RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL-Reference-Cited by-同舟云学术

RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL

Published:2015-02-18 Issue:1 Volume:6 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Lawlor Kate E.,Khan Nufail,Mildenhall Alison,Gerlic Motti,Croker Ben A.,D’Cruz Akshay A.,Hall Cathrine,Kaur Spall Sukhdeep,Anderton Holly,Masters Seth L.,Rashidi Maryam,Wicks Ian P.,Alexander Warren S.,Mitsuuchi Yasuhiro,Benetatos Christopher A.,Condon Stephen M.,Wong W. Wei-Lynn,Silke John,Vaux David L.,Vince James E.

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/ncomms7282.pdf

Reference66 articles.

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3. Mahoney, D. J. et al. Both cIAP1 and cIAP2 regulate TNFalpha-mediated NF-kappaB activation. Proc. Natl Acad. Sci. USA 105, 11778–11783 (2008).

4. Bertrand, M. J. et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol. Cell 30, 689–700 (2008).

5. Haas, T. L. et al. Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol. Cell 36, 831–844 (2009).

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