The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures
Author:
Affiliation:
1. School of Biological SciencesUniversity of WollongongWollongongAustralia
2. Department of ChemistryUniversity of CambridgeCambridgeUK
3. School of Chemistry and PhysicsUniversity of AdelaideAdelaideAustralia
Funder
Australian Research Council
Publisher
Wiley
Subject
Genetics,Molecular Biology,Biochemistry,Biotechnology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.06-7986com
Reference36 articles.
1. Protein Misfolding, Functional Amyloid, and Human Disease
2. Quality control of protein folding in extracellular space
3. Cellular Defenses against Unfolded Proteins
4. Clusterin Has Chaperone-like Activity Similar to That of Small Heat Shock Proteins
5. Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterin
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