Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance.

@article{Schwartz2014CovalentEI,
  title={Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance.},
  author={Phillip A Schwartz and Petr Kuzmi{\vc} and James E Solowiej and Simon Bergqvist and Ben J Bola{\~n}os and Chau Doan Almaden and Asako Nagata and Kevin Ryan and Junli Feng and Deepak K. Dalvie and John Kath and Meirong Xu and Revati Wani and Brion William Murray},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2014},
  volume={111 1},
  pages={173-8}
}
Covalent inhibition is a reemerging paradigm in kinase drug design, but the roles of inhibitor binding affinity and chemical reactivity in overall potency are not well-understood. To characterize the underlying molecular processes at a microscopic level and determine the appropriate kinetic constants, specialized experimental design and advanced numerical integration of differential equations are developed. Previously uncharacterized investigational covalent drugs reported here are shown to be… CONTINUE READING

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