ArticleNature communications2019
Chaperone activation and client binding of a 2-cysteine peroxiredoxin.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed.
- Fungal oxidative stress tolerance depends on peroxiredoxin PrxA-mediated redox signaling to mitochondrial cytochrome c peroxidase Ccp1.The Journal of biological chemistry · 2026Article
- Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins.Nature chemical biology · 2026Article
- Chimerization expands peroxiredoxin scope.Nature chemical biology · 2026Article
- HAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Linoleic Hydroperoxides Are Potent Hyperoxidative Agents of Sensitive and Robust Typical 2-Cys Peroxiredoxins.Antioxidants (Basel, Switzerland) · 2025Article
- The interactome of the Bakers' yeast peroxiredoxin Tsa1 implicates it in redox regulation of intermediary metabolism, glycolysis, and zinc homeostasis.Metallomics : integrated biometal science · 2025Article
- Unraveling the Role of Proteinopathies in Parasitic Infections.Biomedicines · 2025Review
- Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.Journal of the American Chemical Society · 2023Article
- Prx4 acts as DAMP in shrimp, enhancing bacterial resistance via the toll pathway and prophenoloxidase activation.iScience · 2023Article
- Characterization of the Neospora caninum peroxiredoxin: a novel peroxidase and antioxidant enzyme.Parasitology research · 2022Article
- Article
- Chalcones identify cTXNPx as a potential antileishmanial drug target.PLoS neglected tropical diseases · 2021Article
- Effects of Serine or Threonine in the Active Site of Typical 2-Cys Prx on Hyperoxidation Susceptibility and on Chaperone Activity.Antioxidants (Basel, Switzerland) · 2021Article
- Network-based analysis of virulence factors for uncovering Aeromonas veronii pathogenesis.BMC microbiology · 2021Article
- 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
- Moonlighting Proteins in the Fuzzy Logic of Cellular Metabolism.Molecules (Basel, Switzerland) · 2020Review
- The mitochondrial peroxiredoxin displays distinct roles in different developmental stages of African trypanosomes.Redox biology · 2020Article
- Cross-talk between redox signalling and protein aggregation.Biochemical Society transactions · 2020Review
- Structures, functions, and mechanisms of filament forming enzymes: a renaissance of enzyme filamentation.Biophysical reviews · 2019Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Many 2-Cys-peroxiredoxins (2-Cys-Prxs) are dual-function proteins, either acting as peroxidases under non-stress conditions or as chaperones during stress. The mechanism by which 2-Cys-Prxs switch functions remains to be defined. Our work focuses on Leishmania infantum mitochondrial 2-Cys-Prx, whose reduced, decameric subpopulation adopts chaperone function during heat shock, an activity that facilitates the transition from insects to warm-blooded host environments. Here, we have solved the cryo-EM structure of mTXNPx in complex with a thermally unfolded client protein, and revealed that the flexible N-termini of mTXNPx form a well-resolved central belt that contacts and encapsulates the unstructured client protein in the center of the decamer ring. In vivo and in vitro cross-linking studies provide further support for these interactions, and demonstrate that mTXNPx decamers undergo temperature-dependent structural rearrangements specifically at the dimer-dimer interfaces. These structural changes appear crucial for exposing chaperone-client binding sites that are buried in the peroxidase-active protein.
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What OpenQuestion holds
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.