ArticleStructure (London, England : 1993)2012
Moonlighting by different stressors: crystal structure of the chaperone species of a 2-Cys peroxiredoxin.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 109 citations in OpenAlex.
- Fast, Comprehensive, and User Customizable Macromolecule Interface Analysis with FACE2FACE.Journal of chemical information and modeling · 2025Article
- Agglomeration: when folded proteins clump together.Biophysical reviews · 2023Review
- Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.Journal of the American Chemical Society · 2023Article
- Glutathione-Related Enzymes and Proteins: A Review.Molecules (Basel, Switzerland) · 2023Review
- Article
- Relevance of peroxiredoxins in pathogenic microorganisms.Applied microbiology and biotechnology · 2021Review
- Peroxiredoxins-The Underrated Actors during Virus-Induced Oxidative Stress.Antioxidants (Basel, Switzerland) · 2021Review
- Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities.Redox biology · 2021Review
- Review
- Taking Advantage of the Morpheein Behavior of Peroxiredoxin in Bionanotechnology.Bioconjugate chemistry · 2021Review
- Autonomous Non Antioxidant Roles forFrontiers in cellular and infection microbiology · 2021Review
- Real-time monitoring of peroxiredoxin oligomerization dynamics in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cross-talk between redox signalling and protein aggregation.Biochemical Society transactions · 2020Review
- Broad-spectrum antitumor properties of Withaferin A: a proteomic perspective.RSC medicinal chemistry · 2020Review
- Redox Post-translational Modifications of Protein Thiols in Brain Aging and Neurodegenerative Conditions-Focus on S-Nitrosation.Frontiers in aging neuroscience · 2020Review
- Structures, functions, and mechanisms of filament forming enzymes: a renaissance of enzyme filamentation.Biophysical reviews · 2019Review
- Chaperone activation and client binding of a 2-cysteine peroxiredoxin.Nature communications · 2019Article
- Crystal structure of Arabidopsis thaliana peroxiredoxin A C119S mutant.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions.Scientific reports · 2018Article
- Self-assembly of toroidal proteins explored using native mass spectrometry.Chemical science · 2018Article
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
2-Cys peroxiredoxins (Prxs) play two different roles depending on the physiological status of the cell. They are thioredoxin-dependent peroxidases under low oxidative stress and ATP-independent chaperones upon exposure to high peroxide concentrations. These alternative functions have been associated with changes in the oligomerization state from low-(LMW) to high-molecular-weight (HMW) species. Here we present the structures of Schistosoma mansoni PrxI in both states: the LMW decamer and the HMW 20-mer formed by two stacked decamers. The latter is the structure of a 2-Cys Prx chaperonic form. Comparison of the structures sheds light on the mechanism by which chemical stressors, such as high H(2)O(2) concentration and acidic pH, are sensed and translated into a functional switch in this protein family. We also propose a model to account for the in vivo formation of long filaments of stacked Prx rings.
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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.