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Life and destruction: ubiquitin-mediated proteolysis in aging and longevity
The ubiquitin/proteasome system (UPS) regulates the turnover of improperly folded and damaged proteins to maintain protein homeostasis (proteostasis), cellular function, and viability. It is commonly thought that an age-related impairment of the UPS affects general proteostasis networks, which cause...
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Formato: | Texto |
Lenguaje: | English |
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Faculty of 1000 Ltd
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2998811/ https://www.ncbi.nlm.nih.gov/pubmed/21151840 http://dx.doi.org/10.3410/B2-79 |
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author | Hoppe, Thorsten |
author_facet | Hoppe, Thorsten |
author_sort | Hoppe, Thorsten |
collection | PubMed |
description | The ubiquitin/proteasome system (UPS) regulates the turnover of improperly folded and damaged proteins to maintain protein homeostasis (proteostasis), cellular function, and viability. It is commonly thought that an age-related impairment of the UPS affects general proteostasis networks, which causes enhanced protein aggregation and contributes to normal aging. Recent studies identified the existence of ubiquitin-dependent degradation pathways that specifically control lifespan regulators, suggesting additional roles for ubiquitylation in aging and longevity. |
format | Text |
id | pubmed-2998811 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Faculty of 1000 Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-29988112010-12-10 Life and destruction: ubiquitin-mediated proteolysis in aging and longevity Hoppe, Thorsten F1000 Biol Rep Review Article The ubiquitin/proteasome system (UPS) regulates the turnover of improperly folded and damaged proteins to maintain protein homeostasis (proteostasis), cellular function, and viability. It is commonly thought that an age-related impairment of the UPS affects general proteostasis networks, which causes enhanced protein aggregation and contributes to normal aging. Recent studies identified the existence of ubiquitin-dependent degradation pathways that specifically control lifespan regulators, suggesting additional roles for ubiquitylation in aging and longevity. Faculty of 1000 Ltd 2010-11-11 /pmc/articles/PMC2998811/ /pubmed/21151840 http://dx.doi.org/10.3410/B2-79 Text en © 2010 Faculty of 1000 Ltd http://creativecommons.org/licenses/by-nc/3.0/legalcode This is an open-access article distributed under the terms of the Creative Commons Attribution-Non Commercial License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. You may not use this work for commercial purposes |
spellingShingle | Review Article Hoppe, Thorsten Life and destruction: ubiquitin-mediated proteolysis in aging and longevity |
title | Life and destruction: ubiquitin-mediated proteolysis in aging and longevity |
title_full | Life and destruction: ubiquitin-mediated proteolysis in aging and longevity |
title_fullStr | Life and destruction: ubiquitin-mediated proteolysis in aging and longevity |
title_full_unstemmed | Life and destruction: ubiquitin-mediated proteolysis in aging and longevity |
title_short | Life and destruction: ubiquitin-mediated proteolysis in aging and longevity |
title_sort | life and destruction: ubiquitin-mediated proteolysis in aging and longevity |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2998811/ https://www.ncbi.nlm.nih.gov/pubmed/21151840 http://dx.doi.org/10.3410/B2-79 |
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