![]() ![]() Post-translational modifications of histone and non-histone proteins include covalent changes taking place on the amino acid side chain leading to the addition of a chemical group, such as acetyl, methyl, phosphoryl, glycosyl, which significantly change the properties of a protein, its conformation, localization and stability, and help to diversify the protein’s functionalities. Finally, developments on inhibitors against protein citrullination and recent clinical trials providing a promising therapeutic approach to inflammatory disease by targeting citrullination are discussed. Here, we will discuss the biochemical nature of arginine citrullination, the enzymatic machinery behind it and also provide information on the pathological consequences of citrullination in the development of inflammatory diseases (rheumatoid arthritis, multiple sclerosis, psoriasis, systemic lupus erythematosus, periodontitis and COVID-19), cancer and thromboembolism. Accumulating evidence suggest that citrullination plays a significant role in regulating cellular metabolism and gene expression by affecting a multitude of pathways and modulating the chromatin status. The process of citrullination is catalysed by peptidylarginine deiminases (PADs), a family of conserved enzymes expressed in a variety of human tissues. A less explored protein PTM, conversion of peptidylarginine to citrulline, is the subject of this review. The action of the most prevalent PTMs, encompassing phosphorylation, methylation, acylations, ubiquitination and glycosylation is well documented. Post-translational modifications (PTMs) govern the collective metabolism of a cell through altering the structure and functions of proteins. ![]()
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