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http://purl.uniprot.org/citations/25514756http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25514756http://www.w3.org/2000/01/rdf-schema#comment"Multiple factors are involved in the elongation stage of transcription regulation to ensure the passing of RNA polymerases while preserving appropriate nucleosome structure thereafter. The recently reported trimeric sub-module of NuA4 histone acetyltransferase complex involved in this process provides more insight into the sophisticated modulation of transcription elongation."xsd:string
http://purl.uniprot.org/citations/25514756http://purl.org/dc/terms/identifier"doi:10.1080/21541264.2014.995571"xsd:string
http://purl.uniprot.org/citations/25514756http://purl.uniprot.org/core/author"Cheng X."xsd:string
http://purl.uniprot.org/citations/25514756http://purl.uniprot.org/core/author"Cote J."xsd:string
http://purl.uniprot.org/citations/25514756http://purl.uniprot.org/core/date"2014"xsd:gYear
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http://purl.uniprot.org/citations/25514756http://purl.uniprot.org/core/title"A new companion of elongating RNA Polymerase II: TINTIN, an independent sub-module of NuA4/TIP60 for nucleosome transactions."xsd:string
http://purl.uniprot.org/citations/25514756http://purl.uniprot.org/core/volume"5"xsd:string
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http://purl.uniprot.org/citations/25514756http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25514756
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