ArticleScientific reports2015
Sulphur Atoms from Methionines Interacting with Aromatic Residues Are Less Prone to Oxidation.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Article
- Probing the Influence of Sulfur-Aromatic Interactions on the Electronic Structure of Gas-Phase Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- A methionine-lined active site governs carbocation stabilization and product specificity in a bacterial terpene synthase.FEBS letters · 2026Article
- Mechanistic insight into the oxidative degradation of monoclonal antibodies: relevance to developability and the design of stable pharmaceutical formulations.Biochemical Society transactions · 2026Review
- Computational Identification of Potential Novel Allosteric IHF Inhibitors Using QSAR Modeling to Inhibit Plasmid-Mediated Antibiotic Resistance.International journal of molecular sciences · 2026Article
- Gas Tunnel Engineering of Prolyl Hydroxylase Reprograms Hypoxia Signaling in Cells.Angewandte Chemie (International ed. in English) · 2024Article
- Redox-dependent plasticity of oxMIF facilitates its interaction with CD74 and therapeutic antibodies.Redox biology · 2024Article
- Copper(I)-nitrene platform for chemoproteomic profiling of methionine.Nature communications · 2024Article
- The Role of Amino Acids in Non-Enzymatic Antioxidant Mechanisms in Cancer: A Review.Metabolites · 2023Review
- Proximal Methionine Amino Acid Residue Affects the Properties of Redox-Active Tryptophan in an Artificial Model Protein.ACS omega · 2023Article
- Target Prediction of 5,10,15,20-Tetrakis(4'-Sulfonatophenyl)-Porphyrin Using Molecular Docking.Pharmaceutics · 2022Article
- Phylogenies from unaligned proteomes using sequence environments of amino acid residues.Scientific reports · 2022Article
- Comparative Analysis of Sulfonium-π, Ammonium-π, and Sulfur-π Interactions and Relevance to SAM-Dependent Methyltransferases.Journal of the American Chemical Society · 2022Article
- A novel method for in silico assessment of Methionine oxidation risk in monoclonal antibodies: Improvement over the 2-shell model.PloS one · 2022Article
- The Role of Methionine Residues in the Regulation of Liquid-Liquid Phase Separation.Biomolecules · 2021Review
- Machine learning prediction of methionine and tryptophan photooxidation susceptibility.Molecular therapy. Methods & clinical development · 2021Article
- Peripheral Methionine Residues Impact Flavin Photoreduction and Protonation in an Engineered LOV Domain Light Sensor.Biochemistry · 2021Article
- Susceptibility of Protein Methionine Oxidation in Response to Hydrogen Peroxide Treatment-Ex Vivo Versus In Vitro: A Computational Insight.Antioxidants (Basel, Switzerland) · 2020Article
- Methionine in proteins: The Cinderella of the proteinogenic amino acids.Protein science : a publication of the Protein Society · 2019Review
- A comprehensive computational study of amino acid interactions in membrane proteins.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methionine residues exhibit different degrees of susceptibility to oxidation. Although solvent accessibility is a relevant factor, oxidation at particular sites cannot be unequivocally explained by accessibility alone. To explore other possible structural determinants, we assembled different sets of oxidation-sensitive and oxidation-resistant methionines contained in human proteins. Comparisons of the proteins containing oxidized methionines with all proteins in the human proteome led to the conclusion that the former exhibit a significantly higher mean value of methionine content than the latter. Within a given protein, an examination of the sequence surrounding the non-oxidized methionine revealed a preference for neighbouring tyrosine and tryptophan residues, but not for phenylalanine residues. However, because the interaction between sulphur atoms and aromatic residues has been reported to be important for the stabilization of protein structure, we carried out an analysis of the spatial interatomic distances between methionines and aromatic residues, including phenylalanine. The results of these analyses uncovered a new determinant for methionine oxidation: the S-aromatic motif, which decreases the reactivity of the involved sulphur towards oxidants.
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