| pubmed-article:7768839 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7768839 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:7768839 | lifeskim:mentions | umls-concept:C0038838 | lld:lifeskim |
| pubmed-article:7768839 | lifeskim:mentions | umls-concept:C0282498 | lld:lifeskim |
| pubmed-article:7768839 | lifeskim:mentions | umls-concept:C1510824 | lld:lifeskim |
| pubmed-article:7768839 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:7768839 | pubmed:dateCreated | 1995-7-6 | lld:pubmed |
| pubmed-article:7768839 | pubmed:abstractText | Exposure of a superoxide dismutase-null (sodA sodB) strain of Escherichia coli to aerobic heat stress (45 to 48 degrees C) caused a profound loss of viability, whereas the same heat stress applied anaerobically had a negligible effect. A superoxide dismutase-competent parental strain was resistant to the lethal effect of the aerobic heating. It follows that aerobic heating imposes an oxidative burden of which O2- must be a major component. This effect is not seen at 53 degrees C, presumably because, at this higher temperature, direct thermolability of vital cell components overrides the effect of superoxide radicals. | lld:pubmed |
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| pubmed-article:7768839 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7768839 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7768839 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7768839 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7768839 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7768839 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7768839 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:7768839 | pubmed:author | pubmed-author:FridovichII | lld:pubmed |
| pubmed-article:7768839 | pubmed:author | pubmed-author:BenovLL | lld:pubmed |
| pubmed-article:7768839 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7768839 | pubmed:volume | 177 | lld:pubmed |
| pubmed-article:7768839 | pubmed:geneSymbol | sodB | lld:pubmed |
| pubmed-article:7768839 | pubmed:geneSymbol | sodA | lld:pubmed |
| pubmed-article:7768839 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7768839 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7768839 | pubmed:pagination | 3344-6 | lld:pubmed |
| pubmed-article:7768839 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:7768839 | pubmed:meshHeading | pubmed-meshheading:7768839-... | lld:pubmed |
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| pubmed-article:7768839 | pubmed:meshHeading | pubmed-meshheading:7768839-... | lld:pubmed |
| pubmed-article:7768839 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7768839 | pubmed:articleTitle | Superoxide dismutase protects against aerobic heat shock in Escherichia coli. | lld:pubmed |
| pubmed-article:7768839 | pubmed:affiliation | Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA. | lld:pubmed |
| pubmed-article:7768839 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7768839 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7768839 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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