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The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity

Hochberg, Georg K. A.; Ecroyd, Heath; Liu, Cong; Cox, Dezerae; Cascio, Duilio; Sawaya, Michael R.; Collier, Miranda P.; Stroud, James; Carver, John; Baldwin, Andrew J.; Robinson, Carol V.; Eisenberg, David S.; Benesch, Justin L. P.; Laganowsky, Arthur


Mammalian small heat-shock proteins (sHSPs) are molecular chaperones that form polydisperse and dynamic complexes with target proteins, serving as a first line of defense in preventing their aggregation into either amorphous deposits or amyloid fibrils. Their apparently broad target specificity makes sHSPs attractive for investigating ways to tackle disorders of protein aggregation. The two most abundant sHSPs in human tissue are αB-crystallin (ABC) and HSP27; here we present high-resolution...[Show more]

CollectionsANU Research Publications
Date published: 2014
Type: Journal article
Source: PNAS - Proceedings of the National Academy of Sciences of the United States of America
DOI: 10.1073/pnas.1322673111
Access Rights: Open Access


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