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http://purl.uniprot.org/citations/9171108http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9171108http://www.w3.org/2000/01/rdf-schema#comment"The class II trans-activator (CIITA) is the main transcriptional co-activator for the expression of MHC class II proteins. Its N-terminal 125 amino acids function as an independent transcriptional activation domain. Analyses of the primary amino acid sequence of the activation domain predict the presence of three alpha-helices, each with a high proportion of acidic residues. Using site-directed mutagenesis, we found that two of these predicted alpha-helices are required for full transcriptional activation by CIITA. Moreover, a CIITA protein in which both functional alpha-helices have been deleted displays a dominant negative phenotype. This activation domain of CIITA interacts with the 32 kDa subunit of the general transcription complex TFIID, TAFII32. Decreased transcriptional activation by N-terminal deletions of CIITA is correlated directly with their reduced binding to TAFII32. We conclude that interactions between TAFII32 and CIITA are responsible for activation of class II genes."xsd:string
http://purl.uniprot.org/citations/9171108http://purl.org/dc/terms/identifier"doi:10.1093/nar/25.12.2522"xsd:string
http://purl.uniprot.org/citations/9171108http://purl.uniprot.org/core/author"Jiang B."xsd:string
http://purl.uniprot.org/citations/9171108http://purl.uniprot.org/core/author"Peterlin B.M."xsd:string
http://purl.uniprot.org/citations/9171108http://purl.uniprot.org/core/author"Fontes J.D."xsd:string
http://purl.uniprot.org/citations/9171108http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9171108http://purl.uniprot.org/core/name"Nucleic Acids Res"xsd:string
http://purl.uniprot.org/citations/9171108http://purl.uniprot.org/core/pages"2522-2528"xsd:string
http://purl.uniprot.org/citations/9171108http://purl.uniprot.org/core/title"The class II trans-activator CIITA interacts with the TBP-associated factor TAFII32."xsd:string
http://purl.uniprot.org/citations/9171108http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/9171108http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9171108
http://purl.uniprot.org/citations/9171108http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9171108
http://purl.uniprot.org/uniprot/P33076#attribution-0647A2D1CEE441E12D048A55388E100Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9171108
http://purl.uniprot.org/uniprot/Q16594#attribution-0647A2D1CEE441E12D048A55388E100Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9171108