ArticleThe Journal of biological chemistry2012
Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Improving pJournal of chemical theory and computation · 2025Article
- Predicting Reactive Cysteines with Implicit-Solvent-Based Continuous Constant pH Molecular Dynamics in Amber.Journal of chemical theory and computation · 2020Article
- Article
- Myristoylated methionine sulfoxide reductase A is a late endosomal protein.The Journal of biological chemistry · 2018Article
- Combining six genome scan methods to detect candidate genes to salinity in the Mediterranean striped red mullet (Mullus surmuletus).BMC genomics · 2018Article
- A Methionine Residue Promotes Hyperoxidation of the Catalytic Cysteine of Mouse Methionine Sulfoxide Reductase A.Biochemistry · 2016Article
- Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii.PloS one · 2015Article
- Methionine oxidation and reduction in proteins.Biochimica et biophysica acta · 2014Review
- Stereospecific oxidation of calmodulin by methionine sulfoxide reductase A.Free radical biology & medicine · 2013Article
- A low pKa cysteine at the active site of mouse methionine sulfoxide reductase A.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
Abstract
Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide. The cytosolic form of the enzyme is myristoylated, but it is not known to translocate to membranes, and the function of myristoylation is not established. We compared the biochemical and biophysical properties of myristoylated and nonmyristoylated mouse methionine sulfoxide reductase A. These were almost identical for both forms of the enzyme, except that the myristoylated form reduced methionine sulfoxide in protein much faster than the nonmyristoylated form. We determined the solution structure of the myristoylated protein and found that the myristoyl group lies in a relatively surface exposed "myristoyl nest." We propose that this structure functions to enhance protein-protein interaction.
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Registered trials
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