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http://purl.uniprot.org/citations/15155948http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15155948http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15155948http://www.w3.org/2000/01/rdf-schema#comment"Resistin, founding member of the resistin-like molecule (RELM) hormone family, is secreted selectively from adipocytes and induces liver-specific antagonism of insulin action, thus providing a potential molecular link between obesity and diabetes. Crystal structures of resistin and RELMbeta reveal an unusual multimeric structure. Each protomer comprises a carboxy-terminal disulfide-rich beta-sandwich "head" domain and an amino-terminal alpha-helical "tail" segment. The alpha-helical segments associate to form three-stranded coiled coils, and surface-exposed interchain disulfide linkages mediate the formation of tail-to-tail hexamers. Analysis of serum samples shows that resistin circulates in two distinct assembly states, likely corresponding to hexamers and trimers. Infusion of a resistin mutant, lacking the intertrimer disulfide bonds, in pancreatic-insulin clamp studies reveals substantially more potent effects on hepatic insulin sensitivity than those observed with wild-type resistin. This result suggests that processing of the intertrimer disulfide bonds may reflect an obligatory step toward activation."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.org/dc/terms/identifier"doi:10.1126/science.1093466"xsd:string
http://purl.uniprot.org/citations/15155948http://purl.org/dc/terms/identifier"doi:10.1126/science.1093466"xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/author"Patel S.D."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/author"Patel S.D."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/author"Scherer P.E."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/author"Scherer P.E."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/author"Shapiro L."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/author"Shapiro L."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/author"Rossetti L."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/author"Rossetti L."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/author"Rajala M.W."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/author"Rajala M.W."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/pages"1154-1158"xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/pages"1154-1158"xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/title"Disulfide-dependent multimeric assembly of resistin family hormones."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/title"Disulfide-dependent multimeric assembly of resistin family hormones."xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/volume"304"xsd:string
http://purl.uniprot.org/citations/15155948http://purl.uniprot.org/core/volume"304"xsd:string