| pubmed-article:15710040 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15710040 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:15710040 | lifeskim:mentions | umls-concept:C0052350 | lld:lifeskim |
| pubmed-article:15710040 | lifeskim:mentions | umls-concept:C0020276 | lld:lifeskim |
| pubmed-article:15710040 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:15710040 | lifeskim:mentions | umls-concept:C2699006 | lld:lifeskim |
| pubmed-article:15710040 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:15710040 | pubmed:dateCreated | 2005-3-3 | lld:pubmed |
| pubmed-article:15710040 | pubmed:abstractText | The Arg-Gly-Asp (RGD) cell adhesion sequence occurs in several extracellular matrix molecules known to interact with integrin cell-surface receptors. Recently published crystal structures of the extracellular regions of two integrins in complex with peptides containing or mimicking the RGD sequence have identified the Arg and Asp residues as key specificity determinants for integrin recognition, through hydrogen bonding and metal coordination interactions. The central Gly residue also appears to be in close contact with the integrin surface in these structures. | lld:pubmed |
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| pubmed-article:15710040 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15710040 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15710040 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15710040 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15710040 | pubmed:issn | 1472-6807 | lld:pubmed |
| pubmed-article:15710040 | pubmed:author | pubmed-author:HumphriesMart... | lld:pubmed |
| pubmed-article:15710040 | pubmed:author | pubmed-author:BellaJordiJ | lld:pubmed |
| pubmed-article:15710040 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15710040 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:15710040 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15710040 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15710040 | pubmed:pagination | 4 | lld:pubmed |
| pubmed-article:15710040 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15710040 | pubmed:meshHeading | pubmed-meshheading:15710040... | lld:pubmed |
| pubmed-article:15710040 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15710040 | pubmed:articleTitle | Calpha-H...O = C hydrogen bonds contribute to the specificity of RGD cell-adhesion interactions. | lld:pubmed |
| pubmed-article:15710040 | pubmed:affiliation | Wellcome Trust Centre for Cell Matrix Research, Faculty of Life Sciences, University of Manchester. jordi.bella@manchester.ac.uk | lld:pubmed |
| pubmed-article:15710040 | pubmed:publicationType | Journal Article | lld:pubmed |
