Insights into Function, Catalytic Mechanism, and Fold Evolution of Selenoprotein Methionine Sulfoxide Reductase B1 through Structural Analysis*
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
1. Peptide Methionine Sulfoxide Reductase: Structure, Mechanism of Action, and Biological Function
2. Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals
3. Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function
4. Mammals Reduce Methionine-S-sulfoxide with MsrA and Are Unable to Reduce Methionine-R-sulfoxide, and This Function Can Be Restored with a Yeast Reductase
5. Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity
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1. Biological and Catalytic Properties of Selenoproteins;International Journal of Molecular Sciences;2023-06-14
2. Novel Lennard-Jones Parameters for Cysteine and Selenocysteine in the AMBER Force Field;Journal of Chemical Information and Modeling;2023-01-11
3. The selenoprotein methionine sulfoxide reductase B1 (MSRB1);Free Radical Biology and Medicine;2022-10
4. Biosynthesis of selenium-containing small molecules in diverse microorganisms;Nature;2022-09-07
5. A Novel and Prevalent Pathway in Microbial Selenium Metabolism;2022-04-14
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