ArticleJournal of medicinal chemistry2026
Covalent Alkynylpyridopyrimidinones Targeting Cysteine 775 of the Epidermal Growth Factor Receptor Overcome Resistance to Current Therapies.
Article in Journal of medicinal chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- On-resin Heck coupling enables small-molecule ligand discovery with covalent peptide-encoded libraries.Chemical science · 2026Article
- Design of dual-effect molecules based on lysosome-targeting strategy: a mechanistic study on synergistic inhibition of ewing sarcoma and coronaviruses.Frontiers in chemistry · 2026Article
Corrections and comments
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Authors and funding
18 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inhibitors of epidermal growth factor receptor (EGFR) kinase activity are clinically effective treatments for lung cancers driven by activating mutations in EGFR. Resistance to inhibitors develops over time, frequently through further mutations in the kinase domain. On-target resistance to third-generation inhibitor osimertinib, commonly develops through C797S mutation that prevents covalent binding. There is an urgent need for new treatments for osimertinib-resistant EGFR mutants that retain the advantages of the covalent mechanism. Compounds were designed and synthesized to covalently inhibit EGFR through C775, a further cysteine residue we identified in the orthosteric site. Optimisation of the alkynylpyridopyrimidinone scaffold we discovered led to potent compounds that demonstrate inhibition of EGFR phosphorylation and tumor growth in all EGFR mutant cell lines. The covalent C775 mode-of-action was comprehensively established. This work demonstrates that covalent targeting of C775 is a viable mechanism for the treatment of pan-EGFR mutated cancers, particularly those resistant to current therapies.
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Registered trials
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