| pubmed-article:18261887 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C0016055 | lld:lifeskim |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C0425245 | lld:lifeskim |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C0001674 | lld:lifeskim |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C1709450 | lld:lifeskim |
| pubmed-article:18261887 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:18261887 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18261887 | pubmed:dateCreated | 2008-5-5 | lld:pubmed |
| pubmed-article:18261887 | pubmed:abstractText | The 9th-10th type III fibronectin domain pair (9-10FNIII) has found widespread use as a biomimetic surface for cell adhesion. However, the effect of mutations to 9-10FNIII on its surface adsorption characteristics have not been investigated. Here we address this issue using total internal reflection fluorescence (TIRF) and circular dichroism spectroscopy, comparing two conformationally stable 9-10FNIII mutants against the wild type. Desorption of the 9-10FNIII mutants from the silica surface was minimal in comparison to desorption of 9-10FNIII. The extent and rate of protein desorption from silica was empirically matched by loss of secondary structure upon adsorption, with only the spectrum for 9-10FNIII showing extensive loss of the beta-sandwich fold. For the proteins adsorbed to hydrophobic surfaces, only the CD spectra for the 9-10FNIII mutant constrained via an interdomain disulphide bridge showed similarity with the corresponding solution structure. Since the binding of 9-10FNIII to integrin alpha5beta1 is highly dependent on the relative spatial arrangement of the two domains, we suggest that the observed differences in cell adhesion and spreading on wild type 9-10FNIII and mutants may in part be attributed to the extent of protein desorption and unfolding at the surface. | lld:pubmed |
| pubmed-article:18261887 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18261887 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18261887 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18261887 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18261887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18261887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18261887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18261887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18261887 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18261887 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:18261887 | pubmed:issn | 0927-7765 | lld:pubmed |
| pubmed-article:18261887 | pubmed:author | pubmed-author:PereiraPP | lld:pubmed |
| pubmed-article:18261887 | pubmed:author | pubmed-author:KellsS SSS | lld:pubmed |
| pubmed-article:18261887 | pubmed:author | pubmed-author:GellertP RPR | lld:pubmed |
| pubmed-article:18261887 | pubmed:author | pubmed-author:van der... | lld:pubmed |
| pubmed-article:18261887 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18261887 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:18261887 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:18261887 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18261887 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18261887 | pubmed:pagination | 1-9 | lld:pubmed |
| pubmed-article:18261887 | pubmed:dateRevised | 2009-10-16 | lld:pubmed |
| pubmed-article:18261887 | pubmed:meshHeading | pubmed-meshheading:18261887... | lld:pubmed |
| pubmed-article:18261887 | pubmed:meshHeading | pubmed-meshheading:18261887... | lld:pubmed |
| pubmed-article:18261887 | pubmed:meshHeading | pubmed-meshheading:18261887... | lld:pubmed |
| pubmed-article:18261887 | pubmed:meshHeading | pubmed-meshheading:18261887... | lld:pubmed |
| pubmed-article:18261887 | pubmed:meshHeading | pubmed-meshheading:18261887... | lld:pubmed |
| pubmed-article:18261887 | pubmed:meshHeading | pubmed-meshheading:18261887... | lld:pubmed |
| pubmed-article:18261887 | pubmed:meshHeading | pubmed-meshheading:18261887... | lld:pubmed |
| pubmed-article:18261887 | pubmed:meshHeading | pubmed-meshheading:18261887... | lld:pubmed |
| pubmed-article:18261887 | pubmed:meshHeading | pubmed-meshheading:18261887... | lld:pubmed |
| pubmed-article:18261887 | pubmed:meshHeading | pubmed-meshheading:18261887... | lld:pubmed |
| pubmed-article:18261887 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18261887 | pubmed:articleTitle | Interdomain mobility and conformational stability of type III fibronectin domain pairs control surface adsorption, desorption and unfolding. | lld:pubmed |
| pubmed-article:18261887 | pubmed:affiliation | Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, 27 Taylor Street, Glasgow, UK. | lld:pubmed |
| pubmed-article:18261887 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18261887 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
