ArticleOrganic & biomolecular chemistry2009
IDENTIFICATION OF CONOIDIN A AS A COVALENT INHIBITOR OF PEROXIREDOXIN II.
Article in Organic & biomolecular chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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
44 citing papers in PubMed, 77 citations in OpenAlex.
- Mechanism-based peroxiredoxin 3 inhibitors exploit a covalent warhead for cancer therapy.Science advances · 2025Article
- Successful axonal regeneration is associated with intraneuronal metabolic reprogramming.iScience · 2025Article
- Insights into Free Drug Release from EfficaciousACS chemical biology · 2025Article
- Temporal coordination of the transcription factor response to HNature communications · 2024Article
- Intracerebral hemorrhage-induced brain injury in mice: The role of peroxiredoxin 2-Toll-like receptor 4 inflammatory axis.CNS neuroscience & therapeutics · 2024Article
- PRDX1 inhibits ferroptosis by binding to Cullin-3 as a molecular chaperone in colorectal cancer.International journal of biological sciences · 2024Article
- Reactive oxygen species and its role in pathogenesis and resistance to therapy in acute myeloid leukemia.Cancer drug resistance (Alhambra, Calif.) · 2024Review
- Depletion of peroxiredoxin II promotes keratinocyte apoptosis and alleviates psoriatic skin lesions via the PI3K/AKT/GSK3β signaling axis.Cell death discovery · 2023Article
- Article
- Peroxiredoxin 2: An Important Element of the Antioxidant Defense of the Erythrocyte.Antioxidants (Basel, Switzerland) · 2023Review
- Article
- Peroxiredoxin, Senescence, and Cancer.Cells · 2022Review
- Genetic Disruption of Toxoplasma gondii peroxiredoxin (TgPrx) 1 and 3 Reveals the Essential Role of TgPrx3 in Protecting Mice from Fatal Consequences of ToxoplasmosisInternational journal of molecular sciences · 2022Article
- Structural New Data for Mitochondrial Peroxiredoxin FromFrontiers in cellular and infection microbiology · 2022Article
- Proteomic and Functional Analysis of the Effects of Quinoxaline Derivatives onFrontiers in cellular and infection microbiology · 2022Article
- Repurposing of auranofin and honokiol as antifungals againstVirulence · 2021Article
- Effect of 2-Cys Peroxiredoxins Inhibition on Redox Modifications of Bull Sperm Proteins.International journal of molecular sciences · 2021Article
- Relevance of peroxiredoxins in pathogenic microorganisms.Applied microbiology and biotechnology · 2021Review
- Peroxiredoxin alleviates the fitness costs of imidacloprid resistance in an insect pest of rice.PLoS biology · 2021Article
- Rhythmic glucose metabolism regulates the redox circadian clockwork in human red blood cells.Nature communications · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
Abstract
Conoidin A (1) is an inhibitor of host cell invasion by the protozoan parasite Toxoplasma gondii. In the course of studies aimed at identifying potential targets of this compound, we determined that it binds to the T. gondii enzyme peroxiredoxin II (TgPrxII). Peroxiredoxins are a widely conserved family of enzymes that function in antioxidant defense and signal transduction, and changes in PrxII expression are associated with a variety of human diseases, including cancer. Disruption of the TgPrxII gene by homologous recombination had no effect on the sensitivity of the parasites to 1, suggesting that TgPrxII is not the invasion-relevant target of 1. However, we showed that 1 binds covalently to the peroxidatic cysteine of TgPrxII, inhibiting its enzymatic activity in vitro. Studies with human epithelial cells showed that 1 also inhibits hyperoxidation of human PrxII. These data identify Conoidin A as a novel inhibitor of this important class of antioxidant and redox signaling enzymes.
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.