翻译后修饰
化学生物学
赖氨酸
计算生物学
染色质
生物化学
结构生物学
蛋白质结构
小分子
生物
化学
酶
氨基酸
DNA
作者
Zhipeng A. Wang,Philip A. Cole
标识
DOI:10.1016/j.chembiol.2020.07.002
摘要
Lysine (Lys) residues in proteins undergo a wide range of reversible post-translational modifications (PTMs), which can regulate enzyme activities, chromatin structure, protein-protein interactions, protein stability, and cellular localization. Here we discuss the "writers," "erasers," and "readers" of some of the common protein Lys PTMs and summarize examples of their major biological impacts. We also review chemical biology approaches, from small-molecule probes to protein chemistry technologies, that have helped to delineate Lys PTM functions and show promise for a diverse set of biomedical applications.
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