pubmed-article:8889493 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8889493 | lifeskim:mentions | umls-concept:C0003402 | lld:lifeskim |
pubmed-article:8889493 | lifeskim:mentions | umls-concept:C0002191 | lld:lifeskim |
pubmed-article:8889493 | lifeskim:mentions | umls-concept:C0003968 | lld:lifeskim |
pubmed-article:8889493 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
pubmed-article:8889493 | lifeskim:mentions | umls-concept:C1545588 | lld:lifeskim |
pubmed-article:8889493 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
pubmed-article:8889493 | lifeskim:mentions | umls-concept:C1328815 | lld:lifeskim |
pubmed-article:8889493 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
pubmed-article:8889493 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:8889493 | pubmed:dateCreated | 1997-2-5 | lld:pubmed |
pubmed-article:8889493 | pubmed:abstractText | Peroxynitrite, formed by reaction of superoxide and nitric oxide, appears to be an important tissue-damaging species generated at sites of inflammation. In this paper, we compare the abilities of several biological antioxidants to protect against peroxynitrite-dependent inactivation of alpha 1-antiproteinase, and to inhibit tyrosine nitration upon addition of peroxynitrite. GSH and ascorbate protected efficiently in both systems. Uric acid inhibited tyrosine nitration but not alpha 1-antiproteinase inactivation. The possibility that ascorbic acid is an important scavenger of reactive nitrogen species in vivo is discussed. | lld:pubmed |
pubmed-article:8889493 | pubmed:language | eng | lld:pubmed |
pubmed-article:8889493 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8889493 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8889493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8889493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8889493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8889493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8889493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8889493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8889493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8889493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8889493 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8889493 | pubmed:month | Sep | lld:pubmed |
pubmed-article:8889493 | pubmed:issn | 1071-5762 | lld:pubmed |
pubmed-article:8889493 | pubmed:author | pubmed-author:HalliwellBB | lld:pubmed |
pubmed-article:8889493 | pubmed:author | pubmed-author:WhitemanMM | lld:pubmed |
pubmed-article:8889493 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8889493 | pubmed:volume | 25 | lld:pubmed |
pubmed-article:8889493 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8889493 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8889493 | pubmed:pagination | 275-83 | lld:pubmed |
pubmed-article:8889493 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:8889493 | pubmed:meshHeading | pubmed-meshheading:8889493-... | lld:pubmed |
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pubmed-article:8889493 | pubmed:meshHeading | pubmed-meshheading:8889493-... | lld:pubmed |
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pubmed-article:8889493 | pubmed:meshHeading | pubmed-meshheading:8889493-... | lld:pubmed |
pubmed-article:8889493 | pubmed:meshHeading | pubmed-meshheading:8889493-... | lld:pubmed |
pubmed-article:8889493 | pubmed:meshHeading | pubmed-meshheading:8889493-... | lld:pubmed |
pubmed-article:8889493 | pubmed:meshHeading | pubmed-meshheading:8889493-... | lld:pubmed |
pubmed-article:8889493 | pubmed:meshHeading | pubmed-meshheading:8889493-... | lld:pubmed |
pubmed-article:8889493 | pubmed:meshHeading | pubmed-meshheading:8889493-... | lld:pubmed |
pubmed-article:8889493 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8889493 | pubmed:articleTitle | Protection against peroxynitrite-dependent tyrosine nitration and alpha 1-antiproteinase inactivation by ascorbic acid. A comparison with other biological antioxidants. | lld:pubmed |
pubmed-article:8889493 | pubmed:affiliation | Neurodegenerative Disease Research Centre, King's College, London, UK. | lld:pubmed |
pubmed-article:8889493 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8889493 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:8889493 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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