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http://purl.uniprot.org/citations/20681948http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20681948http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20681948http://www.w3.org/2000/01/rdf-schema#comment"RNF4 [RING (really interesting new gene) finger protein 4] family ubiquitin ligases are RING E3 ligases that regulate the homoeostasis of SUMOylated proteins by promoting their ubiquitylation. In the present paper we report that the RING domain of RNF4 forms a stable dimer, and that dimerization is required for ubiquitin transfer. Our results suggest that the stability of the E2~ubiquitin thioester bond is regulated by RING domain dimerization."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.org/dc/terms/identifier"doi:10.1042/bj20100957"xsd:string
http://purl.uniprot.org/citations/20681948http://purl.org/dc/terms/identifier"doi:10.1042/bj20100957"xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/author"Sun H."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/author"Sun H."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/author"Hunter T."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/author"Hunter T."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/author"Liew C.W."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/author"Liew C.W."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/author"Day C.L."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/author"Day C.L."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/pages"23-29"xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/pages"23-29"xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/title"RING domain dimerization is essential for RNF4 function."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/title"RING domain dimerization is essential for RNF4 function."xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/volume"431"xsd:string
http://purl.uniprot.org/citations/20681948http://purl.uniprot.org/core/volume"431"xsd:string
http://purl.uniprot.org/citations/20681948http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20681948
http://purl.uniprot.org/citations/20681948http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20681948