Protein Arginine Methylation and Citrullination in Epigenetic Regulation | Zendy

Jakob Fuhrmann | Zendy; Paul R. Thompson | Zendy

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Protein Arginine Methylation and Citrullination in Epigenetic Regulation

Author(s) -

Jakob Fuhrmann,

Paul R. Thompson

Publication year - 2015

Publication title -

acs chemical biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.899

H-Index - 111

eISSN - 1554-8937

pISSN - 1554-8929

DOI - 10.1021/acschembio.5b00942

Subject(s) - citrullination , epigenetics , histone , epigenomics , biology , arginine , chromatin , histone code , histone modifying enzymes , regulation of gene expression , methylation , histone methylation , protein arginine methyltransferase 5 , histone methyltransferase , microbiology and biotechnology , computational biology , genetics , gene expression , dna methylation , gene , methyltransferase , nucleosome , citrulline , amino acid

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.

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