ArticleProtein science : a publication of the Protein Society2019
Redox-regulated methionine oxidation of Arabidopsis thaliana glutathione transferase Phi9 induces H-site flexibility.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Protein turnover in plants-cost of synthesis, repair, and crop engineering opportunities.Plant physiology · 2026Review
- Molecular Insights into the Action Mechanism, Resistance Development, and Ecological Risks of Cyantraniliprole.International journal of molecular sciences · 2026Review
- Review of protein structure-based analyses that illuminate plant stress mechanisms.Computational and structural biotechnology journal · 2025Review
- Evaluation of the Effectiveness of Innovative Sorbents in Restoring Enzymatic Activity of Soil Contaminated with Bisphenol A (BPA).Molecules (Basel, Switzerland) · 2024Article
- Leafhopper salivary vitellogenin mediates virus transmission to plant phloem.Nature communications · 2024Article
- Glutathione Transferases Are Involved in the Genotype-Specific Salt-Stress Response of Tomato Plants.Antioxidants (Basel, Switzerland) · 2023Article
- (De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants.Life (Basel, Switzerland) · 2022Review
- Co-overexpression ofFrontiers in plant science · 2022Article
- Physiological Roles of Plant Methionine Sulfoxide Reductases in Redox Homeostasis and Signaling.Antioxidants (Basel, Switzerland) · 2018Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Glutathione transferase enzymes help plants to cope with biotic and abiotic stress. They mainly catalyze the conjugation of glutathione (GSH) onto xenobiotics, and some act as glutathione peroxidase. With X-ray crystallography, kinetics, and thermodynamics, we studied the impact of oxidation on Arabidopsis thaliana glutathione transferase Phi 9 (GSTF9). GSTF9 has no cysteine in its sequence, and it adopts a universal GST structural fold characterized by a typical conserved GSH-binding site (G-site) and a hydrophobic co-substrate-binding site (H-site). At elevated H
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Registered trials
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