| pubmed-article:18611274 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18611274 | lifeskim:mentions | umls-concept:C0596981 | lld:lifeskim |
| pubmed-article:18611274 | lifeskim:mentions | umls-concept:C0596997 | lld:lifeskim |
| pubmed-article:18611274 | lifeskim:mentions | umls-concept:C1423716 | lld:lifeskim |
| pubmed-article:18611274 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:18611274 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:18611274 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:18611274 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:18611274 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:18611274 | pubmed:dateCreated | 2008-7-22 | lld:pubmed |
| pubmed-article:18611274 | pubmed:abstractText | Integrins are required for normal muscle differentiation and disruptions in integrin signaling result in human muscle disease. The intracellular components that regulate integrin function during myogenesis are poorly understood. Unc-112 is an integrin-associated protein required for muscle development in C. elegans. To better understand the intracellular effectors of integrin signaling in muscle, we examined the mammalian homolog of Unc-112, kindlin-2. | lld:pubmed |
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| pubmed-article:18611274 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18611274 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18611274 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18611274 | pubmed:issn | 1471-2121 | lld:pubmed |
| pubmed-article:18611274 | pubmed:author | pubmed-author:DowlingJames... | lld:pubmed |
| pubmed-article:18611274 | pubmed:author | pubmed-author:FeldmanEva... | lld:pubmed |
| pubmed-article:18611274 | pubmed:author | pubmed-author:GoldenJeffrey... | lld:pubmed |
| pubmed-article:18611274 | pubmed:author | pubmed-author:KimSusieS | lld:pubmed |
| pubmed-article:18611274 | pubmed:author | pubmed-author:VreedeAndrew... | lld:pubmed |
| pubmed-article:18611274 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18611274 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:18611274 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18611274 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18611274 | pubmed:pagination | 36 | lld:pubmed |
| pubmed-article:18611274 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:18611274 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18611274 | pubmed:articleTitle | Kindlin-2 is required for myocyte elongation and is essential for myogenesis. | lld:pubmed |
| pubmed-article:18611274 | pubmed:affiliation | Department of Pediatrics, University of Michigan, Ann Arbor, USA. jamedowl@umich.edu | lld:pubmed |
| pubmed-article:18611274 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18611274 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18611274 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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