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The BCR-ABL tyrosine kinase is a fusion protein resulting from a reciprocal translocation between chromosomes 9 and 22, creating what is known as the Philadelphia chromosome. This genetic abnormality leads to the fusion of the BCR and ABL1 genes, producing a constitutively active tyrosine kinase that drives the development of chronic myelogenous leukemia. The protein functions as a non-receptor tyrosine kinase that phosphorylates various substrate proteins, activating multiple signaling pathways that promote cell proliferation and survival. The development of tyrosine kinase inhibitors targeting BCR-ABL has revolutionized the treatment of CML, transforming it from a fatal disease to a manageable chronic condition for many patients.
Tyrosine kinase inhibition, ATP-competitive binding, Inhibition of BCR-ABL autophosphorylation
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