2008
WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity
Xiao A, Li H, Shechter D, Ahn SH, Fabrizio LA, Erdjument-Bromage H, Ishibe-Murakami S, Wang B, Tempst P, Hofmann K, Patel DJ, Elledge SJ, Allis CD. WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity. Nature 2008, 457: 57-62. PMID: 19092802, PMCID: PMC2854499, DOI: 10.1038/nature07668.Peer-Reviewed Original ResearchConceptsDNA damage responseIntrinsic tyrosine kinase activityTyrosine kinase activityDamage responseKinase activityWilliams-Beuren syndrome transcription factorDouble-strand break responseNew regulatory mechanismWICH complexKinase foldEukaryotic cellsTranscription factorsWSTFKnowledge of domainsGenomic instabilityBreak responseSequence homologyRegulatory mechanismsCell deathPrecise rolePhosphorylationRepair processNew mechanismChromatinImportant role
2004
Arginine Methylation of Runx1 Regulates Its Biological and Transcriptional Activities.
Zhao X, Parkanani A, Zhang J, Dunne R, Xiao A, Allis C, Nimer S. Arginine Methylation of Runx1 Regulates Its Biological and Transcriptional Activities. Blood 2004, 104: 2041. DOI: 10.1182/blood.v104.11.2041.2041.Peer-Reviewed Original ResearchArginine methylation sitesProtein arginine methyltransferasesArginine methylationRunt domainMethylation sitesTranscriptional repression complexAbility of RUNX1Co-immunoprecipitation assaysChromatin immunoprecipitation assaysSite-specific mutagenesisCell proliferation signalsCarboxy-terminal regionLuciferase gene reporterRepression complexDefinitive hematopoiesisArginine methyltransferasesTranscriptional activatingGATA-1Repressor proteinLysine acetylationMass spectrometry analysisTranscription factorsImmunoprecipitation assaysSerine phosphorylationGene transcription