scholarly journals EGFR tyrosine kinase mutation testing in the treatment of non-small-cell lung cancer

2012 ◽  
Vol 19 (2) ◽  
Author(s):  
S. Kamel-Reid ◽  
G. Chong ◽  
D.N. Ionescu ◽  
A.M. Magliocco ◽  
A. Spatz ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Tyrosine Kinase ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Mutation Testing ◽  
Small Cell ◽  
Small Cell Lung ◽  
Egfr Tyrosine Kinase ◽  
Kinase Mutation

EGFR tyrosine kinase inhibitors in the treatment of advanced non-small cell lung cancer

2008 ◽  
Vol 26 (15_suppl) ◽  
pp. 19117-19117
Author(s):  
D. M. Kowalski ◽  
M. Krzakowski ◽  
P. Jaskiewicz ◽  
A. Janowicz-Zebrowska ◽  
M. Glogowski
Keyword(s):  
Lung Cancer ◽  
Tyrosine Kinase ◽  
Small Cell Lung Cancer ◽  
Tyrosine Kinase Inhibitors ◽  
Cell Lung Cancer ◽  
Kinase Inhibitors ◽  
Small Cell ◽  
Small Cell Lung ◽  
Egfr Tyrosine Kinase ◽  
Egfr Tyrosine Kinase Inhibitors

scholarly journals Primary Erlotinib Resistance in a Patient with Non-Small Cell Lung Cancer Carrying Simultaneous Compound EGFR L718A, Q849H, and L858R Mutations

2021 ◽  
Vol 12 (1) ◽  
pp. 164-174
Author(s):  
Hanifeh Mirtavoos-mahyari ◽  
Elham Rismani ◽  
Alireza Sarkar Lotfabadi ◽  
Azizollah Abbasi Dezfouli ◽  
Kambiz Sheikhy ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Tyrosine Kinase ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Kinase Domain ◽  
Small Cell ◽  
Dynamics Simulation ◽  
Egfr Mutations ◽  
Small Cell Lung ◽  
Egfr Tyrosine Kinase

Abstract Nowadays, mutations in the epidermal growth factor receptor (EGFR) kinase domain are studied in targeted therapy of non-small cell lung cancer (NSCLC) with EGFR tyrosine kinase inhibitors including gefitinib and erlotinib. The present study reports a rare case of a patient harboring three simultaneous EGFR mutations (L718A, Q849H, and L858R). The development of erlotinib resistance was detected in the subsequent treatment. Using a computational approach, the current study investigated the conformational changes of wild-type and mutant EGFR's kinase domains in the interaction with erlotinib. Their binding modes with erlotinib were elucidated during molecular dynamics simulation, where higher fluctuations were detected in the mutated forms of the EGFR tyrosine kinase domain. Prediction of stability and functional effect of mutations revealed that amino acidic substitutions have decreased the protein stability as well as the binding affinity to erlotinib. These results may be useful for a recommendation of EGFR mutational analysis for patients with NSCLC carcinoma.

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