| pubmed-article:8969219 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8969219 | lifeskim:mentions | umls-concept:C0079870 | lld:lifeskim |
| pubmed-article:8969219 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8969219 | lifeskim:mentions | umls-concept:C0002003 | lld:lifeskim |
| pubmed-article:8969219 | lifeskim:mentions | umls-concept:C0012771 | lld:lifeskim |
| pubmed-article:8969219 | lifeskim:mentions | umls-concept:C0205463 | lld:lifeskim |
| pubmed-article:8969219 | pubmed:issue | 52 | lld:pubmed |
| pubmed-article:8969219 | pubmed:dateCreated | 1997-1-28 | lld:pubmed |
| pubmed-article:8969219 | pubmed:abstractText | Aldose reductase is inactivated by physiological disulfides such as GSSG and cystine. To study the mechanism of disulfide-induced enzyme inactivation, we examined the rate and extent of enzyme inactivation using wild-type human aldose reductase and mutants containing cysteine-to-serine substitutions at positions 80 (C80S), 298 (C298S), and 303 (C303S). The wild-type, C80S, and C303S enzymes lost >80% activity following incubation with GSSG, whereas the C298S mutant was not affected. Loss of activity correlated with enzyme thiolation. The binary enzyme-NADP+ complex was less susceptible to enzyme thiolation than the apoenzyme. These results suggest that thiolation of human aldose reductase occurs predominantly at Cys-298. Energy minimization of a hypothetical enzyme complex modified by glutathione at Cys-298 revealed that the glycyl carboxylate of glutathione may participate in a charged interaction with His-110 in a manner strikingly similar to that involving the carboxylate group of the potent aldose reductase inhibitor Zopolrestat. In contrast to what was observed with GSSG and cystine, cystamine inactivated the wild-type enzyme as well as all three cysteine mutants. This suggests that cystamine-induced inactivation of aldose reductase does not involve modification of cysteines exclusively at position 80, 298, or 303. | lld:pubmed |
| pubmed-article:8969219 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8969219 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8969219 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8969219 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8969219 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8969219 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8969219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8969219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8969219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8969219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8969219 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8969219 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8969219 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8969219 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8969219 | pubmed:author | pubmed-author:QuiochoF AFA | lld:pubmed |
| pubmed-article:8969219 | pubmed:author | pubmed-author:MuraUU | lld:pubmed |
| pubmed-article:8969219 | pubmed:author | pubmed-author:MarinoCC | lld:pubmed |
| pubmed-article:8969219 | pubmed:author | pubmed-author:Dal MonteMM | lld:pubmed |
| pubmed-article:8969219 | pubmed:author | pubmed-author:WilsonD KDK | lld:pubmed |
| pubmed-article:8969219 | pubmed:author | pubmed-author:PetrashJ MJM | lld:pubmed |
| pubmed-article:8969219 | pubmed:author | pubmed-author:Del CorsoAA | lld:pubmed |
| pubmed-article:8969219 | pubmed:author | pubmed-author:CappielloMM | lld:pubmed |
| pubmed-article:8969219 | pubmed:author | pubmed-author:VoltarelliMM | lld:pubmed |
| pubmed-article:8969219 | pubmed:author | pubmed-author:CecconiII | lld:pubmed |
| pubmed-article:8969219 | pubmed:author | pubmed-author:VilardoP GPG | lld:pubmed |
| pubmed-article:8969219 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8969219 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:8969219 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8969219 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8969219 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8969219 | pubmed:pagination | 33539-44 | lld:pubmed |
| pubmed-article:8969219 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8969219 | pubmed:meshHeading | pubmed-meshheading:8969219-... | lld:pubmed |
| pubmed-article:8969219 | pubmed:meshHeading | pubmed-meshheading:8969219-... | lld:pubmed |
| pubmed-article:8969219 | pubmed:meshHeading | pubmed-meshheading:8969219-... | lld:pubmed |
| pubmed-article:8969219 | pubmed:meshHeading | pubmed-meshheading:8969219-... | lld:pubmed |
| pubmed-article:8969219 | pubmed:meshHeading | pubmed-meshheading:8969219-... | lld:pubmed |
| pubmed-article:8969219 | pubmed:meshHeading | pubmed-meshheading:8969219-... | lld:pubmed |
| pubmed-article:8969219 | pubmed:meshHeading | pubmed-meshheading:8969219-... | lld:pubmed |
| pubmed-article:8969219 | pubmed:meshHeading | pubmed-meshheading:8969219-... | lld:pubmed |
| pubmed-article:8969219 | pubmed:meshHeading | pubmed-meshheading:8969219-... | lld:pubmed |
| pubmed-article:8969219 | pubmed:meshHeading | pubmed-meshheading:8969219-... | lld:pubmed |
| pubmed-article:8969219 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8969219 | pubmed:articleTitle | Specifically targeted modification of human aldose reductase by physiological disulfides. | lld:pubmed |
| pubmed-article:8969219 | pubmed:affiliation | Dipartimento di Fisiologia e Biochimica, Università di Pisa, via S. Maria 55, 56100 Pisa, Italy. cmario@dfb.unipi.it | lld:pubmed |
| pubmed-article:8969219 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8969219 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8969219 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8969219 | lld:pubmed |
