Journal article icon

Journal article

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

Abstract:

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 ...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1073/pnas.1322673111

Authors


Journal:
Proceedings of the National Academy of Sciences of the United States of America More from this journal
Volume:
111
Issue:
16
Pages:
E1562-E1570
Publication date:
2014-04-07
DOI:
EISSN:
1091-6490
ISSN:
0027-8424

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP