ArticlePlant physiology2006
Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses.
Article in Plant physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers, 1 of them a synthesis 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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Who cites it
116 citing papers in PubMed, 1 synthesis or guideline pooled it, 402 citations in OpenAlex.
- The family of glutathione peroxidase proteins and their role against biotic stress in plants: a systematic review.Frontiers in plant science · 2025Pooled it
- Article
- The meiotic achilles' heel: vulnerability and resilience under environmental stress.Protoplasma · 2026Review
- HDA15-Mediated Deacetylation of GPX1 Inhibits Its Nuclear Translocation and Increases Osmotic Stress Sensitivity in Rice.International journal of molecular sciences · 2026Article
- Gene network analysis predicts the primary regulators of ABA-dependent transcriptional activation and repression in Populus roots.PLoS genetics · 2026Article
- Harnessing Antioxidants for Abiotic Stress Management: Mechanistic Insights and Prospects for Sustainable Agriculture.Antioxidants (Basel, Switzerland) · 2026Review
- Transcriptomics-proteomics analysis reveals the role of SiNRX1 in regulating drought stress in foxtail millet (Setaria italica L.).BMC genomics · 2025Article
- The Glutathione Peroxidase Gene Family inAntioxidants (Basel, Switzerland) · 2025Article
- Ferroptosis in plant immunity.Plant communications · 2025Review
- Hydrogen peroxide, ascorbate, and glutathione: building the Foyer-Halliwell-Asada pathway.Planta · 2025Review
- Characterization ofInternational journal of molecular sciences · 2024Article
- Biochemical and Functional Profiling of Thioredoxin-Dependent Cytosolic GPX-like Proteins inBiomolecules · 2024Article
- The impact of light and thioredoxins on the plant thiol-disulfide proteome.Plant physiology · 2024Article
- Persulfidation of plant and bacteroid proteins is involved in legume nodule development and senescence.Journal of experimental botany · 2024Article
- Overexpression ofGenes · 2024Article
- Physiological and molecular changes of onion (Allium cepa L.) seeds under different aging conditions.BMC plant biology · 2024Article
- Genetic diversity of durum wheat (Triticum turgidum ssp. durum) to mitigate abiotic stress: Drought, heat, and their combination.PloS one · 2024Article
- Redox dynamics in seeds ofFrontiers in plant science · 2024Article
- Mechanisms of Antioxidant Resistance in Different Wheat Genotypes under Salt Stress and Hypoxia.International journal of molecular sciences · 2023Article
- Novel insight into functions of ascorbate peroxidase in higher plants: More than a simple antioxidant enzyme.Redox biology · 2023Review
56 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We provide here an exhaustive overview of the glutathione (GSH) peroxidase (Gpx) family of poplar (Populus trichocarpa). Although these proteins were initially defined as GSH dependent, in fact they use only reduced thioredoxin (Trx) for their regeneration and do not react with GSH or glutaredoxin, constituting a fifth class of peroxiredoxins. The two chloroplastic Gpxs display a marked selectivity toward their electron donors, being exclusively specific for Trxs of the y type for their reduction. In contrast, poplar Gpxs are much less specific with regard to their electron-accepting substrates, reducing hydrogen peroxide and more complex hydroperoxides equally well. Site-directed mutagenesis indicates that the catalytic mechanism and the Trx-mediated recycling process involve only two (cysteine [Cys]-107 and Cys-155) of the three conserved Cys, which form a disulfide bridge with an oxidation-redox midpoint potential of -295 mV. The reduction/formation of this disulfide is detected both by a shift on sodium dodecyl sulfate-polyacrylamide gel electrophoresis or by measuring the intrinsic tryptophan fluorescence of the protein. The six genes identified coding for Gpxs are expressed in various poplar organs, and two of them are localized in the chloroplast, with one colocalizing in mitochondria, suggesting a broad distribution of Gpxs in plant cells. The abundance of some Gpxs is modified in plants subjected to environmental constraints, generally increasing during fungal infection, water deficit, and metal stress, and decreasing during photooxidative stress, showing that Gpx proteins are involved in the response to both biotic and abiotic stress conditions.
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