• Oxidation of active cysteines mediates protein aggregation of S10R, the cataract‐associated mutant of mouse GammaB‐crystallin

    12 days ago - By Wiley

    Abstract
    The Ser10 to Arg mutation in mouse γB-crystallin has been associated with protein aggregation, dense nuclear opacity and the degeneration of fiber cells in the lens core. Overexpression of the gap junction protein, connexin 46, was found to suppress the nuclear opacity and restore normal cell-cell contact 1,2. However, the molecular basis for the protein aggregation and related downstream effects, were not evident from these studies. Here we provide a comparison of the structures and solution properties of wild-type mouse γB-crystallin and the S10R mutant in vitro, and show that...
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