ArticleChemical science2023
Masked cerulenin enables a dual-site selective protein crosslink.
Article in Chemical science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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
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Who cites it
4 citing papers in PubMed.
- A Hidden Binding Pocket in the β- ketoacyl-ACP Synthase FabB.bioRxiv : the preprint server for biology · 2026Article
- Visualizing acyl carrier protein interactions within a crosslinked type I polyketide synthase.Nature communications · 2025Article
- Cryptic Cerulenin Rearrangement in Ketosynthase Covalent Inhibition.Journal of the American Chemical Society · 2024Article
- Contribution of pks+Microorganisms · 2024Review
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Authors and funding
8 authors.
Funding
Abstract
Protein-reactive natural products such as the fungal metabolite cerulenin are recognized for their value as therapeutic candidates, due to their ability to selectively react with catalytic residues within a protein active site or a complex of protein domains. Here, we explore the development of fatty-acid and polyketide-synthase probes by synthetically modulating cerulenin's functional moieties. Using a mechanism-based approach, we reveal unique reactivity within cerulenin and adapt it for fluorescent labeling and crosslinking of fatty-acid and iterative type-I polyketide synthases. We also describe two new classes of silylcyanohydrin and silylhemiaminal masked crosslinking probes that serve as new tools for activity and structure studies of these biosynthetic pathways.
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Registered trials
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