ArticleRSC chemical biology2022
An intramodular thioesterase domain catalyses chain release in the biosynthesis of a cytotoxic virulence factor.
Article in RSC chemical biology, 2022. 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.
- Non-canonical thioesterases in bacterial non-ribosomal peptide biosynthesis.The Journal of antibiotics · 2025Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An essential step in the biosynthesis of polyketide and non-ribosomal peptide natural products is cleavage of the thioester bond that tethers the acyl/peptidyl chain to its biosynthetic enzyme. In modular polyketide synthases (PKS) and non-ribosomal peptide synthetases (NRPS) chain release is typically catalysed by a single C-terminal thioesterase domain. A clear exception is the bimodular PKS-NRPS BurA that produces gonyol-an intermediate in the biosynthesis of the cytotoxic
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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.