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Creating chemical diversity to target protein kinases.

Li, Bing and Liu, Y and Uno, Tetsuo and Gray, Nathanael (2004) Creating chemical diversity to target protein kinases. Combinatorial Chemistry & High Throughput Screening, 7 (5). pp. 453-472. ISSN 1386-2073

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.

Item Type: Article
Related URLs:
Additional Information: author can archive post-print (ie final draft post-refereeing); Publisher's version/PDF cannot be used
Keywords: kinase inhibitors, protein kinases, protein phosphorylation, signal transduction, kinase-targeted libraries, anticancer drugs, anti-inflammatory drugs
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Date Deposited: 14 Dec 2009 14:02
Last Modified: 31 Jan 2013 01:22
URI: https://oak.novartis.com/id/eprint/268

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