The structure of Dasatinib (BMS-354825) bound to activated ABL kinase domain elucidates its inhibitory activity against imatinib-resistant ABL mutants.
By J. Tokarski, J. Newitt, Chiehying Y Chang, Janet D. Cheng, M. Wittekind, S. Kiefer, K. Kish, F. Lee, Robert Borzillerri, L. Lombardo and 3 more. Cancer Research, 2006
660 citations recorded by the source corpus.
Subfields: Genetics, Hematology, Rheumatology
View Paper: https://www.semanticscholar.org/paper/78932c0cbd4ec22b0dab64397f172cf552e32855
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Citations in the corpus
- Second generation inhibitors of BCR-ABL for the treatment of imatinib-resistant chronic myeloid leukaemia (2007, background): “The lack of selectivity over the Src-family kinases is probably related to the fact that dasatinib, in contrast to both imatinib and nilotinib, inhibits BCR-ABL by binding to the active conformation of the ABL kinase domain, which is similar for ABL and the Src kinase”
- Chronic Myeloid Leukemia (2007, positive): “It is about 325-fold more potent than imatinib 46 .”
- AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance. (2009, background): “Modeling analysis indicates that the mutation eliminates a critical hydrogen bonding interaction required for high-affinity binding of imatinib, nilotinib, and dasatinib and alters the topology of the ATP-binding pocket (Tokarski et al., 2006; Weisberg et al., 2005).”