| pubmed-article:10802185 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10802185 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:10802185 | lifeskim:mentions | umls-concept:C0043408 | lld:lifeskim |
| pubmed-article:10802185 | lifeskim:mentions | umls-concept:C2717971 | lld:lifeskim |
| pubmed-article:10802185 | lifeskim:mentions | umls-concept:C0699748 | lld:lifeskim |
| pubmed-article:10802185 | lifeskim:mentions | umls-concept:C1261322 | lld:lifeskim |
| pubmed-article:10802185 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10802185 | pubmed:dateCreated | 2000-7-11 | lld:pubmed |
| pubmed-article:10802185 | pubmed:abstractText | The HtrA stress response protein has been shown to play a role in the virulence of a number of pathogens. For some organisms, htrA mutants are attenuated in the animal model and can be used as live vaccines. A Yersinia pestis htrA orthologue was identified, cloned and sequenced, showing 86% and 87% similarity to Escherichia coli and Salmonella typhimurium HtrAs. An isogenic Y. pestis htrA mutant was constructed using a reverse genetics approach. In contrast to the wild-type strain, the mutant failed to grow at an elevated temperature of 39 degrees C, but showed only a small increase in sensitivity to oxidative stress and was only partially attenuated in the animal model. However, the mutant exhibited a different protein expression profile to that of the wild-type strain when grown at 28 degrees C to simulate growth in the flea. | lld:pubmed |
| pubmed-article:10802185 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10802185 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10802185 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10802185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10802185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10802185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10802185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10802185 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10802185 | pubmed:month | May | lld:pubmed |
| pubmed-article:10802185 | pubmed:issn | 0378-1097 | lld:pubmed |
| pubmed-article:10802185 | pubmed:author | pubmed-author:LUGG | lld:pubmed |
| pubmed-article:10802185 | pubmed:author | pubmed-author:WilliamsKK | lld:pubmed |
| pubmed-article:10802185 | pubmed:author | pubmed-author:OystonP CPC | lld:pubmed |
| pubmed-article:10802185 | pubmed:author | pubmed-author:WrenB WBW | lld:pubmed |
| pubmed-article:10802185 | pubmed:author | pubmed-author:TitballR WRW | lld:pubmed |
| pubmed-article:10802185 | pubmed:author | pubmed-author:DorrellNN | lld:pubmed |
| pubmed-article:10802185 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10802185 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10802185 | pubmed:volume | 186 | lld:pubmed |
| pubmed-article:10802185 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10802185 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10802185 | pubmed:pagination | 281-6 | lld:pubmed |
| pubmed-article:10802185 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10802185 | pubmed:meshHeading | pubmed-meshheading:10802185... | lld:pubmed |
| pubmed-article:10802185 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10802185 | pubmed:articleTitle | Investigation into the role of the serine protease HtrA in Yersinia pestis pathogenesis. | lld:pubmed |
| pubmed-article:10802185 | pubmed:affiliation | Pathogen Molecular Biology and Biochemistry Unit, Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, Keppel Street, London, UK. | lld:pubmed |
| pubmed-article:10802185 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10802185 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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