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http://purl.uniprot.org/citations/16360036http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16360036http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16360036http://www.w3.org/2000/01/rdf-schema#comment"In response to DNA damage, mammalian cells trigger the p53-dependent transcriptional induction of factors that regulate DNA repair, cell-cycle progression, or cell survival. Through differential proteomics, we identify heterogeneous nuclear ribonucleoprotein K (hnRNP K) as being rapidly induced by DNA damage in a manner that requires the DNA-damage signaling kinases ATM or ATR. Induction of hnRNP K ensues through the inhibition of its ubiquitin-dependent proteasomal degradation mediated by the ubiquitin E3 ligase HDM2/MDM2. Strikingly, hnRNP K depletion abrogates transcriptional induction of p53 target genes and causes defects in DNA-damage-induced cell-cycle-checkpoint arrests. Furthermore, in response to DNA damage, p53 and hnRNP K are recruited to the promoters of p53-responsive genes in a mutually dependent manner. These findings establish hnRNP K as a new HDM2 target and show that, by serving as a cofactor for p53, hnRNP K plays key roles in coordinating transcriptional responses to DNA damage."xsd:string
http://purl.uniprot.org/citations/16360036http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2005.09.032"xsd:string
http://purl.uniprot.org/citations/16360036http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2005.09.032"xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/author"Jackson S.P."xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/author"Jackson S.P."xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/author"O'Connor M.J."xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/author"O'Connor M.J."xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/author"Masterson P."xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/author"Masterson P."xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/author"Moumen A."xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/author"Moumen A."xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/pages"1065-1078"xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/pages"1065-1078"xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/title"hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage."xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/title"hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage."xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/volume"123"xsd:string
http://purl.uniprot.org/citations/16360036http://purl.uniprot.org/core/volume"123"xsd:string
http://purl.uniprot.org/citations/16360036http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16360036
http://purl.uniprot.org/citations/16360036http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16360036