ArticleFree radical biology & medicine2013
Stereospecific oxidation of calmodulin by methionine sulfoxide reductase A.
Article in Free radical biology & medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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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.
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Who cites it
23 citing papers in PubMed, 32 citations in OpenAlex.
- Role of Redox-Induced Protein Modifications in Spermatozoa in Health and Disease.Antioxidants (Basel, Switzerland) · 2025Review
- 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
- The Role of Methionine Residues in the Regulation of Liquid-Liquid Phase Separation.Biomolecules · 2021Review
- Individuals Diagnosed with Binge-Eating Disorder Have DNA Hypomethylated Sites in Genes of the Metabolic System: A Pilot Study.Nutrients · 2021Article
- Met125 is essential for maintaining the structural integrity of calmodulin's C-terminal domain.Scientific reports · 2020Article
- Methionine in proteins: The Cinderella of the proteinogenic amino acids.Protein science : a publication of the Protein Society · 2019Review
- Temporal pattern of neuronal insulin release during Caenorhabditis elegans aging: Role of redox homeostasis.Aging cell · 2019Article
- Drosophila methionine sulfoxide reductase A (MSRA) lacks methionine oxidase activity.Free radical biology & medicine · 2019Article
- Methionine in Proteins: It's Not Just for Protein Initiation Anymore.Neurochemical research · 2019Review
- The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function.Antioxidants (Basel, Switzerland) · 2018Review
- Oxidation of Methionine 77 in Calmodulin Alters Mouse Growth and Behavior.Antioxidants (Basel, Switzerland) · 2018Article
- Myristoylated methionine sulfoxide reductase A is a late endosomal protein.The Journal of biological chemistry · 2018Article
- Dimethyl sulfide protects against oxidative stress and extends lifespan via a methionine sulfoxide reductase A-dependent catalytic mechanism.Aging cell · 2017Article
- Methionine residues around phosphorylation sites are preferentially oxidized in vivo under stress conditions.Scientific reports · 2017Article
- Sulphur Atoms from Methionines Interacting with Aromatic Residues Are Less Prone to Oxidation.Scientific reports · 2015Article
- Regulation of protein function by reversible methionine oxidation and the role of selenoprotein MsrB1.Antioxidants & redox signaling · 2015Review
- Corynebacterium diphtheriae methionine sulfoxide reductase a exploits a unique mycothiol redox relay mechanism.The Journal of biological chemistry · 2015Article
- Methionine sulfoxide reductase A negatively controls microglia-mediated neuroinflammation via inhibiting ROS/MAPKs/NF-κB signaling pathways through a catalytic antioxidant function.Antioxidants & redox signaling · 2015Article
- Selenoproteins: molecular pathways and physiological roles.Physiological reviews · 2014Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Methionine sulfoxide reductase A has long been known to reduce S-methionine sulfoxide, both as a free amino acid and within proteins. Recently the enzyme was shown to be bidirectional, capable of oxidizing free methionine and methionine in proteins to S-methionine sulfoxide. A feasible mechanism for controlling the directionality has been proposed, raising the possibility that reversible oxidation and reduction of methionine residues within proteins is a redox-based mechanism for cellular regulation. We undertook studies aimed at identifying proteins that are subject to site-specific, stereospecific oxidation and reduction of methionine residues. We found that calmodulin, which has nine methionine residues, is such a substrate for methionine sulfoxide reductase A. When calmodulin is in its calcium-bound form, Met77 is oxidized to S-methionine sulfoxide by methionine sulfoxide reductase A. When methionine sulfoxide reductase A operates in the reducing direction, the oxidized calmodulin is fully reduced back to its native form. We conclude that reversible covalent modification of Met77 may regulate the interaction of calmodulin with one or more of its many targets.
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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.