可逆赖氨酸翻译后修饰的化学生物学。
The Chemical Biology of Reversible Lysine Post-translational Modifications.
机构信息
Division of Genetics, Department of Medicine, Brigham and Women's Hospital and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 77 Avenue Louis Pasteur NRB, Boston, MA 02115, USA.
Division of Genetics, Department of Medicine, Brigham and Women's Hospital and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 77 Avenue Louis Pasteur NRB, Boston, MA 02115, USA.
出版信息
Cell Chem Biol. 2020 Aug 20;27(8):953-969. doi: 10.1016/j.chembiol.2020.07.002. Epub 2020 Jul 21.
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.
蛋白质中的赖氨酸（Lys）残基经历了广泛的可逆翻译后修饰（PTM），这些修饰可以调节酶活性、染色质结构、蛋白质-蛋白质相互作用、蛋白质稳定性和细胞定位。在这里，我们讨论了一些常见蛋白质 Lys PTM 的“写入器”、“擦除器”和“读取器”，并总结了它们主要生物学影响的实例。我们还回顾了化学生物学方法，从小分子探针到蛋白质化学技术，这些方法有助于描绘 Lys PTM 的功能，并为一系列广泛的生物医学应用提供了前景。
Zotero 插件