Chemical biology of protein citrullination by the protein A arginine deiminases
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Thompson, Paul R
UMass Chan AffiliationsThompson Lab
Program in Chemical Biology
Department of Biochemistry and Molecular Pharmacology
Document TypeJournal Article
KeywordsActivity-based protein profiling
Protein arginine deiminase (PAD)
Amino Acids, Peptides, and Proteins
Enzymes and Coenzymes
MetadataShow full item record
AbstractCitrullination is a post-translational modification (PTM) that converts peptidyl-arginine into peptidyl-citrulline; citrullination is catalyzed by the protein arginine deiminases (PADs). This PTM is associated with several physiological processes, including the epigenetic regulation of gene expression, neutrophil extracellular trap formation, and DNA-damage induced apoptosis. Notably, aberrant protein citrullination is relevant to several autoimmune and neurodegenerative diseases and certain forms of cancer. As such, the PADs are promising therapeutic targets. In this review, we discuss recent advances in the development of PAD inhibitors and activity-based probes, the development and use of citrulline-specific probes in chemoproteomic applications, and methods to site-specifically incorporate citrulline into proteins.
Mondal S, Thompson PR. Chemical biology of protein citrullination by the protein A arginine deiminases. Curr Opin Chem Biol. 2021 Mar 3;63:19-27. doi: 10.1016/j.cbpa.2021.01.010. Epub ahead of print. PMID: 33676233. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/29786
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