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Imatinib, which is an inhibitor of the BCR-ABL tyrosine kinase, has been a
remarkable success for the treatment of Philadelphia chromosome-positive (Ph(+))
chronic myelogenous leukemias (CMLs). However, a significant proportion of
patients chronically treated with imatinib develop resistance because of the
acquisition of mutations in the kinase domain of BCR-ABL. Mutations occur at
residues directly implicated in imatinib binding or, more commonly, at residues
important for the ability of the kinase to adopt the specific closed (inactive)
conformation to which imatinib binds. In our quest to develop new BCR-ABL
inhibitors, we chose to target regions outside the ATP-binding site of this
enzyme because these compounds offer the potential to be unaffected by mutations
that make CML cells resistant to imatinib.
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