPalindromic repeatsClustered RegularlyAssociated 9Human therapyEfficiencyProtocolCell productsCRISPRCrRNARegularlyApplicationsEditing
2009
Dephosphorylation of the C-terminal Tyrosyl Residue of the DNA Damage-related Histone H2A.X Is Mediated by the Protein Phosphatase Eyes Absent*
Krishnan N, Jeong DG, Jung SK, Ryu SE, Xiao A, Allis CD, Kim SJ, Tonks NK. Dephosphorylation of the C-terminal Tyrosyl Residue of the DNA Damage-related Histone H2A.X Is Mediated by the Protein Phosphatase Eyes Absent*. Journal Of Biological Chemistry 2009, 284: 16066-16070. PMID: 19351884, PMCID: PMC2713548, DOI: 10.1074/jbc.c900032200.Peer-Reviewed Original ResearchMeSH KeywordsCell Line, TumorDNA DamageDNA-Binding ProteinsElectrochemistryHistonesHumansIntracellular Signaling Peptides and ProteinsMetalsNuclear ProteinsPhosphorylationProtein Structure, TertiaryProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine PhosphatasesRNA InterferenceSubstrate SpecificityTransfectionTyrosineConceptsEyes AbsentDNA damage responseTyr-142Damage responseTyrosyl residuesProtein tyrosine phosphataseDNA damage repairAtypical kinaseHistone H2A.X.Haloacid dehalogenaseMammalian cellsHistone H2A.XDisplayed specificityElevated basal phosphorylationPhosphorylation statusRNA interferenceDamage repairPhysiological substratesH2A.XNovel roleBasal phosphorylationImportant regulatorDephosphorylationResiduesWSTF