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| pubmed-article:15155948 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:15155948 | lifeskim:mentions | umls-concept:C0019932 | lld:lifeskim |
| pubmed-article:15155948 | lifeskim:mentions | umls-concept:C0963992 | lld:lifeskim |
| pubmed-article:15155948 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:15155948 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:15155948 | pubmed:issue | 5674 | lld:pubmed |
| pubmed-article:15155948 | pubmed:dateCreated | 2004-5-24 | lld:pubmed |
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| pubmed-article:15155948 | pubmed:abstractText | 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. | lld:pubmed |
| pubmed-article:15155948 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15155948 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15155948 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15155948 | pubmed:month | May | lld:pubmed |
| pubmed-article:15155948 | pubmed:issn | 1095-9203 | lld:pubmed |
| pubmed-article:15155948 | pubmed:author | pubmed-author:SchererPhilip... | lld:pubmed |
| pubmed-article:15155948 | pubmed:author | pubmed-author:RossettiLucia... | lld:pubmed |
| pubmed-article:15155948 | pubmed:author | pubmed-author:ShapiroLawren... | lld:pubmed |
| pubmed-article:15155948 | pubmed:author | pubmed-author:RajalaMichael... | lld:pubmed |
| pubmed-article:15155948 | pubmed:author | pubmed-author:PatelSaurabh... | lld:pubmed |
| pubmed-article:15155948 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15155948 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:15155948 | pubmed:volume | 304 | lld:pubmed |
| pubmed-article:15155948 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15155948 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15155948 | pubmed:pagination | 1154-8 | lld:pubmed |
| pubmed-article:15155948 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:15155948 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15155948 | pubmed:articleTitle | Disulfide-dependent multimeric assembly of resistin family hormones. | lld:pubmed |
| pubmed-article:15155948 | pubmed:affiliation | Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. | lld:pubmed |
| pubmed-article:15155948 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15155948 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15155948 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:15155948 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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