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- W2414854025 endingPage "67" @default.
- W2414854025 startingPage "23" @default.
- W2414854025 abstract "The aberrant activation of protein kinases is associated with many human diseases, most notably cancer. Due to this link between kinase deregulation and disease progression, kinases are one of the most targeted protein families for small-molecule inhibition. Within the last 15 years, the U.S. Food and Drug Administration has approved over 20 small-molecule inhibitors of protein kinases for use in the clinic. These inhibitors target the kinase active site and represent the successful hurdling by medicinal chemists of the formidable challenge posed by the high similarity among the active sites of the approximately 500 human kinases. We review the conserved structural features of kinases that are important for inhibitor binding as well as for catalysis. Many clinically approved drugs elicit selectivity by exploiting subtle variation within the kinase active site. We highlight some of the crystallographic studies on the kinase-inhibitor complexes that have provided valuable guidance for the development of these drugs as well as for future drug design efforts." @default.
- W2414854025 created "2016-06-24" @default.
- W2414854025 creator A5015195367 @default.
- W2414854025 creator A5038330393 @default.
- W2414854025 creator A5045644512 @default.
- W2414854025 date "2014-01-01" @default.
- W2414854025 modified "2023-09-27" @default.
- W2414854025 title "A Structural Atlas of Kinases Inhibited by Clinically Approved Drugs" @default.
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