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http://purl.uniprot.org/citations/11839798http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11839798http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11839798http://www.w3.org/2000/01/rdf-schema#comment"The c-Myc oncoprotein functions as a transcription factor that can transform normal cells into tumor cells, as well as playing a direct role in normal cell proliferation. The c-Myc protein transactivates cellular promoters by recruiting nuclear cofactors to chromosomal sites through an N-terminal transactivation domain. We have previously reported the identification and functional characterization of four different c-Myc cofactors: TRRAP, hGCN5, TIP49, and TIP48. Here we present the identification and characterization of the actin-related protein BAF53 as a c-Myc-interacting nuclear cofactor that forms distinct nuclear complexes. In addition to the human SWI/SNF-related BAF complex, BAF53 forms a complex with TIP49 and TIP48 and a separate biochemically distinct complex containing TRRAP and a histone acetyltransferase which does not contain TIP60. Using deletion mutants of BAF53, we show that BAF53 is critical for c-Myc oncogenic activity. Our results indicate that BAF53 plays a functional role in c-Myc-interacting nuclear complexes."xsd:string
http://purl.uniprot.org/citations/11839798http://purl.org/dc/terms/identifier"doi:10.1128/mcb.22.5.1307-1316.2002"xsd:string
http://purl.uniprot.org/citations/11839798http://purl.org/dc/terms/identifier"doi:10.1128/mcb.22.5.1307-1316.2002"xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/author"Park J."xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/author"Park J."xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/author"Cole M.D."xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/author"Cole M.D."xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/author"Wood M.A."xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/author"Wood M.A."xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/pages"1307-1316"xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/pages"1307-1316"xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/title"BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation."xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/title"BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation."xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/11839798http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/11839798http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11839798
http://purl.uniprot.org/citations/11839798http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11839798
http://purl.uniprot.org/citations/11839798http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11839798
http://purl.uniprot.org/citations/11839798http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11839798