Article

An internal disulfide locks a misfolded aggregation-prone intermediate in cataract-linked mutants of human γD-crystallin

2016-07-06

Abstract excerpt

Considerable mechanistic insight has been gained into amyloid aggregation; however, a large class of non-amyloid protein aggregates are considered “amorphous,” and in most cases little is known about their mechanisms. Amorphous aggregation of γ-crystallins in the eye lens causes a widespread disease of aging, cataract. We combined simulations and experiments to study the mechanism of aggregation of two γD-crystall...

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Identifiers and source

Literature Corpus work: 935fef3a-21cb-5aac-8666-136d955b57d6
DOI: 10.1101/062430

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