Abstract
Protein kinases play crucial roles in regulating virtually every cellular process and are currently attracting tremendous interest as drug targets from the pharmaceutical industry. The major challenges facing the development of the potential kinase inhibitor drugs are: selectivity, physical properties (solubility, molecular weight), and pharmacological properties (bioavailability, half life, toxicity, etc.) This review focuses on how selective protein kinase inhibitors that target the ATP and allosteric binding sites are currently being identified and optimized.
Keywords: kinase inhibitors, protein kinases, protein phosphorylation, signal transduction, kinase-targeted libraries, anticancer drugs, anti-inflammatory drugs
Combinatorial Chemistry & High Throughput Screening
Title: Creating Chemical Diversity to Target Protein Kinases
Volume: 7 Issue: 5
Author(s): B. Li, Y. Liu, T. Uno and N. Gray
Affiliation:
Keywords: kinase inhibitors, protein kinases, protein phosphorylation, signal transduction, kinase-targeted libraries, anticancer drugs, anti-inflammatory drugs
Abstract: Protein kinases play crucial roles in regulating virtually every cellular process and are currently attracting tremendous interest as drug targets from the pharmaceutical industry. The major challenges facing the development of the potential kinase inhibitor drugs are: selectivity, physical properties (solubility, molecular weight), and pharmacological properties (bioavailability, half life, toxicity, etc.) This review focuses on how selective protein kinase inhibitors that target the ATP and allosteric binding sites are currently being identified and optimized.
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Cite this article as:
Li B., Liu Y., Uno T. and Gray N., Creating Chemical Diversity to Target Protein Kinases, Combinatorial Chemistry & High Throughput Screening 2004; 7 (5) . https://dx.doi.org/10.2174/1386207043328580
DOI https://dx.doi.org/10.2174/1386207043328580 |
Print ISSN 1386-2073 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5402 |
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