Development of Activity-Based Proteomic Probes for Protein Citrullination

被引：9
|
作者：
Nemmara, Venkatesh V. [1 ,2 ]
Thompson, Paul R. [1 ,2 ]
机构：
[1] Univ Massachusetts, Sch Med, Dept Biochem & Mol Pharmacol, LRB 826,364 Plantat St, Worcester, MA 01605 USA
[2] Univ Massachusetts, Sch Med, Program Chem Biol, LRB 826,364 Plantat St, Worcester, MA 01605 USA
来源：
ACTIVITY-BASED PROTEIN PROFILING | 2019年 / 420卷
关键词：
ARGININE DEIMINASE 4; SCRAPIE-INFECTED MICE; PEPTIDYLARGININE DEIMINASE; PROTEIN-ARGININE-DEIMINASE-4; PAD4; STRUCTURAL BASIS; CL-AMIDINE; IN-VITRO; INHIBITION; ACID; HALOACETAMIDINE;
D O I：
10.1007/82_2018_132
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：
Protein arginine deiminases (PADs) catalyze the post-translational deimination of peptidyl arginine to form peptidyl citrulline. This modification is increased in multiple inflammatory diseases and in certain cancers. PADs regulate a variety of signaling pathways including apoptosis, terminal differentiation, and transcriptional regulation. Activity-based protein profiling (ABPP) probes have been developed to understand the role of the PADs in vivo and to investigate the effect of protein citrullination in various pathological conditions. Furthermore, these ABPPs have been utilized as a platform for high-throughput inhibitor discovery. This review will showcase the development of ABPPs targeting the PADs. In addition, it provides a brief overview of PAD structure and function along with recent advances in PAD inhibitor development.
引用
收藏
页码：233 / 251
页数：19
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