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Chemical Probes and Methods for the Study of Protein Arginine Methylation by Tyler Brown; Terry Nguyen; Bo Zhou; Y. George Zheng is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Chemical Probes and Methods for the Study of Protein Arginine Methylation about?

Protein arginine methylation is a widespread post-translational modification (PTM) in eukaryotic cells. This chemical modification in proteins functionally modulates diverse cellular processes from signal transduction, gene expression, and DNA damage repair to RNA splicing. The chemistry of arginine methylation entails the transfer of the methyl group from __S__-adenosyl-l-methionine (AdoMet, SAM) onto a guanidino nitrogen atom of an arginine residue of a target protein. This reaction is catalyzed by about 10 members of protein arginine methyltransferases (PRMTs). With impacts on a variety of cellular processes, aberrant expression and activity of PRMTs have been shown in many disease conditions. Particularly in oncology, PRMTs are commonly overexpressed in many cancerous tissues and positively correlated with tumor initiation, development and progression. As such, targeting PRMTs is increasingly recognized as an appealing therapeutic strategy for new drug discovery. In the past decade, a great deal of research efforts has been invested in illuminating PRMT functions in diseases and developing chemical probes for the mechanistic study of PRMTs in biological systems. In this review,

Who reads Chemical Probes and Methods for the Study of Protein Arginine Methylation?

Author

Tyler Brown; Terry Nguyen; Bo Zhou; Y. George Zheng

Publisher

Royal Society of Chemistry (RSC)

Published

2023

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)