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Title: Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications. Author: Cherian M, Abraham EC. Journal: Biochem Biophys Res Commun; 1995 Mar 17; 208(2):675-9. PubMed ID: 7695622. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]