| Literature DB >> 32698016 |
Zhipeng A Wang1, Philip A Cole2.
Abstract
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.Entities:
Keywords: acetylation; acetyltransferase; bromodomain; deacetylase; enzyme; methylation; ubiquitination
Mesh:
Substances:
Year: 2020 PMID: 32698016 PMCID: PMC7487139 DOI: 10.1016/j.chembiol.2020.07.002
Source DB: PubMed Journal: Cell Chem Biol ISSN: 2451-9448 Impact factor: 8.116