EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation-Reference-Cited by-同舟云学术

EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation

Published:2017-01-13 Issue:4 Volume:2 Page:
ISSN:2058-5276
Container-title:Nature Microbiology
language:en
Short-container-title:Nat Microbiol

Author:

Pearson Jaclyn S.,Giogha Cristina,Mühlen Sabrina,Nachbur Ueli,Pham Chi L. L.,Zhang Ying,Hildebrand Joanne M.,Oates Clare V.,Lung Tania Wong Fok,Ingle Danielle,Dagley Laura F.,Bankovacki Aleksandra,Petrie Emma J.,Schroeder Gunnar N.,Crepin Valerie F.,Frankel Gad,Masters Seth L.,Vince James,Murphy James M.,Sunde Margaret^ORCID,Webb Andrew I.,Silke John,Hartland Elizabeth L.

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Microbiology (medical),Genetics,Applied Microbiology and Biotechnology,Immunology,Microbiology

Link

http://www.nature.com/articles/nmicrobiol2016258.pdf

Reference43 articles.

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2. Kaiser, W. J. & Offermann, M. K. Apoptosis induced by the toll-like receptor adaptor TRIF is dependent on its receptor interacting protein homotypic interaction motif. J. Immunol. 174, 4942–4952 (2005).

3. Rebsamen, M. et al. DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-κB. EMBO Rep. 10, 916–922 (2009).

4. Li, J. et al. The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell 150, 339–350 (2012).

5. Pasparakis, M. & Vandenabeele, P. Necroptosis and its role in inflammation. Nature 517, 311–320 (2015).

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