| pubmed-article:14659543 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14659543 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:14659543 | lifeskim:mentions | umls-concept:C0079488 | lld:lifeskim |
| pubmed-article:14659543 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:14659543 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:14659543 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:14659543 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:14659543 | pubmed:dateCreated | 2003-12-8 | lld:pubmed |
| pubmed-article:14659543 | pubmed:abstractText | The Sec machinery is one mechanism used by bacteria to translocate proteins across their cytoplasmic membrane. Most of the Sec components have been identified within the important gastric pathogen, Helicobacter pylori, however their functionality has not yet been demonstrated. Here we report the existence of putative homologues to the Sec components yajC (HP1450) and yidC (HP1551), and demonstrate the ability of the H. pylori secD (HP1550) and secG (HP1255) homologues to facilitate inner membrane translocation of the maltose-binding protein MalE, by complementation of the respective secretion-deficient Escherichia coli mutants, thus providing evidence of their functionality. | lld:pubmed |
| pubmed-article:14659543 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14659543 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14659543 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14659543 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14659543 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14659543 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14659543 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14659543 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14659543 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14659543 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14659543 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14659543 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14659543 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14659543 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14659543 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:14659543 | pubmed:issn | 0378-1097 | lld:pubmed |
| pubmed-article:14659543 | pubmed:author | pubmed-author:WilliamsPaulP | lld:pubmed |
| pubmed-article:14659543 | pubmed:author | pubmed-author:HardieKim RKR | lld:pubmed |
| pubmed-article:14659543 | pubmed:author | pubmed-author:FitchenNicola... | lld:pubmed |
| pubmed-article:14659543 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14659543 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:14659543 | pubmed:volume | 229 | lld:pubmed |
| pubmed-article:14659543 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14659543 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14659543 | pubmed:pagination | 57-63 | lld:pubmed |
| pubmed-article:14659543 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:14659543 | pubmed:meshHeading | pubmed-meshheading:14659543... | lld:pubmed |
| pubmed-article:14659543 | pubmed:meshHeading | pubmed-meshheading:14659543... | lld:pubmed |
| pubmed-article:14659543 | pubmed:meshHeading | pubmed-meshheading:14659543... | lld:pubmed |
| pubmed-article:14659543 | pubmed:meshHeading | pubmed-meshheading:14659543... | lld:pubmed |
| pubmed-article:14659543 | pubmed:meshHeading | pubmed-meshheading:14659543... | lld:pubmed |
| pubmed-article:14659543 | pubmed:meshHeading | pubmed-meshheading:14659543... | lld:pubmed |
| pubmed-article:14659543 | pubmed:meshHeading | pubmed-meshheading:14659543... | lld:pubmed |
| pubmed-article:14659543 | pubmed:meshHeading | pubmed-meshheading:14659543... | lld:pubmed |
| pubmed-article:14659543 | pubmed:meshHeading | pubmed-meshheading:14659543... | lld:pubmed |
| pubmed-article:14659543 | pubmed:meshHeading | pubmed-meshheading:14659543... | lld:pubmed |
| pubmed-article:14659543 | pubmed:meshHeading | pubmed-meshheading:14659543... | lld:pubmed |
| pubmed-article:14659543 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14659543 | pubmed:articleTitle | Functional complementation of E. coli secD and secG mutants by Helicobacter pylori homologues. | lld:pubmed |
| pubmed-article:14659543 | pubmed:affiliation | Institute of Infection, Immunity, and Inflammation, University of Nottingham, Queen's Medical School, C-floor West block, Nottingham NG7 2UH, UK. | lld:pubmed |
| pubmed-article:14659543 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14659543 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:949133 | entrezgene:pubmed | pubmed-article:14659543 | lld:entrezgene |
| entrez-gene:947720 | entrezgene:pubmed | pubmed-article:14659543 | lld:entrezgene |
