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

Impact of EGFR point mutations on the sensitivity to gefitinib: Insights from comparative structural analyses and molecular dynamics simulations

22 Aug 2006

Abstract excerpt

Emergence of resistant mutations in drug targets represents a serious problem in the targeted chemotherapy. One challenging issue is to understand the atomic-detailed effect of the mutation on the target. Another intriguing issue is how to predict specific mutations that would show up in the clinical setting, leading to drug resistance. By computational approaches, we have investigated structural, dynamics and...

Read the complete abstract on PubMed

Topics

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

Share to Cancer therapeutics and mechanisms
Share to Lung Cancer Treatments and Mutations
Share to Quinazolinone synthesis and applications

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

Source

Identifiers

PMID: 16927343
DOI: 10.1002/prot.21111

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Impact of EGFR point mutations on the sensitivity to gefitinib: Insights from comparative structural analyses and molecular dynamics simulationsPMID 16927343Read ↗

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

Investigation of molecular mechanism leading to gefitinib and osimertinib resistance against EGFR tyrosine kinase: molecular dynamics and binding free energy calculation.Semantic proximity Read ↗

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

Chemotherapy Drug Response to the L858R-induced Conformational Change of EGFR Activation Loop in Lung Cancer.Semantic proximity Read ↗

Structural dynamics and kinase inhibitory activity of three generations of tyrosine kinase inhibitors against wild-type, L858R/T790M, and L858R/T790M/C797S forms of EGFR.Semantic proximity Read ↗

Primary Erlotinib Resistance in a Patient with Non-Small Cell Lung Cancer Carrying Simultaneous Compound EGFR L718A, Q849H, and L858R Mutations.Semantic proximity Read ↗

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

Computational Prediction of Resistance Induced Alanine-Mutation in ATP Site of Epidermal Growth Factor Receptor.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 ↗

Gefitinib derivatives and drug-resistance: A perspective from molecular dynamics simulations.Semantic proximity Read ↗

Deciphering mechanisms of acquired T790M mutation after EGFR inhibitors for NSCLC by computational simulationsSemantic proximity Read ↗

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