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Structural insight into the binding mechanism of ATP to EGFR and L858R, and T790M and L858R/T790 mutants.
Saldaña-Rivera L, Bello M, Méndez-Luna D. Saldaña-Rivera L, et al. J Biomol Struct Dyn. 2019 Oct;37(17):4671-4684. doi: 10.1080/07391102.2018.1558112. Epub 2019 Jan 11. J Biomol Struct Dyn. 2019. PMID: 30558477
This efficacy decreases due to drug resistance conferred by a second mutation, T790M, which subsequently produces a double mutant, L858R/T790M. ...Regrettably, detailed information at the atomic level on the origins of the increased binding affinity …
This efficacy decreases due to drug resistance conferred by a second mutation, T790M, which subsequently produces a dou …
Exploring Gatekeeper Mutations in EGFR through Computer Simulations.
Kannan S, Fox SJ, Verma CS. Kannan S, et al. J Chem Inf Model. 2019 Jun 24;59(6):2850-2858. doi: 10.1021/acs.jcim.9b00361. Epub 2019 May 30. J Chem Inf Model. 2019. PMID: 31099565
There is a clear need for rigorous methods to predict the likelihood of specific drug-resistance mutations arising in response to the binding of a drug. In this work we attempt to develop a robust computational protocol for predicting drug resis …
There is a clear need for rigorous methods to predict the likelihood of specific drug-resistance mutations arising in r …
Quantitative prediction of fold resistance for inhibitors of EGFR.
Balius TE, Rizzo RC. Balius TE, et al. Biochemistry. 2009 Sep 8;48(35):8435-48. doi: 10.1021/bi900729a. Biochemistry. 2009. PMID: 19627157 Free PMC article.
Clinical use of ATP-competitive inhibitors of the epidermal growth factor receptor (EGFR) kinase domain can lead to an acquired drug resistant mutant L858R&T790M which dramatically reduces binding affinity relative to a prevalent cancer c …
Clinical use of ATP-competitive inhibitors of the epidermal growth factor receptor (EGFR) kinase domain can lead to an …