| pubmed-article:19945619 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19945619 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
| pubmed-article:19945619 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:19945619 | lifeskim:mentions | umls-concept:C0381368 | lld:lifeskim |
| pubmed-article:19945619 | lifeskim:mentions | umls-concept:C0600210 | lld:lifeskim |
| pubmed-article:19945619 | lifeskim:mentions | umls-concept:C1880371 | lld:lifeskim |
| pubmed-article:19945619 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:19945619 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19945619 | pubmed:dateCreated | 2009-11-30 | lld:pubmed |
| pubmed-article:19945619 | pubmed:abstractText | The laminins are a secreted family of heterotrimeric molecules essential for basement membrane formation, structure, and function. It is now well established that the alpha3 subunit of laminins-332, -321, and -311 plays an important role in mediating epidermal-dermal integrity and is essential for the skin to withstand mechanical stresses. These laminins also regulate cell migration and mechanosignal transduction. This article provides an overview of the gene, transcripts, and protein structures of laminin alpha3. Also discussed are the proposed functions for the alpha3 subunit-containing laminins. | lld:pubmed |
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| pubmed-article:19945619 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19945619 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19945619 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19945619 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19945619 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19945619 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19945619 | pubmed:issn | 1558-0520 | lld:pubmed |
| pubmed-article:19945619 | pubmed:author | pubmed-author:JonesJonathan... | lld:pubmed |
