| pubmed-article:21515257 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21515257 | lifeskim:mentions | umls-concept:C0007577 | lld:lifeskim |
| pubmed-article:21515257 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:21515257 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:21515257 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:21515257 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:21515257 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:21515257 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:21515257 | pubmed:dateCreated | 2011-6-20 | lld:pubmed |
| pubmed-article:21515257 | pubmed:abstractText | The ?9?1 integrin is a multifunctional receptor that interacts with a variety of ligands including vascular cell adhesion molecule 1, tenascin-C, and osteopontin. A 2.3-kb truncated form of ?9 integrin subunit cDNA was identified by searching the Medline database. This splice variant, which we called the short form of ?9 integrin (SF?9), encodes a 632-aa isoform lacking transmembrane and cytoplasmic domains, and its authentic expression was verified by PCR and Western blotting. SF?9 is expressed on the cell surface but cannot bind ligand in the absence of the full-length ?9 subunit. Over-expression of SF?9 in cells expressing full-length ?9 promotes ?9-dependent cell adhesion. This promoting effect of SF?9 requires the authentic cytoplasmic domain of the co-expressed full-length ?9 subunit. Thus, SF?9 is a novel functional modulator of ?9?1 integrin by inside-out signaling. | lld:pubmed |
| pubmed-article:21515257 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21515257 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21515257 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21515257 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21515257 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21515257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21515257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21515257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21515257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21515257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21515257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21515257 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21515257 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:21515257 | pubmed:issn | 1090-2422 | lld:pubmed |
| pubmed-article:21515257 | pubmed:author | pubmed-author:SheppardDeanD | lld:pubmed |
| pubmed-article:21515257 | pubmed:author | pubmed-author:KonShigeyukiS | lld:pubmed |
| pubmed-article:21515257 | pubmed:author | pubmed-author:AtakilitAmhaA | lld:pubmed |
| pubmed-article:21515257 | pubmed:copyrightInfo | Copyright © 2011 Elsevier Inc. All rights reserved. | lld:pubmed |
| pubmed-article:21515257 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21515257 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:21515257 | pubmed:volume | 317 | lld:pubmed |
| pubmed-article:21515257 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21515257 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21515257 | pubmed:pagination | 1774-84 | lld:pubmed |
| pubmed-article:21515257 | pubmed:meshHeading | pubmed-meshheading:21515257... | lld:pubmed |
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| pubmed-article:21515257 | pubmed:meshHeading | pubmed-meshheading:21515257... | lld:pubmed |
| pubmed-article:21515257 | pubmed:meshHeading | pubmed-meshheading:21515257... | lld:pubmed |
| pubmed-article:21515257 | pubmed:meshHeading | pubmed-meshheading:21515257... | lld:pubmed |
| pubmed-article:21515257 | pubmed:meshHeading | pubmed-meshheading:21515257... | lld:pubmed |
| pubmed-article:21515257 | pubmed:meshHeading | pubmed-meshheading:21515257... | lld:pubmed |
| pubmed-article:21515257 | pubmed:meshHeading | pubmed-meshheading:21515257... | lld:pubmed |
| pubmed-article:21515257 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21515257 | pubmed:articleTitle | Short form of ?9 promotes ?9?1 integrin-dependent cell adhesion by modulating the function of the full-length ?9 subunit. | lld:pubmed |
| pubmed-article:21515257 | pubmed:affiliation | Lung Biology Center, Department of Medicine, University of California, San Francisco, CA 94143, USA. | lld:pubmed |
| pubmed-article:21515257 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21515257 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21515257 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
