UMMS Affiliation
Department of Biochemistry and Molecular Pharmacology; Program in Chemical Biology
Publication Date
2016-03-18
Document Type
Article
Disciplines
Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics
Abstract
The post-translational modification of arginine residues represents a key mechanism for the epigenetic control of gene expression. Aberrant levels of histone arginine modifications have been linked to the development of several diseases including cancer. In recent years, great progress has been made in understanding the physiological role of individual arginine modifications and their effects on chromatin function. The present review aims to summarize the structural and functional aspects of histone arginine modifying enzymes and their impact on gene transcription. We will discuss the potential for targeting these proteins with small molecules in a variety of disease states.
Rights and Permissions
This is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
DOI of Published Version
10.1021/acschembio.5b00942
Source
ACS Chem Biol. 2016 Mar 18;11(3):654-68. doi: 10.1021/acschembio.5b00942. Epub 2015 Dec 31. Link to article on publisher's site
Journal/Book/Conference Title
ACS chemical biology
Related Resources
PubMed ID
26686581
Repository Citation
Fuhrmann, Jakob and Thompson, Paul R., "Protein Arginine Methylation and Citrullination in Epigenetic Regulation" (2016). Thompson Lab Publications. 106.
https://escholarship.umassmed.edu/thompson/106
Included in
Biochemistry Commons, Enzymes and Coenzymes Commons, Medicinal-Pharmaceutical Chemistry Commons, Therapeutics Commons