ArticleJournal of bacteriology2025
Reductive activation of the disulfide-containing antibiotic thiolutin is mediated by both bacillithiol and FAD-dependent disulfide reductases.
Article in Journal of bacteriology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Design, Synthesis, and Antitubercular Activity of Thiolutin-Cycloserine Hybrids: Reducing Cytotoxicity.Microorganisms · 2026Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Metal ions are universally essential for life and are required for critical enzymes throughout metabolism. Metalloenzymes rely on metal import and trafficking pathways for loading of the desired metal. Many microbes produce natural products that serve as metal chelators, both for their own nutrition and to serve as antimicrobials. In response to infection, our immune cells restrict bacterial growth by deploying proteins that chelate metal ions as part of nutritional immunity. Cells respond to metal depletion by the activation of pathways that prioritize metal delivery to the most essential enzymes. Dithiolopyrrolone (DTP) class natural products are prodrugs that are reduced in cells to generate a potent, dithiol-containing zinc chelator. Here, we identify the cellular reductants, bacillithiol and the FAD-dependent oxidoreductases TrxB and AhpF, that activate the DTP antibiotic thiolutin in
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Registered trials
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