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http://purl.uniprot.org/citations/9755172http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9755172http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9755172http://www.w3.org/2000/01/rdf-schema#comment"Transcripts for a new form of Sox5, called L-Sox5, and Sox6 are coexpressed with Sox9 in all chondrogenic sites of mouse embryos. A coiled-coil domain located in the N-terminal part of L-Sox5, and absent in Sox5, showed >90% identity with a similar domain in Sox6 and mediated homodimerization and heterodimerization with Sox6. Dimerization of L-Sox5/Sox6 greatly increased efficiency of binding of the two Sox proteins to DNA containing adjacent HMG sites. L-Sox5, Sox6 and Sox9 cooperatively activated expression of the chondrocyte differentiation marker Col2a1 in 10T1/2 and MC615 cells. A 48 bp chondrocyte-specific enhancer in this gene, which contains several HMG-like sites that are necessary for enhancer activity, bound the three Sox proteins and was cooperatively activated by the three Sox proteins in non-chondrogenic cells. Our data suggest that L-Sox5/Sox6 and Sox9, which belong to two different classes of Sox transcription factors, cooperate with each other in expression of Col2a1 and possibly other genes of the chondrocytic program."xsd:string
http://purl.uniprot.org/citations/9755172http://purl.org/dc/terms/identifier"doi:10.1093/emboj/17.19.5718"xsd:string
http://purl.uniprot.org/citations/9755172http://purl.org/dc/terms/identifier"doi:10.1093/emboj/17.19.5718"xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/author"de Crombrugghe B."xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/author"de Crombrugghe B."xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/author"Lefebvre V."xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/author"Lefebvre V."xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/pages"5718-5733"xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/pages"5718-5733"xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/title"A new long form of Sox5 (L-Sox5), Sox6 and Sox9 are coexpressed in chondrogenesis and cooperatively activate the type II collagen gene."xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/title"A new long form of Sox5 (L-Sox5), Sox6 and Sox9 are coexpressed in chondrogenesis and cooperatively activate the type II collagen gene."xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/9755172http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/9755172http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9755172
http://purl.uniprot.org/citations/9755172http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9755172
http://purl.uniprot.org/citations/9755172http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9755172
http://purl.uniprot.org/citations/9755172http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9755172