| pubmed-article:18247479 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18247479 | lifeskim:mentions | umls-concept:C0544157 | lld:lifeskim |
| pubmed-article:18247479 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:18247479 | lifeskim:mentions | umls-concept:C0221102 | lld:lifeskim |
| pubmed-article:18247479 | lifeskim:mentions | umls-concept:C0086045 | lld:lifeskim |
| pubmed-article:18247479 | lifeskim:mentions | umls-concept:C0038836 | lld:lifeskim |
| pubmed-article:18247479 | lifeskim:mentions | umls-concept:C0038838 | lld:lifeskim |
| pubmed-article:18247479 | lifeskim:mentions | umls-concept:C1704211 | lld:lifeskim |
| pubmed-article:18247479 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:18247479 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:18247479 | pubmed:dateCreated | 2008-2-19 | lld:pubmed |
| pubmed-article:18247479 | pubmed:abstractText | Deinococcus radiodurans (Drad), a bacterium with an extraordinary capacity to tolerate high levels of ionizing radiation, produces only a manganese-containing superoxide dismutase (MnSOD). As MnSOD has been shown to remove superoxide radical with varying efficiency depending upon its cellular origin, a comparison of the Drad MnSOD efficiency with that of both human and Escherichia coli MnSODs was undertaken. Pulse radiolysis studies demonstrate that, under identical ratios of enzyme to superoxide radical, the dismutation efficiencies scaled as Drad MnSOD > E. coli MnSOD > human MnSOD. Further, Drad MnSOD is most effective at high superoxide fluxes found under conditions of high radioactivity. A mechanism is postulated to account for the differences in the activities of the MnSODs that considers the release of peroxide as not always an optimal process. | lld:pubmed |
| pubmed-article:18247479 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18247479 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18247479 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18247479 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18247479 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18247479 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18247479 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18247479 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:18247479 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:18247479 | pubmed:author | pubmed-author:SilvermanDavi... | lld:pubmed |
| pubmed-article:18247479 | pubmed:author | pubmed-author:CabelliDiane... | lld:pubmed |
| pubmed-article:18247479 | pubmed:author | pubmed-author:NickHarry SHS | lld:pubmed |
| pubmed-article:18247479 | pubmed:author | pubmed-author:AbreuIsabel... | lld:pubmed |
| pubmed-article:18247479 | pubmed:author | pubmed-author:AnHaiqainH | lld:pubmed |
| pubmed-article:18247479 | pubmed:author | pubmed-author:HearnAmyA | lld:pubmed |
| pubmed-article:18247479 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18247479 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:18247479 | pubmed:volume | 47 | lld:pubmed |
| pubmed-article:18247479 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18247479 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18247479 | pubmed:pagination | 2350-6 | lld:pubmed |
| pubmed-article:18247479 | pubmed:meshHeading | pubmed-meshheading:18247479... | lld:pubmed |
| pubmed-article:18247479 | pubmed:meshHeading | pubmed-meshheading:18247479... | lld:pubmed |
| pubmed-article:18247479 | pubmed:meshHeading | pubmed-meshheading:18247479... | lld:pubmed |
| pubmed-article:18247479 | pubmed:meshHeading | pubmed-meshheading:18247479... | lld:pubmed |
| pubmed-article:18247479 | pubmed:meshHeading | pubmed-meshheading:18247479... | lld:pubmed |
| pubmed-article:18247479 | pubmed:meshHeading | pubmed-meshheading:18247479... | lld:pubmed |
| pubmed-article:18247479 | pubmed:meshHeading | pubmed-meshheading:18247479... | lld:pubmed |
| pubmed-article:18247479 | pubmed:meshHeading | pubmed-meshheading:18247479... | lld:pubmed |
| pubmed-article:18247479 | pubmed:meshHeading | pubmed-meshheading:18247479... | lld:pubmed |
| pubmed-article:18247479 | pubmed:meshHeading | pubmed-meshheading:18247479... | lld:pubmed |
| pubmed-article:18247479 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18247479 | pubmed:articleTitle | The kinetic mechanism of manganese-containing superoxide dismutase from Deinococcus radiodurans: a specialized enzyme for the elimination of high superoxide concentrations. | lld:pubmed |
| pubmed-article:18247479 | pubmed:affiliation | Chemistry Department, Brookhaven National Laboratory, Building 555, Upton, New York 11973-5000, USA. | lld:pubmed |
| pubmed-article:18247479 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18247479 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:18247479 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:18247479 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18247479 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:6648 | entrezgene:pubmed | pubmed-article:18247479 | lld:entrezgene |
| entrez-gene:1797407 | entrezgene:pubmed | pubmed-article:18247479 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18247479 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18247479 | lld:entrezgene |
