The Chemical Biology of Reversible Lysine Post-translational Modifications.

Cell Chemical Biology
Zhipeng A Wang, Philip A Cole

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.

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Citations

Nov 6, 2020·Organic & Biomolecular Chemistry·Tianjiong YaoScott K Silverman
Jan 22, 2021·Chemical Communications : Chem Comm·Yanli JiWeimin Xuan
Mar 7, 2021·International Journal of Molecular Sciences·Claudio D'Amore, Mauro Salvi
Nov 18, 2020·Journal of Chemical Theory and Computation·Claudia ScatignoRoberto Senesi
Aug 26, 2021·Biological Chemistry·Anna-Theresa BlaslMichael Lammers
Sep 18, 2021·Briefings in Bioinformatics·Shaherin BasithBalachandran Manavalan
Sep 24, 2021·Accounts of Chemical Research·Xin Li, Xiang David Li
Sep 29, 2021·Omics : a Journal of Integrative Biology·Pratigya Subba, Thottethodi Subrahmanya Keshava Prasad
Nov 4, 2021·Drug Discovery Today·Geoffrey A HoldgateRobert Sheppard
Nov 18, 2021·Journal of the American Chemical Society·Katsuya MaruyamaMotomu Kanai

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