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- W2900492213 abstract "In the vertebrate eye, limiting oxidation of proteins and lipids is key to maintaining lens function and avoiding cataract formation. A study by Serebryany et al. identifies a surprising contributor to the eye's oxidative defense in their demonstration that γD-crystallin (HγD) functions as an oxidoreductase and uses disulfide exchange to initiate aggregation of mutant crystallins that mimic oxidative damage. These insights suggest a mechanism by which a dynamic pool of closely packed proteins might avoid oxidation-driven protein-folding traps, providing new avenues to understand the basis of a human disease with global impact." @default.
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- W2900492213 date "2018-11-01" @default.
- W2900492213 modified "2023-10-13" @default.
- W2900492213 title "γ-Crystallin redox–detox in the lens" @default.
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- W2900492213 doi "https://doi.org/10.1074/jbc.h118.006240" @default.
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