| pubmed-article:2838466 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2838466 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:2838466 | lifeskim:mentions | umls-concept:C1159339 | lld:lifeskim |
| pubmed-article:2838466 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:2838466 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:2838466 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:2838466 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:2838466 | lifeskim:mentions | umls-concept:C0243067 | lld:lifeskim |
| pubmed-article:2838466 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:2838466 | pubmed:dateCreated | 1988-8-4 | lld:pubmed |
| pubmed-article:2838466 | pubmed:abstractText | SecA protein synthesis levels were elevated 10- to 20-fold when protein secretion was blocked in secA, secD, and secY mutants or in a malE-lacZ fusion-containing strain but not in a secB null mutant. An active secB gene product was not required to derepress secA, since SecA levels were elevated during protein export blocks in secB secY and secB malE-lacZ double mutants. | lld:pubmed |
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| pubmed-article:2838466 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2838466 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2838466 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2838466 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2838466 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:2838466 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:2838466 | pubmed:author | pubmed-author:OliverD BDB | lld:pubmed |
| pubmed-article:2838466 | pubmed:author | pubmed-author:RolloE EEE | lld:pubmed |
| pubmed-article:2838466 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2838466 | pubmed:volume | 170 | lld:pubmed |
| pubmed-article:2838466 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2838466 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2838466 | pubmed:pagination | 3281-2 | lld:pubmed |
| pubmed-article:2838466 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:2838466 | pubmed:meshHeading | pubmed-meshheading:2838466-... | lld:pubmed |
| pubmed-article:2838466 | pubmed:meshHeading | pubmed-meshheading:2838466-... | lld:pubmed |
| pubmed-article:2838466 | pubmed:meshHeading | pubmed-meshheading:2838466-... | lld:pubmed |
| pubmed-article:2838466 | pubmed:meshHeading | pubmed-meshheading:2838466-... | lld:pubmed |
| pubmed-article:2838466 | pubmed:meshHeading | pubmed-meshheading:2838466-... | lld:pubmed |
| pubmed-article:2838466 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2838466 | pubmed:articleTitle | Regulation of the Escherichia coli secA gene by protein secretion defects: analysis of secA, secB, secD, and secY mutants. | lld:pubmed |
| pubmed-article:2838466 | pubmed:affiliation | Department of Microbiology, State University of New York, Stony Brook 11794-8621. | lld:pubmed |
| pubmed-article:2838466 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2838466 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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