ReviewThe Biochemical journal2001
Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily.
Review in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 539 papers.
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Who cites it
539 citing papers in PubMed, 1,524 citations in OpenAlex.
- Identification and functional validation of glutathione S-transferase genes involved in detoxification of sulfoxaflor, afidopyropen and lambda-cyhalothrin in Aphis glycines.Pest management science · 2026Article
- Food-dependent activation of one-carbon metabolism during heat shock in Mytilus californianus.The Journal of experimental biology · 2026Article
- Functional Characterization and Inhibition Analysis of a Glutathione Transferase fromPharmaceuticals (Basel, Switzerland) · 2026Article
- Genome-wide characterization and transcriptional responses of Tuta absoluta glutathione S-transferases to chlorantraniliprole and spinetoram.Journal of insect science (Online) · 2026Article
- Identification of myokines associated with the pathological stress response in theJournal of neuromuscular diseases · 2026Article
- Identification and Characterization of the Detoxification Genes from the Transcriptome ofInsects · 2026Article
- Glutathione Transferase as a Potential First-Tier Biomarker of Environmental Pollution in Workers and Residents of Umbria Region, Italy.Antioxidants (Basel, Switzerland) · 2026Article
- Large-scale genomic analysis reveals the origin and evolution of Glutathione S-transferases (GSTs) in plants.BMC genomics · 2026Article
- An integrated in vitro and in silico approach to assess the potential inhibitory actions of auxins on human placental glutathione S-transferase P1-1.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Tanzanian goat gut microbiomes adapt to roadside pollutants and environmental stressors.Microbiology spectrum · 2026Article
- Hydrophobic tagging: A promising paradigm for targeted protein degradation.Cell insight · 2026Review
- Genome-wide identification of the GST reveals ZmGST1 enhances the resistance to Exserohilum turcicum in maize.BMC plant biology · 2026Article
- Sunitinib and Fenofibrate as Combination Therapy for MDR Glioblastoma: Insights fromOncology research · 2026Article
- Understanding the role of non-HLA antibodies in kidney transplantation: a literature review.Frontiers in immunology · 2026Review
- Article
- Genome-wide analysis of the glutathione S-transferase family inFrontiers in plant science · 2026Article
- Maternal Vitamin D Status, Oxidative Stress, and Implications for Neonatal Development: A Cross-Sectional Study.Metabolites · 2025Article
- Aging of the human eye lens: Epigenetic landscape and therapeutic targets in age‑related cataracts (Review).International journal of molecular medicine · 2025Review
- Punica granatum extract demonstrates antiparasitic effects against Caligus clemensi through in silico and in vitro studies.Scientific reports · 2025Article
- Evidence of Intraspecific Adaptive Variation in the American Pika (Ochotona princeps) on a Continental Scale Using a Target Enrichment and Mitochondrial Genome Skimming Approach.Molecular ecology · 2025Article
479 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glutathione transferases (GSTs; also known as glutathione S-transferases) are major phase II detoxification enzymes found mainly in the cytosol. In addition to their role in catalysing the conjugation of electrophilic substrates to glutathione (GSH), these enzymes also carry out a range of other functions. They have peroxidase and isomerase activities, they can inhibit the Jun N-terminal kinase (thus protecting cells against H(2)O(2)-induced cell death), and they are able to bind non-catalytically a wide range of endogenous and exogenous ligands. Cytosolic GSTs of mammals have been particularly well characterized, and were originally classified into Alpha, Mu, Pi and Theta classes on the basis of a combination of criteria such as substrate/inhibitor specificity, primary and tertiary structure similarities and immunological identity. Non-mammalian GSTs have been much less well characterized, but have provided a disproportionately large number of three-dimensional structures, thus extending our structure-function knowledge of the superfamily as a whole. Moreover, several novel classes identified in non-mammalian species have been subsequently identified in mammals, sometimes carrying out functions not previously associated with GSTs. These studies have revealed that the GSTs comprise a widespread and highly versatile superfamily which show similarities to non-GST stress-related proteins. Independent classification systems have arisen for groups of organisms such as plants and insects. This review surveys the classification of GSTs in non-mammalian sources, such as bacteria, fungi, plants, insects and helminths, and attempts to relate them to the more mainstream classification system for mammalian enzymes. The implications of this classification with regard to the evolution of GSTs are discussed.
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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.