ArticleACS infectious diseases2024
Discovery and Biosynthesis of Persiathiacins: Unusual Polyglycosylated Thiopeptides Active Against Multidrug Resistant Tuberculosis.
Article in ACS infectious diseases, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The trial behind it
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Who cites it
5 citing papers in PubMed.
- Total Synthesis ofJournal of the American Chemical Society · 2026Article
- Pharmacokinetic and pharmacodynamic studies of injectable nocathiacin as a novel antibacterial agent.npj antimicrobials and resistance · 2025Article
- Iterative glycosylation on a single residue of a mature lasso peptide.Chemical science · 2025Article
- Mode of Action and Mechanisms of Resistance to the Unusual Polyglycosylated Thiopeptide Antibiotic Persiathiacin A.ACS infectious diseases · 2025Article
- Selective biosynthesis of a rhamnosyl nosiheptide by a novel bacterial rhamnosyltransferase.Microbial biotechnology · 2024Article
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
Thiopeptides are ribosomally biosynthesized and post-translationally modified peptides (RiPPs) that potently inhibit the growth of Gram-positive bacteria by targeting multiple steps in protein biosynthesis. The poor pharmacological properties of thiopeptides, particularly their low aqueous solubility, has hindered their development into clinically useful antibiotics. Antimicrobial activity screens of a library of Actinomycetota extracts led to discovery of the novel polyglycosylated thiopeptides persiathiacins A and B from
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Registered trials
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