| pubmed-article:2500362 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2500362 | lifeskim:mentions | umls-concept:C0021585 | lld:lifeskim |
| pubmed-article:2500362 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:2500362 | lifeskim:mentions | umls-concept:C0034435 | lld:lifeskim |
| pubmed-article:2500362 | lifeskim:mentions | umls-concept:C1261381 | lld:lifeskim |
| pubmed-article:2500362 | lifeskim:mentions | umls-concept:C0301872 | lld:lifeskim |
| pubmed-article:2500362 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:2500362 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:2500362 | lifeskim:mentions | umls-concept:C0072883 | lld:lifeskim |
| pubmed-article:2500362 | lifeskim:mentions | umls-concept:C1292733 | lld:lifeskim |
| pubmed-article:2500362 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2500362 | pubmed:dateCreated | 1989-7-28 | lld:pubmed |
| pubmed-article:2500362 | pubmed:abstractText | Melanization and encapsulation of invading foreign organisms observed during the immune response in insects is known to be due to the action of activated phenoloxidase. Phenoloxidase-generated quinones are deposited either directly or after self-polymerization on foreign objects accounting for the observed reactions. Since the reactions of quinones are nonenzymatic, they do not discriminate self from nonself and hence will also destroy self-matter. In this report we present evidence for the presence of a novel quinone/quinone methide isomerase in the hemolymph of Sarcophaga bullata which destroys long-lived quinones and hence acts to protect the self-matter. Quinone methides, formed by the action of this enzyme on physiologically important quinones, being unstable undergo rapid hydration to form nontoxic metabolites. | lld:pubmed |
| pubmed-article:2500362 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2500362 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2500362 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2500362 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2500362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2500362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2500362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2500362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2500362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2500362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2500362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2500362 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2500362 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2500362 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:2500362 | pubmed:author | pubmed-author:SugumaranMM | lld:pubmed |
| pubmed-article:2500362 | pubmed:author | pubmed-author:SaulS JSJ | lld:pubmed |
| pubmed-article:2500362 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2500362 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:2500362 | pubmed:volume | 249 | lld:pubmed |
| pubmed-article:2500362 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2500362 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2500362 | pubmed:pagination | 155-8 | lld:pubmed |
| pubmed-article:2500362 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:meshHeading | pubmed-meshheading:2500362-... | lld:pubmed |
| pubmed-article:2500362 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2500362 | pubmed:articleTitle | o-quinone/quinone methide isomerase: a novel enzyme preventing the destruction of self-matter by phenoloxidase-generated quinones during immune response in insects. | lld:pubmed |
| pubmed-article:2500362 | pubmed:affiliation | Department of Biology, University of Massachusetts, Boston 02125. | lld:pubmed |
| pubmed-article:2500362 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2500362 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2500362 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2500362 | lld:pubmed |
