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Advances in the Study of the Ubiquitin-Editing Enzyme A20

Ubiquitin modification is a common post-translational protein modification and an important mechanism whereby the body regulates protein levels and functions. As a common enzyme associated with ubiquitin modification, the ubiquitin-editing enzyme A20 may be closely associated with the development of...

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Autores principales: Bai, Wenya, Huo, Siying, Li, Junjie, Shao, Jianlin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9110840/
https://www.ncbi.nlm.nih.gov/pubmed/35592427
http://dx.doi.org/10.3389/fphar.2022.845262
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author Bai, Wenya
Huo, Siying
Li, Junjie
Shao, Jianlin
author_facet Bai, Wenya
Huo, Siying
Li, Junjie
Shao, Jianlin
author_sort Bai, Wenya
collection PubMed
description Ubiquitin modification is a common post-translational protein modification and an important mechanism whereby the body regulates protein levels and functions. As a common enzyme associated with ubiquitin modification, the ubiquitin-editing enzyme A20 may be closely associated with the development of numerous pathological processes through its different structural domains. The aim of this paper is to provide an overview of the following: advances in ubiquitination research, the structure and function of A20, and the relationships between A20 and immune inflammatory response, apoptosis, necroptosis, pyroptosis, and autophagy.
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spelling pubmed-91108402022-05-18 Advances in the Study of the Ubiquitin-Editing Enzyme A20 Bai, Wenya Huo, Siying Li, Junjie Shao, Jianlin Front Pharmacol Pharmacology Ubiquitin modification is a common post-translational protein modification and an important mechanism whereby the body regulates protein levels and functions. As a common enzyme associated with ubiquitin modification, the ubiquitin-editing enzyme A20 may be closely associated with the development of numerous pathological processes through its different structural domains. The aim of this paper is to provide an overview of the following: advances in ubiquitination research, the structure and function of A20, and the relationships between A20 and immune inflammatory response, apoptosis, necroptosis, pyroptosis, and autophagy. Frontiers Media S.A. 2022-05-03 /pmc/articles/PMC9110840/ /pubmed/35592427 http://dx.doi.org/10.3389/fphar.2022.845262 Text en Copyright © 2022 Bai, Huo, Li and Shao. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Pharmacology
Bai, Wenya
Huo, Siying
Li, Junjie
Shao, Jianlin
Advances in the Study of the Ubiquitin-Editing Enzyme A20
title Advances in the Study of the Ubiquitin-Editing Enzyme A20
title_full Advances in the Study of the Ubiquitin-Editing Enzyme A20
title_fullStr Advances in the Study of the Ubiquitin-Editing Enzyme A20
title_full_unstemmed Advances in the Study of the Ubiquitin-Editing Enzyme A20
title_short Advances in the Study of the Ubiquitin-Editing Enzyme A20
title_sort advances in the study of the ubiquitin-editing enzyme a20
topic Pharmacology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9110840/
https://www.ncbi.nlm.nih.gov/pubmed/35592427
http://dx.doi.org/10.3389/fphar.2022.845262
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