Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis

RIPK1 integrates signals that drive both NF-κB activation and cell death pathways. Here Zhang et al. generate RIPK1 knock-in mice lacking a major ubiquitination site and demonstrate that this modification is important to suppress cell death during embryogenesis and inflammation postnatally.

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Autores principales:	Xixi Zhang, Haiwei Zhang, Chengxian Xu, Xiaoming Li, Ming Li, Xiaoxia Wu, Wenjuan Pu, Bin Zhou, Haikun Wang, Dali Li, Qiurong Ding, Hao Ying, Hui Wang, Haibing Zhang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/7a20ff8bd8654fe78c8cee847d1dc433
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spelling	oai:doaj.org-article:7a20ff8bd8654fe78c8cee847d1dc4332021-12-02T15:35:11ZUbiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis10.1038/s41467-019-11839-w2041-1723https://doaj.org/article/7a20ff8bd8654fe78c8cee847d1dc4332019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11839-whttps://doaj.org/toc/2041-1723RIPK1 integrates signals that drive both NF-κB activation and cell death pathways. Here Zhang et al. generate RIPK1 knock-in mice lacking a major ubiquitination site and demonstrate that this modification is important to suppress cell death during embryogenesis and inflammation postnatally.Xixi ZhangHaiwei ZhangChengxian XuXiaoming LiMing LiXiaoxia WuWenjuan PuBin ZhouHaikun WangDali LiQiurong DingHao YingHui WangHaibing ZhangNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Xixi Zhang Haiwei Zhang Chengxian Xu Xiaoming Li Ming Li Xiaoxia Wu Wenjuan Pu Bin Zhou Haikun Wang Dali Li Qiurong Ding Hao Ying Hui Wang Haibing Zhang Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
description	RIPK1 integrates signals that drive both NF-κB activation and cell death pathways. Here Zhang et al. generate RIPK1 knock-in mice lacking a major ubiquitination site and demonstrate that this modification is important to suppress cell death during embryogenesis and inflammation postnatally.
format	article
author	Xixi Zhang Haiwei Zhang Chengxian Xu Xiaoming Li Ming Li Xiaoxia Wu Wenjuan Pu Bin Zhou Haikun Wang Dali Li Qiurong Ding Hao Ying Hui Wang Haibing Zhang
author_facet	Xixi Zhang Haiwei Zhang Chengxian Xu Xiaoming Li Ming Li Xiaoxia Wu Wenjuan Pu Bin Zhou Haikun Wang Dali Li Qiurong Ding Hao Ying Hui Wang Haibing Zhang
author_sort	Xixi Zhang
title	Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
title_short	Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
title_full	Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
title_fullStr	Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
title_full_unstemmed	Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
title_sort	ubiquitination of ripk1 suppresses programmed cell death by regulating ripk1 kinase activation during embryogenesis
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/7a20ff8bd8654fe78c8cee847d1dc433
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_version_	1718386605260013568

Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis

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