| pubmed-article:16024509 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16024509 | lifeskim:mentions | umls-concept:C1312720 | lld:lifeskim |
| pubmed-article:16024509 | lifeskim:mentions | umls-concept:C0332875 | lld:lifeskim |
| pubmed-article:16024509 | lifeskim:mentions | umls-concept:C0872079 | lld:lifeskim |
| pubmed-article:16024509 | pubmed:dateCreated | 2005-7-18 | lld:pubmed |
| pubmed-article:16024509 | pubmed:abstractText | Tetraspanins are evolutionarily conserved membrane proteins that tend to associate laterally with one another and to cluster dynamically with numerous partner proteins in membrane microdomains. Consequently, members of this family are involved in the coordination of intracellular and intercellular processes, including signal transduction; cell proliferation, adhesion, and migration; cell fusion; and host-parasite interactions. | lld:pubmed |
| pubmed-article:16024509 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16024509 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16024509 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16024509 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16024509 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16024509 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16024509 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16024509 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16024509 | pubmed:issn | 1548-9213 | lld:pubmed |
| pubmed-article:16024509 | pubmed:author | pubmed-author:LevyShoshanaS | lld:pubmed |
| pubmed-article:16024509 | pubmed:author | pubmed-author:ShohamTsipiT | lld:pubmed |
| pubmed-article:16024509 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16024509 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:16024509 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16024509 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16024509 | pubmed:pagination | 218-24 | lld:pubmed |
| pubmed-article:16024509 | pubmed:dateRevised | 2010-1-14 | lld:pubmed |
| pubmed-article:16024509 | pubmed:meshHeading | pubmed-meshheading:16024509... | lld:pubmed |
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| pubmed-article:16024509 | pubmed:meshHeading | pubmed-meshheading:16024509... | lld:pubmed |
| pubmed-article:16024509 | pubmed:meshHeading | pubmed-meshheading:16024509... | lld:pubmed |
| pubmed-article:16024509 | pubmed:meshHeading | pubmed-meshheading:16024509... | lld:pubmed |
| pubmed-article:16024509 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16024509 | pubmed:articleTitle | Protein-protein interactions in the tetraspanin web. | lld:pubmed |
| pubmed-article:16024509 | pubmed:affiliation | Division of Oncology, Department of Medicine, Stanford University Medical Center, Stanford, CA, USA. levy@cmgm.stanford.edu | lld:pubmed |
| pubmed-article:16024509 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16024509 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16024509 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:16024509 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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