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The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series
Poly(ADP-ribosyl)ation is a post-translational modification of proteins that is mediated by poly(ADP-ribose) polymerases (PARPs). Although the existence and nature of the nucleic acid-like molecule poly(ADP-ribose) (PAR) has been known for 40 years, understanding its biological functions—originally...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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Nature Publishing Group
2008
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2581850/ https://www.ncbi.nlm.nih.gov/pubmed/18927583 http://dx.doi.org/10.1038/embor.2008.191 |
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author | Hakmé, Antoinette Wong, Heng-Kuan Dantzer, Françoise Schreiber, Valérie |
author_facet | Hakmé, Antoinette Wong, Heng-Kuan Dantzer, Françoise Schreiber, Valérie |
author_sort | Hakmé, Antoinette |
collection | PubMed |
description | Poly(ADP-ribosyl)ation is a post-translational modification of proteins that is mediated by poly(ADP-ribose) polymerases (PARPs). Although the existence and nature of the nucleic acid-like molecule poly(ADP-ribose) (PAR) has been known for 40 years, understanding its biological functions—originally thought to be only the regulation of chromatin superstructure when DNA is broken—is still the subject of intense research. Here, we review the mechanisms controlling the biosynthesis of this complex macromolecule and some of its main biological functions, with an emphasis on the most recent advances and hypotheses that have developed in this rapidly growing field. |
format | Text |
id | pubmed-2581850 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-25818502009-11-01 The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series Hakmé, Antoinette Wong, Heng-Kuan Dantzer, Françoise Schreiber, Valérie EMBO Rep Review Article Poly(ADP-ribosyl)ation is a post-translational modification of proteins that is mediated by poly(ADP-ribose) polymerases (PARPs). Although the existence and nature of the nucleic acid-like molecule poly(ADP-ribose) (PAR) has been known for 40 years, understanding its biological functions—originally thought to be only the regulation of chromatin superstructure when DNA is broken—is still the subject of intense research. Here, we review the mechanisms controlling the biosynthesis of this complex macromolecule and some of its main biological functions, with an emphasis on the most recent advances and hypotheses that have developed in this rapidly growing field. Nature Publishing Group 2008-11 2008-10-17 /pmc/articles/PMC2581850/ /pubmed/18927583 http://dx.doi.org/10.1038/embor.2008.191 Text en Copyright © 2008, European Molecular Biology Organization |
spellingShingle | Review Article Hakmé, Antoinette Wong, Heng-Kuan Dantzer, Françoise Schreiber, Valérie The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series |
title | The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series |
title_full | The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series |
title_fullStr | The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series |
title_full_unstemmed | The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series |
title_short | The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series |
title_sort | expanding field of poly(adp-ribosyl)ation reactions. ‘protein modifications: beyond the usual suspects' review series |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2581850/ https://www.ncbi.nlm.nih.gov/pubmed/18927583 http://dx.doi.org/10.1038/embor.2008.191 |
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