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http://purl.uniprot.org/citations/11295558http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11295558http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11295558http://www.w3.org/2000/01/rdf-schema#comment"Transcription factor TFIID is a multiprotein complex composed of the TATA binding protein and its associated factors, and is required for accurate and regulated initiation of transcription by RNA polymerase II. The subunit composition of this factor is highly conserved from yeast to mammals. X-ray crystallography and biochemical experiments have shown that the histone fold motif mediates many of the subunit interactions within this complex. These results, together with electron microscopy and yeast genetics, provide insights into the overall organization of this complex."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.org/dc/terms/identifier"doi:10.1016/s0968-0004(00)01741-2"xsd:string
http://purl.uniprot.org/citations/11295558http://purl.org/dc/terms/identifier"doi:10.1016/s0968-0004(00)01741-2"xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/author"Romier C."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/author"Romier C."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/author"Davidson I."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/author"Davidson I."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/author"Werten S."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/author"Werten S."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/author"Gangloff Y.G."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/author"Gangloff Y.G."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/author"Thuault S."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/author"Thuault S."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/name"Trends Biochem. Sci."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/name"Trends Biochem. Sci."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/pages"250-257"xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/pages"250-257"xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/title"The histone fold is a key structural motif of transcription factor TFIID."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/title"The histone fold is a key structural motif of transcription factor TFIID."xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/volume"26"xsd:string
http://purl.uniprot.org/citations/11295558http://purl.uniprot.org/core/volume"26"xsd:string