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http://purl.uniprot.org/citations/9448000http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9448000http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9448000http://www.w3.org/2000/01/rdf-schema#comment"The estrogen receptor (ER) modulates transcription by forming complexes with other proteins and then binding to the estrogen response element (ERE). We have identified a novel interaction of this receptor with the POU transcription factors Brn-3a and Brn-3b which was independent of ligand binding. By pull-down assays and the yeast two-hybrid system, the POU domain of Brn-3a and Brn-3b was shown to interact with the DNA-binding domain of the ER. Brn-3-ER interactions also affect transcriptional activity of an ERE-containing promoter, such that in estradiol-stimulated cells, Brn-3b strongly activated the promoter via the ERE, while Brn-3a had a mild inhibitory effect. The POU domain of Brn-3b which interacts with the ER was sufficient to confer this activation potential, and the change of a single amino acid in the first helix of the POU homeodomain of Brn-3a to its equivalent in Brn-3b can change the mild repressive effect of Brn-3a to a stimulatory Brn-3b-like effect. These observations and their implications for transcriptional regulation by the ER are discussed."xsd:string
http://purl.uniprot.org/citations/9448000http://purl.org/dc/terms/identifier"doi:10.1128/mcb.18.2.1029"xsd:string
http://purl.uniprot.org/citations/9448000http://purl.org/dc/terms/identifier"doi:10.1128/mcb.18.2.1029"xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/author"Parker M."xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/author"Parker M."xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/author"Latchman D.S."xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/author"Latchman D.S."xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/author"Budhram-Mahadeo V."xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/author"Budhram-Mahadeo V."xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/pages"1029-1041"xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/pages"1029-1041"xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/title"POU transcription factors Brn-3a and Brn-3b interact with the estrogen receptor and differentially regulate transcriptional activity via an estrogen response element."xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/title"POU transcription factors Brn-3a and Brn-3b interact with the estrogen receptor and differentially regulate transcriptional activity via an estrogen response element."xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/9448000http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/9448000http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9448000
http://purl.uniprot.org/citations/9448000http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9448000
http://purl.uniprot.org/citations/9448000http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9448000
http://purl.uniprot.org/citations/9448000http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9448000