ArticleRSC chemical biology2026
Exploring RiPP-derived
Article in RSC chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipopeptides possess diverse bioactivities with widespread uses as antimicrobial drugs and biosurfactants but their biosynthetic engineering remains challenging. Classical lipopeptides (such as daptomycin or surfactin) are biosynthesized by modular, non-ribosomal megasynthetases. An alternative streamlined route to lipopeptides are the ribosomally synthesized and post-translationally modified peptides (RiPPs) derived from gene-encoded precursor proteins. We recently characterized a novel class of post-translational modification enzymes in RiPPs that catalyze fatty acylation of ornithine and lysine side chains. The resulting lipopeptides were termed selidamides. To assess the use of selidamide
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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.