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Structural Studies of Fourth-Generation EGFR Inhibitors Reveal Insights into Selective T790M and C797S Targeting.

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ACS medicinal chemistry letters 📖 저널 OA 100% 2024: 2/2 OA 2025: 12/12 OA 2026: 16/16 OA 2024~2026 2026
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Damghani T, Song S, Lin KS, Li J, Heppner DE

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Inhibitors targeting mutant EGFR remain a persistent need in combating drug resistance in non-small cell lung cancer.

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↓ .bib ↓ .ris
APA Damghani T, Song S, et al. (2026). Structural Studies of Fourth-Generation EGFR Inhibitors Reveal Insights into Selective T790M and C797S Targeting.. ACS medicinal chemistry letters. https://doi.org/10.1021/acsmedchemlett.5c00725
MLA Damghani T, et al.. "Structural Studies of Fourth-Generation EGFR Inhibitors Reveal Insights into Selective T790M and C797S Targeting.." ACS medicinal chemistry letters, 2026.
PMID 41684669 ↗

Abstract

Inhibitors targeting mutant EGFR remain a persistent need in combating drug resistance in non-small cell lung cancer. To better understand the molecular factors involved in targeting T790M and C797S mutations, we determined X-ray cocrystal structures of fourth-generation inhibitors BI-8128 and BI-4732. Analysis from molecular dynamics and thermodynamic integration calculations correlated with biochemical and cellular measurements indicate that BI-8128 binds the double T790M/C797S more strongly than the single mutations individually. This observation showcases strengths in the design of these fourth-generation EGFR inhibitors as profile criteria require drugs to inhibit an array of oncogenic and drug resistance mutations.

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Supplementary Material

Supplementary Material
Supporting Information DocumentASSOCIATED CONTENT
Supporting Information
The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acsmedchemlett.5c00725.
Methods (protein expression, crystallization, biochemical activity assays, molecular dynamics simulations), crystallography and refinement statistics, extended structural images (PDF)

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