| pubmed-article:16647110 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16647110 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:16647110 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:16647110 | lifeskim:mentions | umls-concept:C0021641 | lld:lifeskim |
| pubmed-article:16647110 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:16647110 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:16647110 | lifeskim:mentions | umls-concept:C0205464 | lld:lifeskim |
| pubmed-article:16647110 | lifeskim:mentions | umls-concept:C0024779 | lld:lifeskim |
| pubmed-article:16647110 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16647110 | pubmed:dateCreated | 2006-5-22 | lld:pubmed |
| pubmed-article:16647110 | pubmed:abstractText | Phosphoinositide 3-kinases (PI3-Ks) are an important emerging class of drug targets, but the unique roles of PI3-K isoforms remain poorly defined. We describe here an approach to pharmacologically interrogate the PI3-K family. A chemically diverse panel of PI3-K inhibitors was synthesized, and their target selectivity was biochemically enumerated, revealing cryptic homologies across targets and chemotypes. Crystal structures of three inhibitors bound to p110gamma identify a conformationally mobile region that is uniquely exploited by selective compounds. This chemical array was then used to define the PI3-K isoforms required for insulin signaling. We find that p110alpha is the primary insulin-responsive PI3-K in cultured cells, whereas p110beta is dispensable but sets a phenotypic threshold for p110alpha activity. Compounds targeting p110alpha block the acute effects of insulin treatment in vivo, whereas a p110beta inhibitor has no effect. These results illustrate systematic target validation using a matrix of inhibitors that span a protein family. | lld:pubmed |
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| pubmed-article:16647110 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16647110 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16647110 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16647110 | pubmed:month | May | lld:pubmed |
| pubmed-article:16647110 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:16647110 | pubmed:author | pubmed-author:WilliamsRoger... | lld:pubmed |
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| pubmed-article:16647110 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16647110 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:16647110 | pubmed:volume | 125 | lld:pubmed |
| pubmed-article:16647110 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16647110 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16647110 | pubmed:pagination | 733-47 | lld:pubmed |
| pubmed-article:16647110 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:16647110 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16647110 | pubmed:articleTitle | A pharmacological map of the PI3-K family defines a role for p110alpha in insulin signaling. | lld:pubmed |
| pubmed-article:16647110 | pubmed:affiliation | Department of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California, San Francisco, CA 94143, USA. | lld:pubmed |
| pubmed-article:16647110 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16647110 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16647110 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| pubmed-article:16647110 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
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