Binding of γ-Crystallin Substrate Prevents the Binding of Copper and Zinc Ions to the Molecular Chaperone α-Crystallin-Reference-Cited by-同舟云学术

Binding of γ-Crystallin Substrate Prevents the Binding of Copper and Zinc Ions to the Molecular Chaperone α-Crystallin

Published:2011-03-30 Issue:16 Volume:50 Page:3279-3281
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ghosh Kalyan S.¹,Pande Ajay¹,Pande Jayanti¹

Affiliation:

1. Department of Chemistry, Life Sciences Research Building, University at Albany, State University of New York, Albany, New York 12222, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi200091q

Reference25 articles.

1. Alpha-crystallin can function as a molecular chaperone.

2. Î±-Crystallin as a molecular chaperone

3. Structure and Mechanism of Protein Stability Sensors: Chaperone Activity of Small Heat Shock Proteins

4. Lens aging: Effects of crystallins

5. Partially Folded Aggregation Intermediates of Human γD-, γC-, and γS-Crystallin Are Recognized and Bound by Human αB-Crystallin Chaperone

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