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Protein Arginine Methylation and Citrullination in Epigenetic Regulation
[Image: see text] 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 prog...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4802296/ https://www.ncbi.nlm.nih.gov/pubmed/26686581 http://dx.doi.org/10.1021/acschembio.5b00942 |
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author | Fuhrmann, Jakob Thompson, Paul R. |
author_facet | Fuhrmann, Jakob Thompson, Paul R. |
author_sort | Fuhrmann, Jakob |
collection | PubMed |
description | [Image: see text] 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. |
format | Online Article Text |
id | pubmed-4802296 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-48022962016-03-23 Protein Arginine Methylation and Citrullination in Epigenetic Regulation Fuhrmann, Jakob Thompson, Paul R. ACS Chem Biol [Image: see text] 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. American Chemical Society 2015-12-19 2016-03-18 /pmc/articles/PMC4802296/ /pubmed/26686581 http://dx.doi.org/10.1021/acschembio.5b00942 Text en Copyright © 2015 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes. |
spellingShingle | Fuhrmann, Jakob Thompson, Paul R. Protein Arginine Methylation and Citrullination in Epigenetic Regulation |
title | Protein Arginine Methylation and Citrullination in
Epigenetic Regulation |
title_full | Protein Arginine Methylation and Citrullination in
Epigenetic Regulation |
title_fullStr | Protein Arginine Methylation and Citrullination in
Epigenetic Regulation |
title_full_unstemmed | Protein Arginine Methylation and Citrullination in
Epigenetic Regulation |
title_short | Protein Arginine Methylation and Citrullination in
Epigenetic Regulation |
title_sort | protein arginine methylation and citrullination in
epigenetic regulation |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4802296/ https://www.ncbi.nlm.nih.gov/pubmed/26686581 http://dx.doi.org/10.1021/acschembio.5b00942 |
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