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| http://purl.uniprot.org/citations/12596909 | http://www.w3.org/2000/01/rdf-schema#comment | "Multiple chromatin modifying proteins and multisubunit complexes have been characterized in recent years. Histone acetyltransferase (HAT) activities have been the most thoroughly studied, both biochemically and functionally. This review sums up the current knowledge on a specific group of proteins that is extremely well conserved throughout evolution, the MYST family of histone acetyltransferases. These proteins play critical roles in various nuclear functions and the control of cell proliferation."xsd:string |
| http://purl.uniprot.org/citations/12596909 | http://purl.org/dc/terms/identifier | "doi:10.1007/978-3-642-55747-7_8"xsd:string |
| http://purl.uniprot.org/citations/12596909 | http://purl.uniprot.org/core/author | "Cote J."xsd:string |
| http://purl.uniprot.org/citations/12596909 | http://purl.uniprot.org/core/author | "Utley R.T."xsd:string |
| http://purl.uniprot.org/citations/12596909 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12596909 | http://purl.uniprot.org/core/name | "Curr Top Microbiol Immunol"xsd:string |
| http://purl.uniprot.org/citations/12596909 | http://purl.uniprot.org/core/pages | "203-236"xsd:string |
| http://purl.uniprot.org/citations/12596909 | http://purl.uniprot.org/core/title | "The MYST family of histone acetyltransferases."xsd:string |
| http://purl.uniprot.org/citations/12596909 | http://purl.uniprot.org/core/volume | "274"xsd:string |
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