Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Elucidating the role of the T790M mutation in BLU-945 selectivity for mutant EGFR: structural and energetic insights.

Journal of computer-aided molecular design - 21 Feb 2026

Tariq Amina, Shoaib Muhammad, Qu Lingbo, Nan Xiaofei, Song Jinshuai

Abstract excerpt

Resistance mutations in the epidermal growth factor receptor (EGFR), particularly the gatekeeper T790M mutation, pose a major challenge for tyrosine kinase inhibitors in the treatment of non-small cell lung cancer. Previous experimental studies reported that the inhibitor BLU-945 selectively targets EGFR variants (EGFRL858R, EGFRL858R/T790M, and EGFRL858R/T790M/C797S) while sparing wild-type EGFR. Here, we...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acrylamides
Share to Carcinoma, Non-Small-Cell Lung

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Drug Resistance, Neoplasm

Share to ErbB Receptors

Share to Lung Neoplasms

Share to Molecular Dynamics Simulation

Share to Protein Kinase Inhibitors

Share to Thiazoles

Source

Identifiers

PMID: 41721922
DOI: 10.1007/s10822-026-00770-0

Genes

EGFR
MET

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 23 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Elucidating the role of the T790M mutation in BLU-945 selectivity for mutant EGFR: structural and energetic insights.PMID 41721922Read ↗

Structural elements that enable specificity for mutant EGFR kinase domains with next-generation small-molecule inhibitors.Semantic proximity Read ↗

Binding Thermodynamics of Fourth-Generation EGFR Inhibitors Revealed by Absolute Binding Free Energy Calculations.Semantic proximity Read ↗

Structural basis for the altered drug sensitivities of non-small cell lung cancer-associated mutants of human epidermal growth factor receptor.Semantic proximity Read ↗

Deciphering the T790M/L858R-Selective Inhibition Mechanism of an Allosteric Inhibitor of EGFR: Insights from Molecular Simulations.Semantic proximity Read ↗

Uncovering the Molecular Basis for the Better Gefitinib Sensitivity of EGFR with Complex Mutations over Single Rare Mutation: Insights from Molecular Simulations.Semantic proximity Read ↗

Discovery of BLU-945, a Reversible, Potent, and Wild-Type-Sparing Next-Generation EGFR Mutant Inhibitor for Treatment-Resistant Non-Small-Cell Lung Cancer.Semantic proximity Read ↗

Epidermal growth factor receptor as a target enzyme in cancer therapy: Structural and functional insights from crystallography.Semantic proximity Read ↗

Discovery of Novel EGFR Inhibitor Targeting Wild-Type and Mutant Forms of EGFR: In Silico and In Vitro Study.Semantic proximity Read ↗

Structural and mechanistic underpinnings of the differential drug sensitivity of EGFR mutations in non-small cell lung cancer.Semantic proximity Read ↗

Challenges and Perspectives on the Development of Small-Molecule EGFR Inhibitors against T790M-Mediated Resistance in Non-Small-Cell Lung CancerSemantic proximity Read ↗

Structural signature of the G719S-T790M double mutation in the EGFR kinase domain and its response to inhibitors.Semantic proximity Read ↗

Structural Analysis of Interactions between Epidermal Growth Factor Receptor (EGFR) Mutants and Their InhibitorsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.