The selective inhibition of phosphatases by natural toxins: The anhydride domain of tautomycin is not a primary factor in controlling PP1/PP2A selectivity
The selective inhibition of phosphatases by natural toxins: The anhydride domain of tautomycin is not a primary factor in controlling PP1/PP2A selectivity
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DOI：
10.1016/s0960-894x(03)00105-7
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发表时间：
2003-05-05
影响因子：
2.7
通讯作者：
Chamberlin, AR
中科院分区：
文献类型：
--
作者：
Liu, W;Sheppeck, JE;Chamberlin, AR
在C1 ′-C7 ′酸酐部分进行修饰，制备了有效的和中等选择性的PP 1/PP 2A抑制剂互变霉素（TM）的类似物。虽然所有保留不同程度的活性在3000倍的效力范围内，他们也显示出显着的恒定性，在其IC 50比，这表明酸酐部分不是关键的控制抑制的选择性。(C)2003爱思唯尔科技有限公司版权所有。
Analogues of the potent and moderately selective PP1/PP2A inhibitor tautomycin (TM) were prepared with modifications in the C1'-C7' anhydride moiety. While all retain varying degrees of activity within a 3000-fold range of potencies, they also show remarkable constancy in their IC50 ratios, suggesting that the anhydride moiety is not critical in controlling the selectivity of inhibition. (C) 2003 Elsevier Science Ltd. All rights reserved.