| pubmed-article:7695622 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7695622 | lifeskim:mentions | umls-concept:C0002257 | lld:lifeskim |
| pubmed-article:7695622 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
| pubmed-article:7695622 | lifeskim:mentions | umls-concept:C0678226 | lld:lifeskim |
| pubmed-article:7695622 | lifeskim:mentions | umls-concept:C0205216 | lld:lifeskim |
| pubmed-article:7695622 | lifeskim:mentions | umls-concept:C0033666 | lld:lifeskim |
| pubmed-article:7695622 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:7695622 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7695622 | pubmed:dateCreated | 1995-4-24 | lld:pubmed |
| pubmed-article:7695622 | pubmed:abstractText | We studied the effect of oxidation, mixed disulfide formation and glycation of alpha-crystallins on their molecular chaperone property. The ability of alpha-crystallins to protect heat-induced denaturation and aggregation of beta L-crystallin was significantly diminished by these modifications. alpha-Crystallin from senile human lenses also showed significant loss of chaperone-like property. Age-dependent increase in posttranslationally modified alpha-crystallins is the likely cause for this change. | lld:pubmed |
| pubmed-article:7695622 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7695622 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7695622 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7695622 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7695622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7695622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7695622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7695622 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7695622 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7695622 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:7695622 | pubmed:author | pubmed-author:AbrahamE CEC | lld:pubmed |
| pubmed-article:7695622 | pubmed:author | pubmed-author:CherianMM | lld:pubmed |
| pubmed-article:7695622 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7695622 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:7695622 | pubmed:volume | 208 | lld:pubmed |
| pubmed-article:7695622 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7695622 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7695622 | pubmed:pagination | 675-9 | lld:pubmed |
| pubmed-article:7695622 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7695622 | pubmed:meshHeading | pubmed-meshheading:7695622-... | lld:pubmed |
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| pubmed-article:7695622 | pubmed:meshHeading | pubmed-meshheading:7695622-... | lld:pubmed |
| pubmed-article:7695622 | pubmed:meshHeading | pubmed-meshheading:7695622-... | lld:pubmed |
| pubmed-article:7695622 | pubmed:meshHeading | pubmed-meshheading:7695622-... | lld:pubmed |
| pubmed-article:7695622 | pubmed:meshHeading | pubmed-meshheading:7695622-... | lld:pubmed |
| pubmed-article:7695622 | pubmed:meshHeading | pubmed-meshheading:7695622-... | lld:pubmed |
| pubmed-article:7695622 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7695622 | pubmed:articleTitle | Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications. | lld:pubmed |
| pubmed-article:7695622 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta 30912-2100. | lld:pubmed |
| pubmed-article:7695622 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7695622 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7695622 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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