| pubmed-article:17142917 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17142917 | lifeskim:mentions | umls-concept:C0243040 | lld:lifeskim |
| pubmed-article:17142917 | lifeskim:mentions | umls-concept:C1706395 | lld:lifeskim |
| pubmed-article:17142917 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:17142917 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:17142917 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:17142917 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:17142917 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:17142917 | pubmed:issue | Pt 12 | lld:pubmed |
| pubmed-article:17142917 | pubmed:dateCreated | 2006-12-4 | lld:pubmed |
| pubmed-article:17142917 | pubmed:abstractText | FedF is the two-domain tip adhesin of F18 fimbriae from enterotoxigenic Escherichia coli. Bacterial adherence, mediated by the N-terminal receptor-binding domain of FedF to carbohydrate receptors on intestinal microvilli, causes diarrhoea and oedema disease in newly weaned piglets and induces the secretion of Shiga toxins. A truncate containing only the receptor-binding domain of FedF was found to be further cleaved at its N-terminus. Reconstruction of this N-terminal truncate rendered FedF amenable to crystallization, resulting in crystals with space group P2(1)2(1)2(1) and unit-cell parameters a = 36.20, b = 74.64, c = 99.03 A that diffracted to beyond 2 A resolution. The binding specificity of FedF was screened for on a glycan array, exposing 264 glycoconjugates, to identify specific receptors for cocrystallization with FedF. | lld:pubmed |
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| pubmed-article:17142917 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17142917 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17142917 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17142917 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17142917 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17142917 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:17142917 | pubmed:issn | 1744-3091 | lld:pubmed |
| pubmed-article:17142917 | pubmed:author | pubmed-author:WynsLodeL | lld:pubmed |
| pubmed-article:17142917 | pubmed:author | pubmed-author:BrysLeaL | lld:pubmed |
| pubmed-article:17142917 | pubmed:author | pubmed-author:BouckaertJuli... | lld:pubmed |
| pubmed-article:17142917 | pubmed:author | pubmed-author:De... | lld:pubmed |
| pubmed-article:17142917 | pubmed:author | pubmed-author:Van... | lld:pubmed |
| pubmed-article:17142917 | pubmed:author | pubmed-author:De... | lld:pubmed |
| pubmed-article:17142917 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17142917 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17142917 | pubmed:volume | 62 | lld:pubmed |
| pubmed-article:17142917 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17142917 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17142917 | pubmed:pagination | 1278-82 | lld:pubmed |
| pubmed-article:17142917 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:17142917 | pubmed:meshHeading | pubmed-meshheading:17142917... | lld:pubmed |
| pubmed-article:17142917 | pubmed:meshHeading | pubmed-meshheading:17142917... | lld:pubmed |
| pubmed-article:17142917 | pubmed:meshHeading | pubmed-meshheading:17142917... | lld:pubmed |
| pubmed-article:17142917 | pubmed:meshHeading | pubmed-meshheading:17142917... | lld:pubmed |
| pubmed-article:17142917 | pubmed:meshHeading | pubmed-meshheading:17142917... | lld:pubmed |
| pubmed-article:17142917 | pubmed:meshHeading | pubmed-meshheading:17142917... | lld:pubmed |
| pubmed-article:17142917 | pubmed:meshHeading | pubmed-meshheading:17142917... | lld:pubmed |
| pubmed-article:17142917 | pubmed:meshHeading | pubmed-meshheading:17142917... | lld:pubmed |
| pubmed-article:17142917 | pubmed:meshHeading | pubmed-meshheading:17142917... | lld:pubmed |
| pubmed-article:17142917 | pubmed:meshHeading | pubmed-meshheading:17142917... | lld:pubmed |
| pubmed-article:17142917 | pubmed:meshHeading | pubmed-meshheading:17142917... | lld:pubmed |
| pubmed-article:17142917 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17142917 | pubmed:articleTitle | N-terminal truncation enables crystallization of the receptor-binding domain of the FedF bacterial adhesin. | lld:pubmed |
| pubmed-article:17142917 | pubmed:affiliation | Department of Ultrastructure, Vrije Universiteit Brussel, Flanders Interuniversity Institute for Biotechnology, Pleinlaan 2, 1050 Brussels, Belgium. | lld:pubmed |
| pubmed-article:17142917 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17142917 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17142917 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17142917 | lld:entrezgene |
