ReviewFree radical biology & medicine2017
Regulated methionine oxidation by monooxygenases.
Review in Free radical biology & medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
38 citing papers in PubMed, 83 citations in OpenAlex.
- Prevalence and Functional Roles of Intrinsic Disorder in the [F-actin]-monooxygenase MICAL Family Members and their Interactors.Cell biochemistry and biophysics · 2026Article
- Chiral methionine oxidation reagents reveal stereospecific proteome modifications.bioRxiv : the preprint server for biology · 2026Article
- Methionine Oxidation Footprinting in Intact Proteins (MOFIP) Using Top-Down Proteomics.Proteomics · 2025Article
- Formylation facilitates the reduction of oxidized initiator methionines.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Copper(I)-nitrene platform for chemoproteomic profiling of methionine.Nature communications · 2024Article
- Methionine Alkylation as an Approach to Quantify Methionine Oxidation Using Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Health position paper and redox perspectives - Disease burden by transportation noise.Redox biology · 2024Review
- Substrate-dependent metabolomic signatures of myeloperoxidase activity in airway epithelial cells: Implications for early cystic fibrosis lung disease.Free radical biology & medicine · 2023Article
- Parallel actin monomers in the 8S complex of actin-INF2.Journal of biomolecular structure & dynamics · 2023Article
- Genomic Analysis of G2P[4] Group A Rotaviruses in Zambia Reveals Positive Selection in Amino Acid Site 7 of Viral Protein 3.Viruses · 2023Article
- MICAL-mediated oxidation of actin and its effects on cytoskeletal and cellular dynamics.Frontiers in cell and developmental biology · 2023Review
- A peptide-crosslinking approach identifies HSPA8 and PFKL as selective interactors of an actin-derived peptide containing reduced and oxidized methionine.RSC chemical biology · 2022Article
- The Potential of a Protein Model Synthesized Absent of Methionine.Molecules (Basel, Switzerland) · 2022Review
- Article
- Protein folding stabilities are a major determinant of oxidation rates for buried methionine residues.The Journal of biological chemistry · 2022Article
- Article
- Profilin and Mical combine to impair F-actin assembly and promote disassembly and remodeling.Nature communications · 2021Article
- The Role of Methionine Residues in the Regulation of Liquid-Liquid Phase Separation.Biomolecules · 2021Review
- Propagation of F-actin disassembly via Myosin15-Mical interactions.Science advances · 2021Article
- Enhanced Production of the Mical Redox Domain for Enzymology and F-actin Disassembly Assays.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Protein function can be regulated via post-translational modifications by numerous enzymatic and non-enzymatic mechanisms, including oxidation of cysteine and methionine residues. Redox-dependent regulatory mechanisms have been identified for nearly every cellular process, but the major paradigm has been that cellular components are oxidized (damaged) by reactive oxygen species (ROS) in a relatively unspecific way, and then reduced (repaired) by designated reductases. While this scheme may work with cysteine, it cannot be ascribed to other residues, such as methionine, whose reaction with ROS is too slow to be biologically relevant. However, methionine is clearly oxidized in vivo and enzymes for its stereoselective reduction are present in all three domains of life. Here, we revisit the chemistry and biology of methionine oxidation, with emphasis on its generation by enzymes from the monooxygenase family. Particular attention is placed on MICALs, a recently discovered family of proteins that harbor an unusual flavin-monooxygenase domain with an NADPH-dependent methionine sulfoxidase activity. Based on structural and kinetic information we provide a rational framework to explain MICAL mechanism, inhibition, and regulation. Methionine residues that are targeted by MICALs are reduced back by methionine sulfoxide reductases, suggesting that reversible methionine oxidation may be a general mechanism analogous to the regulation by phosphorylation by kinases/phosphatases. The identification of new enzymes that catalyze the oxidation of methionine will open a new area of research at the forefront of redox signaling.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.