Creating chemical diversity to target protein kinases
Creating chemical diversity to target protein kinases
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DOI：
10.2174/1386207043328580
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发表时间：
2004-08-01
影响因子：
1.8
通讯作者：
Gray, N
中科院分区：
文献类型：
--
作者：
Li, B;Liu, Y;Gray, N
蛋白激酶在调节几乎每个细胞过程中发挥着至关重要的作用，目前作为制药行业的药物靶标引起了极大的兴趣。潜在激酶抑制剂药物开发面临的主要挑战是：选择性、物理性质（溶解度、分子量）和药理学性质（生物利用度、半衰期、毒性等）。本综述重点关注目前如何识别和优化针对 ATP 和变构结合位点的选择性蛋白激酶抑制剂。
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.