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Avoiding the oligomeric state: αB-crystallin inhibits fragmentation and induces dissociation of apolipoprotein C-II amyloid fibrils

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Date

2013

Authors

Binger, Katrina J.
Ecroyd, Heath
Yang, Shuo
Carver, John
Howlett, Geoffrey
Griffin, Michael D.W.

Journal Title

Journal ISSN

Volume Title

Publisher

Federation of American Societies for Experimental Biology

Abstract

The in vivo aggregation of proteins into amyloid fibrils suggests that cellular mechanisms that normally prevent or reverse this aggregation have failed. The small heat-shock molecular chaperone protein αB-crystallin (αB-c) inhibits amyloid formation an

Description

Keywords

Keywords: alpha crystallin; amyloid; apolipoprotein C2; small heat shock protein; thioflavine; article; controlled study; dilution; dissociation; dissociation constant; fragmentation reaction; molecular weight; oligomerization; priority journal; protein binding; pr Aggregation; Heat-shock protein; Molecular chaperone; Protein misfolding

Citation

URI

http://hdl.handle.net/1885/62170

Collections

ANU Research Publications

Source

FASEB Journal

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1096/fj.12-220657

Restricted until

2037-12-31

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