Isoform selective inhibition of STAT1 or STAT3 homo-dimerization via peptidomimetic probes: Structural recognition of STAT SH2 domains
Isoform selective inhibition of STAT1 or STAT3 homo-dimerization via peptidomimetic probes: Structural recognition of STAT SH2 domains
复制标题
DOI：
10.1016/j.bmcl.2007.01.077
复制
发表时间：
2007-04-01
影响因子：
2.7
通讯作者：
Hamilton, Andrew D.
中科院分区：
文献类型：
--
作者：
Gunning, Patrick T.;Katt, William P.;Hamilton, Andrew D.
在异常细胞信号传导途径中组成型激活的STAT（信号转导和转录激活因子）蛋白的鉴定已经导致针对与致癌直接相关的特定STAT同种型的选择性破坏的研究。我们已经通过设计拟肽抑制剂文库鉴定了在低微摩尔浓度下选择性破坏STAT1或STAT3同源二聚化的试剂。ISS 840对STAT 1同源二聚化的抑制作用（IC50值为31 μ M）是对STAT 3的抑制作用（IC50值为560 μ M）的20倍。(c)2007爱思唯尔有限公司出版
The identification of constitutively activated STAT (Signal Transducers and Activators of Transcription) proteins in aberrant cell signaling pathways has led to investigations targeting the selective disruption of specific STAT isoforms directly associated with oncogenisis. We have identified, through the design of a library of peptidomimetic inhibitors, agents that selectively disrupt STAT1 or STAT3 homo-dimerization at low micromolar concentrations. ISS840 has 20-fold higher inhibition of STAT1 homo-dimerization (IC50 value of 31 mu M) relative to STAT3 (IC50 value of 560 mu M). (c) 2007 Published by Elsevier Ltd.