ArticleProceedings of the National Academy of Sciences of the United States of America2026
De novo discovery of bicyclic cysteine-rich peptides targeting gasdermin D.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. 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
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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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Who cites it
3 citing papers in PubMed.
- De Novo Discovery of Nonstandard Thioisoindole-Bridged Bicyclic Peptides Targeting Traf2- and NCK-Interacting Kinase.Angewandte Chemie (International ed. in English) · 2026Article
- The gasdermin family: from pyroptosis mechanisms to therapeutic targets.Signal transduction and targeted therapy · 2026Review
- Gasdermin D in Neurodegenerative Diseases: Pathogenic Roles and Therapeutic Perspectives.Molecular neurobiology · 2026Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Gasdermin D (GSDMD) is the principal executor of pyroptosis, a form of proinflammatory programmed cell death misregulation of which is associated with numerous diseases. Despite significant interest, no specific GSDMD inhibitors have been developed for clinical use so far. Here, we developed a strategy to generate mRNA-displayed libraries of bicyclic cysteine-rich peptides (bCRP), and utilized these libraries to develop potent peptide ligands to full-length GSDMD using a two-stage discovery process. Initial hit compounds were de novo discovered from GSDMD affinity selections using Random Nonstandard Peptides Integrated Discovery system, and were then optimized using mRNA display-based saturation mutagenesis. The resulting bCRPs bound to full-length GSDMD (best K
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