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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 ma...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_13104a8bcb9e4fa4a4030c31c509ba7c

Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners

About this item

Full title

Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2020-12, Vol.11 (1), p.6364-6364, Article 6364

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

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...

Alternative Titles

Full title

Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners

Identifiers

Primary Identifiers

Record Identifier

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

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-020-19935-y

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