Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct ma...
Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners
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Author / Creator
Li, Xingyan , Zhang, Mengmeng , Huang, Xinyue , Liang, Wei , Li, Ganquan , Lu, Xiaojuan , Li, Yanxia , Pan, Heling , Shi, Linyu , Zhu, Hong , Qian, Lihui , Shan, Bing and Yuan, Junying
Publisher
London: Nature Publishing Group UK
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English
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Publisher
London: Nature Publishing Group UK
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Contents
RIPK1 is a death-domain (DD) containing kinase involved in regulating apoptosis, necroptosis and inflammation. RIPK1 activation is known to be regulated by its DD-mediated interaction and ubiquitination, though underlying mechanisms remain incompletely understood. Here we show that K627 in human RIPK1-DD and its equivalent K612 in murine RIPK1-DD i...
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Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners
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TN_cdi_doaj_primary_oai_doaj_org_article_13104a8bcb9e4fa4a4030c31c509ba7c
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_13104a8bcb9e4fa4a4030c31c509ba7c
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-020-19935-y