ArticleACS catalysis2020
Dynamics of a Key Conformational Transition in the Mechanism of Peroxiredoxin Sulfinylation.
Article in ACS catalysis, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
10 citing papers in PubMed, 22 citations in OpenAlex.
- Protein persulfidation: a ubiquitous modification regulating a broad spectrum of biological processes.Journal of experimental botany · 2026Review
- A katE katG double-knockout E. coli strain eliminates the risk of catalase contamination in recombinant proteins.Applied microbiology and biotechnology · 2026Article
- Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins.Nature chemical biology · 2026Article
- The Ensemble Basis of Allostery and Function: Insights from Models of Local Unfolding.Journal of molecular biology · 2025Review
- Mechanism of glutathionylation of the active site thiols of peroxiredoxin 2.The Journal of biological chemistry · 2025Article
- Oxidative Cysteine Post Translational Modifications Drive the Redox Code Underlying Neurodegeneration and Amyotrophic Lateral Sclerosis.Antioxidants (Basel, Switzerland) · 2024Review
- Anti-Inflammatory Activity of Bryophytes Extracts in LPS-Stimulated RAW264.7 Murine Macrophages.Molecules (Basel, Switzerland) · 2022Article
- Native state fluctuations in a peroxiredoxin active site match motions needed for catalysis.Structure (London, England : 1993) · 2022Article
- 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
- Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peroxiredoxins from the Prx1 subfamily (Prx) are moonlighting peroxidases that operate in peroxide signaling and are regulated by sulfinylation. Prxs offer a major model of protein-thiol oxidative modification. They react with H
Identifiers
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.