Clusterin Is an ATP−Independent Chaperone with Very Broad Substrate Specificity that Stabilizes Stressed Proteins in a Folding-Competent State-Reference-Cited by-同舟云学术

Clusterin Is an ATP−Independent Chaperone with Very Broad Substrate Specificity that Stabilizes Stressed Proteins in a Folding-Competent State

Published:2000-12-01 Issue:51 Volume:39 Page:15953-15960
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Poon Stephen¹,Easterbrook-Smith Simon B.¹,Rybchyn Mark S¹,Carver John A.¹,Wilson Mark R.¹

Affiliation:

1. Department of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, NSW. 2522, Australia, and Department of Biochemistry, University of Sydney, Sydney, NSW. 2006, Australia, and Department of Chemistry, University of Wollongong, Northfields Avenue, Wollongong, NSW. 2522, Australia

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi002189x

Reference31 articles.

1. Multiple Involvement of Clusterin in Chicken Ovarian Follicle Development

2. Stress-induced transcription of the clusterin/apoJ gene

3. Clusterin Has Chaperone-like Activity Similar to That of Small Heat Shock Proteins

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