| pubmed-article:1423622 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1423622 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:1423622 | lifeskim:mentions | umls-concept:C0016055 | lld:lifeskim |
| pubmed-article:1423622 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1423622 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:1423622 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:1423622 | lifeskim:mentions | umls-concept:C0205444 | lld:lifeskim |
| pubmed-article:1423622 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:1423622 | lifeskim:mentions | umls-concept:C1709061 | lld:lifeskim |
| pubmed-article:1423622 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1423622 | pubmed:dateCreated | 1992-12-11 | lld:pubmed |
| pubmed-article:1423622 | pubmed:abstractText | The solution structure of the tenth type III module of fibronectin has been determined using nuclear magnetic resonance techniques. The molecule has a fold similar to that of immunoglobulin domains, with seven beta strands forming two antiparallel beta sheets, which pack against each other. Both beta sheets contribute conserved hydrophobic residues to a compact core. The topology is more similar to that of domain 2 of CD4, PapD, and the extracellular domain of the human growth hormone receptor than to that of immunoglobulin C domains. The module contains an Arg-Gly-Asp sequence known to be involved in cell adhesion. This tripeptide is solvent exposed and lies on a conformationally mobile loop between strands F and G, consistent with its cell adhesion function. | lld:pubmed |
| pubmed-article:1423622 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1423622 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1423622 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1423622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1423622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1423622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1423622 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1423622 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:1423622 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:1423622 | pubmed:author | pubmed-author:CampbellI DID | lld:pubmed |
| pubmed-article:1423622 | pubmed:author | pubmed-author:BaronMM | lld:pubmed |
| pubmed-article:1423622 | pubmed:author | pubmed-author:BoydJJ | lld:pubmed |
| pubmed-article:1423622 | pubmed:author | pubmed-author:HarounE TET | lld:pubmed |
| pubmed-article:1423622 | pubmed:author | pubmed-author:MainA LAL | lld:pubmed |
| pubmed-article:1423622 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1423622 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:1423622 | pubmed:volume | 71 | lld:pubmed |
| pubmed-article:1423622 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1423622 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1423622 | pubmed:pagination | 671-8 | lld:pubmed |
| pubmed-article:1423622 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1423622 | pubmed:meshHeading | pubmed-meshheading:1423622-... | lld:pubmed |
| pubmed-article:1423622 | pubmed:meshHeading | pubmed-meshheading:1423622-... | lld:pubmed |
| pubmed-article:1423622 | pubmed:meshHeading | pubmed-meshheading:1423622-... | lld:pubmed |
| pubmed-article:1423622 | pubmed:meshHeading | pubmed-meshheading:1423622-... | lld:pubmed |
| pubmed-article:1423622 | pubmed:meshHeading | pubmed-meshheading:1423622-... | lld:pubmed |
| pubmed-article:1423622 | pubmed:meshHeading | pubmed-meshheading:1423622-... | lld:pubmed |
| pubmed-article:1423622 | pubmed:meshHeading | pubmed-meshheading:1423622-... | lld:pubmed |
| pubmed-article:1423622 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1423622 | pubmed:articleTitle | The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. | lld:pubmed |
| pubmed-article:1423622 | pubmed:affiliation | Department of Biochemistry, University of Oxford, England. | lld:pubmed |
| pubmed-article:1423622 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1423622 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:2335 | entrezgene:pubmed | pubmed-article:1423622 | lld:entrezgene |
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