The Chemical Biology of Reversible Lysine Post-translational Modifications

被引：103
|
作者：
Wang, Zhipeng A. [1 ,2 ]
Colel, Philip A. [1 ,2 ]
机构：
[1] Harvard Med Sch, Brigham & Womens Hosp, Dept Med, Div Genet, 77 Ave Louis Pasteur NRB, Boston, MA 02115 USA
[2] Harvard Med Sch, Dept Biol Chem & Mol Pharmacol, 77 Ave Louis Pasteur NRB, Boston, MA 02115 USA
来源：
CELL CHEMICAL BIOLOGY | 2020年 / 27卷 / 08期
关键词：
SITE-SPECIFIC INSTALLATION; SMALL-MOLECULE INHIBITOR; BINDING-PROTEIN; HISTONE DEMETHYLATION; SELECTIVE-INHIBITION; GENETIC-CODE; DOMAIN; BROMODOMAIN; DEACETYLASE; CHROMATIN;
D O I：
10.1016/j.chembiol.2020.07.002
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
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.
引用
收藏
页码：953 / 969
页数：17
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