Mechanism and design of allosteric activators of SIRT1

被引：0

作者：

Fei Liu ^{[1
]}

Ningning Pang ^{[1
]}

RuiMing Xu ^{[2
]}

Na Yang ^{[1
]}

机构：

[1] State Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Key Laboratory of Medical Data Analysis and Statistical Research of Tianjin, Nankai University

[2] National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of

来源：

Protein & Cell | 2023年 / 14卷 / 05期

关键词：

D O I：

暂无

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

<正>Dear Editor,The sirtuin family Nicotinamide adenine dinucleotide-dependent deacetylases have important roles in many biological processes (Milne and Denu, 2008). SIRT1 is a mammalian homolog of yeast Sir2, which is the founding member of the sirtuin family. Many SIRT1 substrates have been reported, including histones, p53, FOXOs, and PGC1α (Hsu et al., 2013).

引用

页码：387 / 392

页数：6

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