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

Link to article in PubMed

PubMed ID

30203394

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