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• W2316153640 abstract "Modern molecular technology helped identify more than 10 protein tyrosine kinases related to myeloid malignancies, which allowed the development of small molecule inhibitors targeting deregulated protein tyrosine kinase activity. Protein tyrosine kinase deregulation can occur as a consequence of fusion gene formation because of chromosomal translocations, or as distinct gain-of-function point mutations. Although the tyrosine kinase inhibitor imatinib mesylate (Gleevec) targeting the ABL protein tyrosine kinase has revolutionized current chronic myeloid leukemia therapy, it became rapidly evident that overcoming the multiple cellular resistance mechanisms will be very challenging. To develop efficient therapeutic alternatives, one must understand the complex signal transduction mechanisms involved in transformation by deregulated protein tyrosine kinases. This article reviews the most recently identified molecular mechanisms involved in cell transformation by the BCR/ABL protein tyrosine kinase fusion and presents new members of the increasing family of deregulated protein tyrosine kinases involved in myeloproliferative disorders. In addition, the article discusses new, promising small molecule protein tyrosine kinase inhibitors and the molecular mechanism that may lead to resistance to these drugs. Finally, the article highlights putative alternative strategies that could be used to block signal transduction pathways of deregulated protein tyrosine kinase activity." @default.
• W2316153640 created "2016-06-24" @default.
• W2316153640 creator A5030763668 @default.
• W2316153640 creator A5091167223 @default.
• W2316153640 date "2003-01-01" @default.
• W2316153640 modified "2023-09-23" @default.
• W2316153640 title "Role of constitutively activated protein tyrosine kinases in malignant myeloproliferative disorders: an update" @default.
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• W2316153640 doi "https://doi.org/10.1097/00062752-200301000-00007" @default.
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• W2316153640 hasPublicationYear "2003" @default.
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