Structure-based optimization of click-based histone deacetylase inhibitors

DOI: 10.1016/j.ejmech.2011.04.027

Source and publish data:

European Journal of Medicinal Chemistry p. 3190 - 3200 (2011)

Update date:2022-07-29

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Authors:

Hou, Jingli

Feng, Congran

Li, Zhonghua

Fang, Qinghong

Wang, Huihui

Gu, Guoxian

Shi, Yikang

Liu, Pi Liu, Pi

Xu, Feng

Yin, Zheng

Shen, Jie

Wang, Peng

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Article abstract of DOI:10.1016/j.ejmech.2011.04.027

Previously, we reported a click-chemistry based approach to the synthesis of a novel class of histone deacetylase (HDAC) inhibitors [1]. The lead compound NSC746457 was found to be as potent as SAHA (Vorinostat). Further optimization of NSC746457 by using

Full text of DOI:10.1016/j.ejmech.2011.04.027

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