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@ARTICLE{Hett:136920,
      author       = {Hett, Erik C and Slater, Louise H and Mark, Kevin G and
                      Kawate, Tomohiko and Monks, Brian G and Stutz, Andrea and
                      Latz, Eicke and Hung, Deborah T},
      title        = {{C}hemical genetics reveals a kinase-independent role for
                      protein kinase {R} in pyroptosis.},
      journal      = {Nature chemical biology},
      volume       = {9},
      number       = {6},
      issn         = {1552-4450},
      address      = {Basingstoke},
      publisher    = {Nature Publishing Group},
      reportid     = {DZNE-2020-03242},
      pages        = {398-405},
      year         = {2013},
      abstract     = {Formation of the inflammasome, a scaffolding complex that
                      activates caspase-1, is important in numerous diseases.
                      Pyroptotic cell death induced by anthrax lethal toxin (LT)
                      is a model for inflammasome-mediated caspase-1 activation.
                      We discovered 7-desacetoxy-6,7-dehydrogedunin (7DG) in a
                      phenotypic screen as a small molecule that protects
                      macrophages from LT-induced death. Using chemical
                      proteomics, we identified protein kinase R (PKR) as the
                      target of 7DG and show that RNAi knockdown of PKR
                      phenocopies treatment with 7DG. Further, we show that PKR's
                      role in ASC assembly and caspase-1 activation induced by
                      several different inflammasome stimuli is independent of
                      PKR's kinase activity, demonstrating that PKR has a
                      previously uncharacterized role in caspase-1 activation and
                      pyroptosis that is distinct from its reported
                      kinase-dependent roles in apoptosis and inflammasome
                      formation in lipopolysaccharide-primed cells. Remarkably,
                      PKR has different roles in two distinct cell death pathways
                      and has a broad role in inflammasome function relevant in
                      other diseases.},
      keywords     = {Animals / Bacillus anthracis: enzymology / Caspase 1:
                      metabolism / Catalytic Domain / Cell Death / Cell Line /
                      Enzyme-Linked Immunosorbent Assay / HSP90 Heat-Shock
                      Proteins: metabolism / Hydrogen-Ion Concentration /
                      Inflammation / Macrophages: metabolism / Mice / Mice, Inbred
                      BALB C / Models, Biological / Peptide Hydrolases: metabolism
                      / Proteasome Endopeptidase Complex: metabolism / Protein
                      Conformation / eIF-2 Kinase: chemistry / HSP90 Heat-Shock
                      Proteins (NLM Chemicals) / eIF-2 Kinase (NLM Chemicals) /
                      Peptide Hydrolases (NLM Chemicals) / Caspase 1 (NLM
                      Chemicals) / Proteasome Endopeptidase Complex (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:23603659},
      pmc          = {pmc:PMC6615456},
      doi          = {10.1038/nchembio.1236},
      url          = {https://pub.dzne.de/record/136920},
}