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@ARTICLE{Stunden:136817,
author = {Stunden, H James and Latz, Eicke},
title = {{PKR} stirs up inflammasomes.},
journal = {Cell research},
volume = {23},
number = {2},
issn = {1001-0602},
address = {[London]},
publisher = {Macmillan Publishers Limited, part of Springer Nature},
reportid = {DZNE-2020-03139},
pages = {168-170},
year = {2013},
abstract = {Inflammasomes are multiprotein complexes that detect and
respond to foreign and endogenous danger signals by
activating caspase-1; active caspase-1, in turn, matures the
pro-inflammatory IL-1β family cytokines by cleaving their
pro-forms into the biologically active cytokines. The
upstream mechanisms leading to inflammasome activation, in
particular for the NRLP3 inflammasome, remain poorly
understood. Lu and colleagues identify a new function of
Protein Kinase R (PKR) for activating the NLRP1, NLRP3,
NLRC4 and AIM2 inflammasomes, thus identifying a potential
new target for treating inflammasome-mediated diseases.},
subtyp = {Editorial},
keywords = {Animals / Carrier Proteins: metabolism / Humans /
Inflammasomes: metabolism / NLR Family, Pyrin
Domain-Containing 3 Protein / Nitric Oxide: metabolism /
Shock, Septic: prevention $\&$ control / Carrier Proteins
(NLM Chemicals) / Inflammasomes (NLM Chemicals) / NLR
Family, Pyrin Domain-Containing 3 Protein (NLM Chemicals) /
Nlrp3 protein, mouse (NLM Chemicals) / Nitric Oxide (NLM
Chemicals)},
cin = {AG Latz},
ddc = {570},
cid = {I:(DE-2719)1013024},
pnm = {342 - Disease Mechanisms and Model Systems (POF3-342)},
pid = {G:(DE-HGF)POF3-342},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:22945351},
pmc = {pmc:PMC3567816},
doi = {10.1038/cr.2012.125},
url = {https://pub.dzne.de/record/136817},
}