دورية أكاديمية
Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance.
العنوان: | Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance. |
---|---|
المؤلفون: | Schwartz, Phillip A., Kuzmic, Petr, Solowiej, James, Bergqvist, Simon, Bolanos, Ben, Chau Almaden, Asako Nagata, Ryan, Kevin, Junli Feng, Dalvie, Deepak, Kath, John C., Meirong Xu, Wani, Revati, William Murray, Brion |
المصدر: | Proceedings of the National Academy of Sciences of the United States of America; 1/7/2014, Vol. 111 Issue 1, p173-178, 6p |
مصطلحات موضوعية: | DRUG resistance, MATHEMATICAL models, CHEMICAL reactions, CATALYSIS, ENZYME metabolism, DIFFERENTIAL equations |
مستخلص: | 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 extremely effective epidermal growth factor receptor (EGFR) inhibitors (k |
Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
قاعدة البيانات: | Complementary Index |
كن أول من يترك تعليقا!