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Catalysis of cataract-associated human γD crystallin aggregation via dynamic disulfide exchange
[article]
2018
bioRxiv
pre-print
Several mutations in human γD-crystallin (HγD), a long-lived eye lens protein, cause misfolding and aggregation, leading to cataract. Surprisingly, wild-type HγD catalyzes aggregation of its cataract related W42Q variant while itself remaining soluble -- the inverse of the classical prion-like scenario whereby misfolded polypeptides catalyze aggregation of natively folded ones. The search for a biochemical mechanism of catalysis of W42Q aggregation by WT has revealed that WT HγD can transfer a
doi:10.1101/300608
fatcat:s26yjsh6dfhmtfzme3bpxmkz6y