ArticleChemical science2025
Iterative glycosylation on a single residue of a mature lasso peptide.
Article in Chemical science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Iterative acylation on mature lasso peptides by widespread acetyltransferases.Nature chemical biology · 2026Article
- RiPP recognition elements evolved to prevent pathway interference through leader peptide discrimination.Nature communications · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Iterative catalysis is a unique characteristic of the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs) to boost structural and biological diversity. Lasso peptides are an abundant class of RiPPs featuring lariat knot structures, which pose obstacles to iterative post-translational modifications (PTMs) after macrocyclization. Here, we present a unique glycotransferase (GT), IgtG, that iteratively glycosylates a Ser residue up to four times within a mature lasso peptide, as the final biosynthetic step of davasins. Such iterative catalysis diverges from classical iterative modifications on linear peptides. Bioinformatic analysis reveals 24 IgtG-like GTs that are potentially involved in the biosynthesis of graspetides, and IgtG-like GTs are evolutionarily distinct from known RiPP GTs. The discovery of PTM enzymes functioning on mature lasso peptides showcases the divergent biosynthetic strategies of RiPPs and provides valuable enzymatic tools for diversification of lasso peptides through combinatorial biosynthesis.
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.