BiochemistrybioRxivPreprint
Accumulative deamidation of human lens protein γS-crystallin leads to partially unfolded intermediates with enhanced aggregation propensity
C. J. Vetter, D. Thorn, S. G. Wheeler…·K. J. Lampi
This study shows that deamidation of γS-crystallin at specific sites leads to protein destabilization, increased unfolding, and enhanced aggregation in cataractous lenses.
DOI 10.1101/2020.02.21.960237