ArticleProtein science : a publication of the Protein Society1998
Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
Article in Protein science : a publication of the Protein Society, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- The Role of Peroxiredoxins in Cancer Development.Biology · 2023Review
- Bioinformatic Analyses of Peroxiredoxins and RF-Prx: A Random Forest-Based Predictor and Classifier for Prxs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Rice Lesion Mimic Mutants (LMM): The Current Understanding of Genetic Mutations in the Failure of ROS Scavenging during Lesion Formation.Plants (Basel, Switzerland) · 2021Review
- Structure of the Prx6-subfamily 1-Cys peroxiredoxin from Sulfolobus islandicus.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria.Journal of bacteriology · 2015Review
- The role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancer.Free radical biology & medicine · 2011Review
- Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.Current opinion in structural biology · 2011Review
- Identification of S-nitrosylation of proteins of Helicobacter pylori in response to nitric oxide stress.Journal of microbiology (Seoul, Korea) · 2011Article
- Genome-wide analysis of thioredoxin fold superfamily peroxiredoxins in Arabidopsis and rice.Plant signaling & behavior · 2010Article
- An extracellular disulfide bond forming protein (DsbF) from Mycobacterium tuberculosis: structural, biochemical, and gene expression analysis.Journal of molecular biology · 2010Article
- Crystallization and preliminary crystallographic analysis of mouse peroxiredoxin II with significant pseudosymmetry.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Protein-protein interactions within peroxiredoxin systems.Photosynthesis research · 2006Review
- Biochemical dysfunction in heart mitochondria exposed to ischaemia and reperfusion.The Biochemical journal · 2005Review
- Redox paradox: insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets.Diabetes · 2005Review
- Differential gene expression in response to hydrogen peroxide and the putative PerR regulon of Synechocystis sp. strain PCC 6803.Journal of bacteriology · 2004Article
- Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity.Plant physiology · 2003Article
- Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor.Plant physiology · 2001Article
- Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization.Journal of bacteriology · 2001Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peroxiredoxins catalyze reduction of hydrogen peroxide or alkyl peroxide, to water or the corresponding alcohol. Detailed analysis of their sequences indicates that these enzymes possess a thioredoxin (Trx)-like fold and consequently are homologues of both thioredoxin and glutathione peroxidase (GPx). Sequence- and structure-based multiple sequence alignments indicate that the peroxiredoxin active site cysteine and GPx active site selenocysteine are structurally equivalent. Homologous peroxiredoxin and GPx enzymes are predicted to catalyze equivalent reactions via similar reaction intermediates.
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