ReviewFrontiers in plant science2019
Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases.
Review in Frontiers in plant science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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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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Who cites it
53 citing papers in PubMed, 111 citations in OpenAlex.
- An In Silico Investigation of the Structural and Evolutionary Features of MAPEG Proteins in Bacteria.Current issues in molecular biology · 2026Article
- Antioxidant Compounds in Microalgae and Cyanobacteria: A Sustainable Source of Bioactive Molecules.Marine drugs · 2026Review
- Sustainable tea plantations: Harnessing chemical-microbial synergy and smart application triangulation for targeted weed control.Journal of advanced research · 2026Review
- Genome-wide identification and expression analysis of the Glutathione S-transferase (GST) gene family in Avicennia marina under salt and auxin stress.BMC plant biology · 2026Article
- Large-scale genomic analysis reveals the origin and evolution of Glutathione S-transferases (GSTs) in plants.BMC genomics · 2026Article
- Pan-Genome-Wide Analysis and Expression Profiling of the Potato GST Gene Family.Plants (Basel, Switzerland) · 2026Article
- The non-catalytic binding of auxin, cytokinin and salicylic acid by tomato Phi class glutathione transferases: insights from computational modelling.Plant molecular biology · 2026Article
- Molecular identification, isolation and functional characterization of a glutathione S-transferase gene CsGST in saffron (Crocus sativus L.).Scientific reports · 2026Article
- Genome-wide analysis of the glutathione S-transferase family inFrontiers in plant science · 2026Article
- Detoxification of deoxynivalenol by pathogen-inducible tau-class glutathione transferases from wheat.The Journal of biological chemistry · 2025Article
- Plant Defense Proteins: Recent Discoveries and Applications.Plants (Basel, Switzerland) · 2025Review
- Glutathione S-transferase in mediating adaptive responses of oats (Avena sativa) to osmotic and cadmium stress: genome-wide analysis.BMC plant biology · 2025Article
- CaBMC plant biology · 2025Article
- PfGSTF2 endows resistance to quizalofop-p-ethyl in Polypogon fugax by GSH conjugation.Plant biotechnology journal · 2025Article
- Genome-wide identification and in silico analysis of GSTs reveals hormone mediated stress response in saffron.Frontiers in plant science · 2025Article
- Review of protein structure-based analyses that illuminate plant stress mechanisms.Computational and structural biotechnology journal · 2025Review
- Toxicological qualities and detoxification trends of fruit by-products for valorization: A review.Open life sciences · 2025Review
- Overlooked and misunderstood: can glutathione conjugates be clues to understanding plant glutathione transferases?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Review
- Metabolism-Based Herbicide Resistance to Mesosulfuron-methyl and Identification of Candidate Genes inPlants (Basel, Switzerland) · 2024Article
- Comparative population genomics reveals convergent and divergent selection in the apricot-peach-plum-mei complex.Horticulture research · 2024Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutathione transferases (GSTs) belong to a ubiquitous multigenic family of enzymes involved in diverse biological processes including xenobiotic detoxification and secondary metabolism. A canonical GST is formed by two domains, the N-terminal one adopting a thioredoxin (TRX) fold and the C-terminal one an all-helical structure. The most recent genomic and phylogenetic analysis based on this domain organization allowed the classification of the GST family into 14 classes in terrestrial plants. These GSTs are further distinguished based on the presence of the ancestral cysteine (Cys-GSTs) present in TRX family proteins or on its substitution by a serine (Ser-GSTs). Cys-GSTs catalyze the reduction of dehydroascorbate and deglutathionylation reactions whereas Ser-GSTs catalyze glutathione conjugation reactions and eventually have peroxidase activity, both activities being important for stress tolerance or herbicide detoxification. Through non-catalytic, so-called ligandin properties, numerous plant GSTs also participate in the binding and transport of small heterocyclic ligands such as flavonoids including anthocyanins, and polyphenols. So far, this function has likely been underestimated compared to the other documented roles of GSTs. In this review, we compiled data concerning the known enzymatic and structural properties as well as the biochemical and physiological functions associated to plant GSTs having a conserved serine in their active site.
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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.