| pubmed-article:17601576 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17601576 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:17601576 | lifeskim:mentions | umls-concept:C0085481 | lld:lifeskim |
| pubmed-article:17601576 | lifeskim:mentions | umls-concept:C0023820 | lld:lifeskim |
| pubmed-article:17601576 | lifeskim:mentions | umls-concept:C0020284 | lld:lifeskim |
| pubmed-article:17601576 | lifeskim:mentions | umls-concept:C0037081 | lld:lifeskim |
| pubmed-article:17601576 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:17601576 | pubmed:dateCreated | 2007-7-19 | lld:pubmed |
| pubmed-article:17601576 | pubmed:abstractText | Desulfovibrio vulgaris Hildenborough has a membrane-bound [NiFeSe] hydrogenase whose mode of membrane association was unknown since it is constituted by two hydrophilic subunits. This work shows that this hydrogenase is a bacterial lipoprotein bound to the membrane by lipidic groups found at the N-terminus of the large subunit, which is unusual since it is missing the typical lipoprotein signal peptide. Nevertheless, the large subunit has a conserved four residue lipobox and its synthesis is sensitive to the signal peptidase II inhibitor globomycin. The D. vulgaris [NiFeSe] hydrogenase is the first example of a bacterial lipoprotein translocated through the Tat pathway. | lld:pubmed |
| pubmed-article:17601576 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17601576 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17601576 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17601576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17601576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17601576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17601576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17601576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17601576 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17601576 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:17601576 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:17601576 | pubmed:author | pubmed-author:RegallaManuel... | lld:pubmed |
| pubmed-article:17601576 | pubmed:author | pubmed-author:ValenteFilipa... | lld:pubmed |
| pubmed-article:17601576 | pubmed:author | pubmed-author:PereiraPatríc... | lld:pubmed |
| pubmed-article:17601576 | pubmed:author | pubmed-author:CoelhoAna VAV | lld:pubmed |
| pubmed-article:17601576 | pubmed:author | pubmed-author:PereiraInês... | lld:pubmed |
| pubmed-article:17601576 | pubmed:author | pubmed-author:VenceslauSofi... | lld:pubmed |
| pubmed-article:17601576 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17601576 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:17601576 | pubmed:volume | 581 | lld:pubmed |
| pubmed-article:17601576 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17601576 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17601576 | pubmed:pagination | 3341-4 | lld:pubmed |
| pubmed-article:17601576 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:17601576 | pubmed:meshHeading | pubmed-meshheading:17601576... | lld:pubmed |
| pubmed-article:17601576 | pubmed:meshHeading | pubmed-meshheading:17601576... | lld:pubmed |
| pubmed-article:17601576 | pubmed:meshHeading | pubmed-meshheading:17601576... | lld:pubmed |
| pubmed-article:17601576 | pubmed:meshHeading | pubmed-meshheading:17601576... | lld:pubmed |
| pubmed-article:17601576 | pubmed:meshHeading | pubmed-meshheading:17601576... | lld:pubmed |
| pubmed-article:17601576 | pubmed:meshHeading | pubmed-meshheading:17601576... | lld:pubmed |
| pubmed-article:17601576 | pubmed:meshHeading | pubmed-meshheading:17601576... | lld:pubmed |
| pubmed-article:17601576 | pubmed:meshHeading | pubmed-meshheading:17601576... | lld:pubmed |
| pubmed-article:17601576 | pubmed:meshHeading | pubmed-meshheading:17601576... | lld:pubmed |
| pubmed-article:17601576 | pubmed:meshHeading | pubmed-meshheading:17601576... | lld:pubmed |
| pubmed-article:17601576 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17601576 | pubmed:articleTitle | The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide. | lld:pubmed |
| pubmed-article:17601576 | pubmed:affiliation | Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 1781-901 Oeiras, Portugal. | lld:pubmed |
| pubmed-article:17601576 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17601576 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17601576 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17601576 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17601576 | lld:pubmed |
