Creating Chemical Diversity to Target Protein Kinases

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.

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