ArticleBiochemistry2009
Glutathione transferases are structural and functional outliers in the thioredoxin fold.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 3 of them syntheses that pooled it.
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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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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
60 citing papers in PubMed, 3 syntheses or guidelines pooled it.
- Pooled it
- Quantitative assessment of the effect of glutathione S-transferase genes GSTM1 and GSTT1 on hepatocellular carcinoma risk.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Pooled it
- Pooled it
- Structural and Functional Insights into a Honey Bee Omega-Class Glutathione S-Transferase Mediating Chemical Sequestration and Antioxidative Stress.Journal of agricultural and food chemistry · 2026Article
- Plant derived biopesticides for controlling imported fire ants (Frontiers in plant science · 2026Review
- The role of glutathione S-transferases in human disease pathogenesis and their current inhibitors.Genes & diseases · 2025Review
- Structural Adaptations of Bacterial Grx3 to Temperature: Pro29 Is Essential for Cold Adaptation inACS omega · 2025Article
- Occurrence of a population of the root-knot nematode, Meloidogyne incognita, with low sensitivity to two major nematicides, fosthiazate and fluopyram, in Japan.Pest management science · 2025Article
- Possible Association of Glutathione S-Transferase Pi 1 (GSTP1) Gene Polymorphism in Iraqi Patients with Breast Cancer.Reports of biochemistry & molecular biology · 2025Article
- Glutathione-Dependent Pathways in Cancer Cells.International journal of molecular sciences · 2024Review
- Sigma-Class Glutathione Transferases (GSTσ): A New Target with Potential for Helminth Control.Tropical medicine and infectious disease · 2024Review
- Repurposing Glutathione Transferases: Directed Evolution Combined with Chemical Modification for the Creation of a Semisynthetic Enzyme with High Hydroperoxidase Activity.Antioxidants (Basel, Switzerland) · 2023Article
- Potent GST Ketosteroid Isomerase Activity Relevant to Ecdysteroidogenesis in the Malaria VectorBiomolecules · 2023Article
- Tat-GSTpi Inhibits Dopaminergic Cells against MPPBiomedicines · 2023Article
- Glutathione-Related Enzymes and Proteins: A Review.Molecules (Basel, Switzerland) · 2023Review
- Immaturin-Nuclease as a Model System for a Gene-Programmed Sexual Development and Rejuvenescence inMicroorganisms · 2022Article
- Biochemical characterization and peptide mass fingerprinting of two glutathione transferases from Biomphalaria alexandrina snails (Gastropoda: Planorbidae).Journal, genetic engineering & biotechnology · 2022Article
- Early loss of glutathione -s- transferase (GST) activity during diverse forms of acute renal tubular injury.Physiological reports · 2022Article
- Bioinformatic Analyses of Peroxiredoxins and RF-Prx: A Random Forest-Based Predictor and Classifier for Prxs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Association of GSTP1 p.Ile105Val (rs1695, c.313A > G) Variant with the Risk of Breast Carcinoma among Egyptian Women.Biochemical genetics · 2021Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Glutathione transferases (GSTs) are ubiquitous scavengers of toxic compounds that fall, structurally and functionally, within the thioredoxin fold suprafamily. The fundamental catalytic capability of GSTs is catalysis of the nucleophilic addition or substitution of glutathione at electrophilic centers in a wide range of small electrophilic compounds. While specific GSTs have been studied in detail, little else is known about the structural and functional relationships between different groupings of GSTs. Through a global analysis of sequence and structural similarity, it was determined that variation in the binding of glutathione between the two major subgroups of cytosolic (soluble) GSTs results in a different mode of glutathione activation. Additionally, the convergent features of glutathione binding between cytosolic GSTs and mitochondrial GST kappa are described. The identification of these structural and functional themes helps to illuminate some of the fundamental contributions of the thioredoxin fold to catalysis in the GSTs and clarify how the thioredoxin fold can be modified to enable new functions.
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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.