Article
Human γS-Crystallin-Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage.
Biochemistry - 30 Jun 2020
Roskamp Kyle W, Azim Sana, Kassier Günther, Norton-Baker Brenna, Sprague-Piercy Marc A, Miller R J Dwyane, Martin Rachel W
Abstract excerpt
Divalent metal cations can play a role in protein aggregation diseases, including cataract. Here we compare the aggregation of human γS-crystallin, a key structural protein of the eye lens, via mutagenesis, ultraviolet light damage, and the addition of metal ions. All three aggregation pathways result in globular, amorphous-looking structures that do not elongate into fibers. We also investigate the molecular...
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