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- W2012161142 abstract "The tyrosine specific protein kinases (TK) are a subgroup of the largest known gene family, the kinases. Latest estimates suggest that there are over 2000 kinases encoded in the human genome [1]. TKs catalyse the transfer of phosphate to the phenolic hydroxyl of tyrosine residues in substrate proteins, consequently modifying the target protein properties. By working in concert with tyrosine phosphatases, which drive the reverse process, the TKs provide a switching system resulting in the transduction of signals from cell surface receptor to the nucleus. Inappropriate activation of TKs can lead to abnormal, dysregulated cellular proliferation and many of the known oncogenes are kinases. Naturally, there has been great interest in TKs as potential molecular targets for developing drugs for the treatment of cancer and results from the first clinical trials are now being published. Preclinical research is also focused on other therapeutic applications of TK inhibitors. This review concentrates on TK inhibitors which are either already in the clinic or likely to enter Phase I studies in the near future." @default.
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- W2012161142 date "2000-10-01" @default.
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- W2012161142 title "Selective tyrosine kinase inhibitors" @default.
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- W2012161142 doi "https://doi.org/10.1517/14728214.5.3.287" @default.
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