肌动蛋白解聚因子
化学
激酶
体外
小分子
体内
生物化学
磷酸化
体外毒理学
酶
细胞生物学
细胞
生物
肌动蛋白细胞骨架
细胞骨架
生物技术
作者
Ross J. Collins,Hyunah Lee,D. Heulyn Jones,J.M. Elkins,Jason A Gillespie,C. Thomas,Alex G. Baldwin,Kimberley M Jones,Loren Waters,Marie Paine,John Atack,Simon E. Ward,Olivera Grubisha,David W. Foley
标识
DOI:10.1021/acs.jmedchem.2c00751
摘要
LIM domain kinases 1 and 2 (LIMK1 and LIMK2) regulate actin dynamics and subsequently key cellular functions such as proliferation and migration. LIMK1 and LIMK2 phosphorylate and inactivate cofilin leading to increased actin polymerization. As a result, LIMK inhibitors are emerging as a promising treatment strategy for certain cancers and neurological disorders. High-quality chemical probes are required if the role of these kinases in health and disease is to be understood. To that end, we report the results of a comparative assessment of 17 reported LIMK1/2 inhibitors in a variety of in vitro enzymatic and cellular assays. Our evaluation has identified three compounds (TH-257, LIJTF500025, and LIMKi3) as potent and selective inhibitors suitable for use as in vitro and in vivo pharmacological tools for the study of LIMK function in cell biology.
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