Development of activity-based proteomic probes for protein citrullination

Venkatesh V. Nemmara, Paul R. Thompson

Research output: Chapter in Book/Report/Conference proceedingChapter

5 Scopus citations

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.

Original languageEnglish (US)
Title of host publicationCurrent Topics in Microbiology and Immunology
PublisherSpringer Verlag
Pages233-251
Number of pages19
DOIs
StatePublished - 2019
Externally publishedYes

Publication series

NameCurrent Topics in Microbiology and Immunology
Volume420
ISSN (Print)0070-217X
ISSN (Electronic)2196-9965

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Microbiology
  • Immunology
  • Microbiology (medical)

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