ArticleJournal of the American Chemical Society2026
Repositioning the Leader Peptide in Graspetide Biosynthesis.
Article in Journal of the American Chemical Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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.
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Who cites it
1 citing paper in PubMed.
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
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5 authors.
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Abstract
Applying enzymes from unique biosynthetic pathways in a combinatorial fashion to garner new-to-nature products has been a long-standing goal of synthetic biology. Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a family of natural products that comprise a broad array of chemical and structural diversity, including mechanically interlocked molecular architectures. Guided by supramolecular recognition of an N-terminal leader sequence, the core region of a precursor peptide is decorated by tailoring enzymes to generate a mature RiPP. Through repositioning the leader sequence of the fuscimiditide precursor peptide C-terminal to the core, we have shown that substrate-selective post-translational modification by the graspetide synthetase, ThfB, is retained
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