Selenocysteine Positional Variants Reveal Contributions to Copper Binding from Cysteine Residues in Domains 2 and 3 of Human Copper Chaperone for Superoxide Dismutase
Author:
Affiliation:
1. Department of Science and Engineering, School of Medicine, Oregon Health and Sciences University, Beaverton, Oregon 97006, and Departments of Biochemistry and Chemistry, University of Illinois at Urbana−Champaign, Urbana, Illinois 61801
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi801438g
Reference45 articles.
1. The Copper Chaperone for Superoxide Dismutase
2. Activation of superoxide dismutases: Putting the metal to the pedal
3. Function, Structure, and Mechanism of Intracellular Copper Trafficking Proteins
4. Copper Delivery by Metallochaperone Proteins
5. Posttranslational Modifications in Cu,Zn-Superoxide Dismutase and Mutations Associated with Amyotrophic Lateral Sclerosis
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