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Deubiquitination in virus infection
Post-translational modification of proteins and peptides by ubiquitin, a highly evolutionarily conserved 76 residue protein, and ubiquitin-like modifiers has emerged as a major regulatory mechanism in various cellular activities. Eukaryotic viruses are known to modulate protein ubiquitination to the...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Published by Elsevier Inc.
2007
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103280/ https://www.ncbi.nlm.nih.gov/pubmed/17291557 http://dx.doi.org/10.1016/j.virol.2006.12.035 |
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author | Lindner, Holger A. |
author_facet | Lindner, Holger A. |
author_sort | Lindner, Holger A. |
collection | PubMed |
description | Post-translational modification of proteins and peptides by ubiquitin, a highly evolutionarily conserved 76 residue protein, and ubiquitin-like modifiers has emerged as a major regulatory mechanism in various cellular activities. Eukaryotic viruses are known to modulate protein ubiquitination to their advantage in various ways. At the same time, the evidence for the importance of deubiquitination as a viral target also is growing. This review centers on known viral interactions with protein deubiquitination, on viral enzymes for which deubiquitinating activities were recently demonstrated, and on the roles of viral ubiquitin-like sequences. |
format | Online Article Text |
id | pubmed-7103280 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Published by Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71032802020-03-31 Deubiquitination in virus infection Lindner, Holger A. Virology Article Post-translational modification of proteins and peptides by ubiquitin, a highly evolutionarily conserved 76 residue protein, and ubiquitin-like modifiers has emerged as a major regulatory mechanism in various cellular activities. Eukaryotic viruses are known to modulate protein ubiquitination to their advantage in various ways. At the same time, the evidence for the importance of deubiquitination as a viral target also is growing. This review centers on known viral interactions with protein deubiquitination, on viral enzymes for which deubiquitinating activities were recently demonstrated, and on the roles of viral ubiquitin-like sequences. Published by Elsevier Inc. 2007-06-05 2007-02-07 /pmc/articles/PMC7103280/ /pubmed/17291557 http://dx.doi.org/10.1016/j.virol.2006.12.035 Text en Crown copyright © 2007 Published by Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Lindner, Holger A. Deubiquitination in virus infection |
title | Deubiquitination in virus infection |
title_full | Deubiquitination in virus infection |
title_fullStr | Deubiquitination in virus infection |
title_full_unstemmed | Deubiquitination in virus infection |
title_short | Deubiquitination in virus infection |
title_sort | deubiquitination in virus infection |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103280/ https://www.ncbi.nlm.nih.gov/pubmed/17291557 http://dx.doi.org/10.1016/j.virol.2006.12.035 |
work_keys_str_mv | AT lindnerholgera deubiquitinationinvirusinfection |