| pubmed-article:16518399 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16518399 | lifeskim:mentions | umls-concept:C0023764 | lld:lifeskim |
| pubmed-article:16518399 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
| pubmed-article:16518399 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:16518399 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16518399 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:16518399 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16518399 | pubmed:dateCreated | 2006-5-22 | lld:pubmed |
| pubmed-article:16518399 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518399 | pubmed:abstractText | Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from Burkholderia glumae in complex with its cognate lipase. The structure reveals how Lif uses a novel alpha-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform. | lld:pubmed |
| pubmed-article:16518399 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16518399 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518399 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16518399 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518399 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518399 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518399 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518399 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518399 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16518399 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16518399 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:16518399 | pubmed:issn | 1545-9993 | lld:pubmed |
| pubmed-article:16518399 | pubmed:author | pubmed-author:SavvidesSavva... | lld:pubmed |
| pubmed-article:16518399 | pubmed:author | pubmed-author:WynsLodeL | lld:pubmed |
| pubmed-article:16518399 | pubmed:author | pubmed-author:LustigArielA | lld:pubmed |
| pubmed-article:16518399 | pubmed:author | pubmed-author:Van... | lld:pubmed |
| pubmed-article:16518399 | pubmed:author | pubmed-author:TommassenJanJ | lld:pubmed |
| pubmed-article:16518399 | pubmed:author | pubmed-author:PauwelsKrisK | lld:pubmed |
| pubmed-article:16518399 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16518399 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:16518399 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16518399 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16518399 | pubmed:pagination | 374-5 | lld:pubmed |
| pubmed-article:16518399 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:16518399 | pubmed:meshHeading | pubmed-meshheading:16518399... | lld:pubmed |
| pubmed-article:16518399 | pubmed:meshHeading | pubmed-meshheading:16518399... | lld:pubmed |
| pubmed-article:16518399 | pubmed:meshHeading | pubmed-meshheading:16518399... | lld:pubmed |
| pubmed-article:16518399 | pubmed:meshHeading | pubmed-meshheading:16518399... | lld:pubmed |
| pubmed-article:16518399 | pubmed:meshHeading | pubmed-meshheading:16518399... | lld:pubmed |
| pubmed-article:16518399 | pubmed:meshHeading | pubmed-meshheading:16518399... | lld:pubmed |
| pubmed-article:16518399 | pubmed:meshHeading | pubmed-meshheading:16518399... | lld:pubmed |
| pubmed-article:16518399 | pubmed:meshHeading | pubmed-meshheading:16518399... | lld:pubmed |
| pubmed-article:16518399 | pubmed:meshHeading | pubmed-meshheading:16518399... | lld:pubmed |
| pubmed-article:16518399 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16518399 | pubmed:articleTitle | Structure of a membrane-based steric chaperone in complex with its lipase substrate. | lld:pubmed |
| pubmed-article:16518399 | pubmed:affiliation | Department of Molecular and Cellular Interactions, Flanders Interuniversity Institute for Biotechnology (VIB) and Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium. | lld:pubmed |
| pubmed-article:16518399 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16518399 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16518399 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16518399 | lld:pubmed |
