| pubmed-article:15383714 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15383714 | lifeskim:mentions | umls-concept:C0031921 | lld:lifeskim |
| pubmed-article:15383714 | lifeskim:mentions | umls-concept:C0580797 | lld:lifeskim |
| pubmed-article:15383714 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
| pubmed-article:15383714 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
| pubmed-article:15383714 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:15383714 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
| pubmed-article:15383714 | lifeskim:mentions | umls-concept:C1707959 | lld:lifeskim |
| pubmed-article:15383714 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:15383714 | pubmed:dateCreated | 2004-9-22 | lld:pubmed |
| pubmed-article:15383714 | pubmed:abstractText | An overwhelming number of infectious diseases in both humans and animals are initiated by bacterial adhesion to carbohydrate structures on a mucosal surface. Most bacterial pathogens mediate this adhesion by fimbriae or pili which contain an adhesive lectin subunit. The importance of fimbriae as virulence factors led to research elucidating the regulation of fimbrial expression and their molecular assembly process. This review provides an overview of the current knowledge of induction, expression and assembly of F4 (K88) fimbriae and discusses its unique as well as its identical characteristics compared to other intensively studied fimbriae or pili expressed by Escherichia coli. | lld:pubmed |
| pubmed-article:15383714 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15383714 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15383714 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15383714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15383714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15383714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15383714 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15383714 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15383714 | pubmed:issn | 1464-1801 | lld:pubmed |
| pubmed-article:15383714 | pubmed:author | pubmed-author:VerdonckFF | lld:pubmed |
| pubmed-article:15383714 | pubmed:author | pubmed-author:CoxEE | lld:pubmed |
| pubmed-article:15383714 | pubmed:author | pubmed-author:GoddeerisB... | lld:pubmed |
| pubmed-article:15383714 | pubmed:copyrightInfo | Copyright 2004 S. Karger AG, Basel | lld:pubmed |
| pubmed-article:15383714 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15383714 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:15383714 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15383714 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15383714 | pubmed:pagination | 155-69 | lld:pubmed |
| pubmed-article:15383714 | pubmed:dateRevised | 2005-11-16 | lld:pubmed |
| pubmed-article:15383714 | pubmed:meshHeading | pubmed-meshheading:15383714... | lld:pubmed |
| pubmed-article:15383714 | pubmed:meshHeading | pubmed-meshheading:15383714... | lld:pubmed |
| pubmed-article:15383714 | pubmed:meshHeading | pubmed-meshheading:15383714... | lld:pubmed |
| pubmed-article:15383714 | pubmed:meshHeading | pubmed-meshheading:15383714... | lld:pubmed |
| pubmed-article:15383714 | pubmed:meshHeading | pubmed-meshheading:15383714... | lld:pubmed |
| pubmed-article:15383714 | pubmed:meshHeading | pubmed-meshheading:15383714... | lld:pubmed |
| pubmed-article:15383714 | pubmed:meshHeading | pubmed-meshheading:15383714... | lld:pubmed |
| pubmed-article:15383714 | pubmed:meshHeading | pubmed-meshheading:15383714... | lld:pubmed |
| pubmed-article:15383714 | pubmed:meshHeading | pubmed-meshheading:15383714... | lld:pubmed |
| pubmed-article:15383714 | pubmed:meshHeading | pubmed-meshheading:15383714... | lld:pubmed |
| pubmed-article:15383714 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15383714 | pubmed:articleTitle | F4 fimbriae expressed by porcine enterotoxigenic Escherichia coli, an example of an eccentric fimbrial system? | lld:pubmed |
| pubmed-article:15383714 | pubmed:affiliation | Laboratory of Veterinary Immunology, Faculty of Veterinary Medicine, Ghent University, Merelbeke, Belgium. Frank.Verdonck@UGent.be | lld:pubmed |
| pubmed-article:15383714 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15383714 | pubmed:publicationType | Review | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15383714 | lld:pubmed |
