Detection and identification of protein citrullination in complex biological systems

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology; Program in Chemical Biology

Publication Date


Document Type



Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics


Protein citrullination is a post-translational modification of arginine that is catalyzed by the Protein Arginine Deiminase (PAD) family of enzymes. Aberrantly increased citrullination is associated with a host of inflammatory diseases and cancer and PAD inhibitors have shown remarkable efficacy in a range of diseases including rheumatoid arthritis, lupus, atherosclerosis, and ulcerative colitis. In rheumatoid arthritis, citrullinated proteins serve as key antigens for rheumatoid arthritis-associated autoantibodies. These data suggest that citrullinated proteins may serve more generally as biomarkers of specific disease states, however, the identification of citrullinated residues remains challenging due to the small 1Da mass change that occurs upon citrullination. Herein, we highlight the available techniques to identify citrullinated proteins/residues focusing on advanced MS techniques as well as chemical derivatization strategies that are currently being employed to identify citrullinated proteins as well as the specific residues modified within those proteins.

DOI of Published Version



Curr Opin Chem Biol. 2016 Feb;30:1-6. doi: 10.1016/j.cbpa.2015.10.014. Epub 2015 Oct 27.Link to article on publisher's site

Journal/Book/Conference Title

Current opinion in chemical biology

Related Resources

Link to Article in PubMed

PubMed ID