ReviewAntioxidants & redox signaling2015
Regulation of protein function by reversible methionine oxidation and the role of selenoprotein MsrB1.
Review in Antioxidants & redox signaling, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 94 citations in OpenAlex.
- Sulfur valence normalization to expand quantitative peptide selection in protein metrology.Analytical and bioanalytical chemistry · 2026Article
- Selenoproteins: Minute yet vital players governing cellular fate.Genes & diseases · 2026Review
- Modulating Protein Function through Genetically Encoded Oxidative Chemistry.Journal of the American Chemical Society · 2026Article
- Chiral methionine oxidation reagents reveal stereospecific proteome modifications.bioRxiv : the preprint server for biology · 2026Article
- Selenium-Biofortified Probiotics: A Synergistic Microbial-Nutritional Strategy Against Exercise-Induced Stress.Nutrients · 2026Review
- Role of Redox-Induced Protein Modifications in Spermatozoa in Health and Disease.Antioxidants (Basel, Switzerland) · 2025Review
- Selenium and Skeletal Muscle Health in Sports Nutrition.Nutrients · 2025Review
- Facts, Dogmas, and Unknowns About Mitochondrial Reactive Oxygen Species in Cancer.Antioxidants (Basel, Switzerland) · 2024Review
- Cellular and molecular roles of reactive oxygen species in wound healing.Communications biology · 2024Review
- Fundamentals of redox regulation in biology.Nature reviews. Molecular cell biology · 2024Review
- Unresolved questions regarding cellular cysteine sources and their possible relationships to ferroptosis.Advances in cancer research · 2024Review
- Response to oxidative stress of AML12 hepatocyte cells with knockout of methionine sulfoxide reductases.Free radical biology & medicine · 2023Article
- Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023Review
- Selenoproteins synergistically protect porcine skeletal muscle from oxidative damage via relieving mitochondrial dysfunction and endoplasmic reticulum stress.Journal of animal science and biotechnology · 2023Article
- How the Disruption of Mitochondrial Redox Signalling Contributes to Ageing.Antioxidants (Basel, Switzerland) · 2023Review
- Methionine Sulfoxide Reductases Suppress the Formation of the [Antioxidants (Basel, Switzerland) · 2023Article
- The integrated stress response protects against ER stress but is not required for altered translation and lifespan from dietary restriction inFrontiers in cell and developmental biology · 2023Article
- A Vitamin BAngewandte Chemie (International ed. in English) · 2022Article
- A Vitamin BAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Regulation of Retroviral and SARS-CoV-2 Protease Dimerization and Activity through Reversible Oxidation.Antioxidants (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
significanceProtein structure and function can be regulated via post-translational modifications by numerous enzymatic and nonenzymatic mechanisms. Regulation involving oxidation of sulfur-containing residues emerged as a key mechanism of redox control. Unraveling the participants and principles of such regulation is necessary for understanding the biological significance of redox control of cellular processes. RECENT ADVANCES: Reversible oxidation of methionine residues by monooxygenases of the Mical family and subsequent reduction of methionine sulfoxides by a selenocysteine-containing methionine sulfoxide reductase B1 (MsrB1) was found to control the assembly and disassembly of actin in mammals, and the Mical/MsrB pair similarly regulates actin in fruit flies. This finding has opened up new avenues for understanding the use of stereospecific methionine oxidation in regulating cellular processes and the roles of MsrB1 and Micals in regulation of actin dynamics. CRITICAL ISSUES: So far, Micals have been the only known partners of MsrB1, and actin is the only target. It is important to identify additional substrates of Micals and characterize other Mical-like enzymes. FUTURE DIRECTIONS: Oxidation of methionine, reviewed here, is an emerging but not well-established mechanism. Studies suggest that methionine oxidation is a form of oxidative damage of proteins, a modification that alters protein structure or function, a tool in redox signaling, and a mechanism that controls protein function. Understanding the functional impact of reversible oxidation of methionine will require identification of targets, substrates, and regulators of Micals and Msrs. Linking the biological processes, in which these proteins participate, might also lead to insights into disease conditions, which involve regulation of actin by Micals and Msrs.
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