The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3

The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3

The NLRP3 inflammasome controls the response of the host to pathogens; precise regulation is required to limit autoimmune diseases. Here, the authors identify the E3 ligase TRIM31 that aids the ubiquitin-mediated proteasomal degradation of NLRP3, which may be a therapeutic target for alleviating dis...

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Autores principales: Hui Song, Bingyu Liu, Wanwan Huai, Zhongxia Yu, Wenwen Wang, Jing Zhao, Lihui Han, Guosheng Jiang, Lining Zhang, Chengjiang Gao, Wei Zhao
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
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Acceso en línea:https://doaj.org/article/31c893075bd949ecb0be2ccee158b0c3
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spelling oai:doaj.org-article:31c893075bd949ecb0be2ccee158b0c32021-12-02T17:33:20ZThe E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP310.1038/ncomms137272041-1723https://doaj.org/article/31c893075bd949ecb0be2ccee158b0c32016-12-01T00:00:00Zhttps://doi.org/10.1038/ncomms13727https://doaj.org/toc/2041-1723The NLRP3 inflammasome controls the response of the host to pathogens; precise regulation is required to limit autoimmune diseases. Here, the authors identify the E3 ligase TRIM31 that aids the ubiquitin-mediated proteasomal degradation of NLRP3, which may be a therapeutic target for alleviating disease.Hui SongBingyu LiuWanwan HuaiZhongxia YuWenwen WangJing ZhaoLihui HanGuosheng JiangLining ZhangChengjiang GaoWei ZhaoNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Hui Song
Bingyu Liu
Wanwan Huai
Zhongxia Yu
Wenwen Wang
Jing Zhao
Lihui Han
Guosheng Jiang
Lining Zhang
Chengjiang Gao
Wei Zhao
The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3
description The NLRP3 inflammasome controls the response of the host to pathogens; precise regulation is required to limit autoimmune diseases. Here, the authors identify the E3 ligase TRIM31 that aids the ubiquitin-mediated proteasomal degradation of NLRP3, which may be a therapeutic target for alleviating disease.
format article
author Hui Song
Bingyu Liu
Wanwan Huai
Zhongxia Yu
Wenwen Wang
Jing Zhao
Lihui Han
Guosheng Jiang
Lining Zhang
Chengjiang Gao
Wei Zhao
author_facet Hui Song
Bingyu Liu
Wanwan Huai
Zhongxia Yu
Wenwen Wang
Jing Zhao
Lihui Han
Guosheng Jiang
Lining Zhang
Chengjiang Gao
Wei Zhao
author_sort Hui Song
title The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3
title_short The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3
title_full The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3
title_fullStr The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3
title_full_unstemmed The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3
title_sort e3 ubiquitin ligase trim31 attenuates nlrp3 inflammasome activation by promoting proteasomal degradation of nlrp3
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/31c893075bd949ecb0be2ccee158b0c3
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