Title
Development of Activity-Based Proteomic Probes for Protein Citrullination.
UMMS Affiliation
Thompson Lab; Department of Biochemistry and Molecular Pharmacology; Program in Chemical Biology
Publication Date
2018-09-11
Document Type
Article
Disciplines
Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry
Abstract
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.
DOI of Published Version
10.1007/82_2018_132
Source
Curr Top Microbiol Immunol. 2018 Sep 11. doi: 10.1007/82_2018_132. [Epub ahead of print]
Journal/Book/Conference Title
Current topics in microbiology and immunology
Related Resources
PubMed ID
30203394
Repository Citation
Nemmara, Venkatesh V. and Thompson, Paul R., "Development of Activity-Based Proteomic Probes for Protein Citrullination." (2018). University of Massachusetts Medical School Publications. 12.
https://escholarship.umassmed.edu/publications/12