Human γS-Crystallin–Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage-Reference-Cited by-同舟云学术

Human γS-Crystallin–Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage

Published:2020-06-08 Issue:25 Volume:59 Page:2371-2385
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Roskamp Kyle W.¹,Azim Sana²,Kassier Günther²,Norton-Baker Brenna¹²,Sprague-Piercy Marc A.³,Miller R. J. Dwyane²⁴^ORCID,Martin Rachel W.¹³^ORCID

Affiliation:

1. Department of Chemistry, University of California, Irvine, California 92697-2025, United States

2. Max Planck Institute for the Structure and Dynamics of Matter, Center for Free Electron Laser Science, Luruper Chaussee 149, Hamburg 22761, Germany

3. Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900, United States

4. Departments of Chemistry and Physics, University of Toronto, 80 St. George Street, Toronto, ON M5S 3H6, Canada

Funder

Howard Hughes Medical Institute

Division of Mathematical Sciences

National Eye Institute

Division of Graduate Education

Deutsche Forschungsgemeinschaft

Max-Planck-Gesellschaft

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00293

Reference106 articles.

1. Normal human lens—the distribution of protein

2. The βγ-crystallins: Native state stability and pathways to aggregation

3. Gamma crystallins of the human eye lens

4. Conformational catalysis of cataract-associated aggregation in a human eye lens crystallin occurs via interface stealing

5. Lens α-crystallin: Function and structure

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