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Volumn 17, Issue 3, 2017, Pages 151-164

Programmed cell death as a defence against infection

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 11; CASPASE 8; INFLAMMASOME; INTERFERON; INTERLEUKIN 18; INTERLEUKIN 1BETA CONVERTING ENZYME; PHOSPHOTRANSFERASE; PROTEIN; RIP KINASE 3; UNCLASSIFIED DRUG; Z DNA BINDING PROTEIN 1;

EID: 85010966276     PISSN: 14741733     EISSN: 14741741     Source Type: Journal    
DOI: 10.1038/nri.2016.147     Document Type: Review
Times cited : (748)

References (180)
  • 1
    • 81055125652 scopus 로고    scopus 로고
    • Programmed cell death in animal development and disease
    • Fuchs, Y., Steller, H. Programmed cell death in animal development and disease. Cell 147, 742-758 (2011)
    • (2011) Cell , vol.147 , pp. 742-758
    • Fuchs, Y.1    Steller, H.2
  • 2
  • 4
    • 84964042566 scopus 로고    scopus 로고
    • Developmental checkpoints guarded by regulated necrosis
    • Dillon, C. P., Tummers, B., Baran, K., Green, D. R. Developmental checkpoints guarded by regulated necrosis. Cell. Mol. Life Sci. 73, 2125-2136 (2016)
    • (2016) Cell. Mol. Life Sci , vol.73 , pp. 2125-2136
    • Dillon, C.P.1    Tummers, B.2    Baran, K.3    Green, D.R.4
  • 6
    • 84927745897 scopus 로고    scopus 로고
    • Pyroptotic cell death defends against intracellular pathogens
    • Jorgensen, I., Miao, E. A. Pyroptotic cell death defends against intracellular pathogens. Immunol. Rev. 265, 130-142 (2015)
    • (2015) Immunol. Rev , vol.265 , pp. 130-142
    • Jorgensen, I.1    Miao, E.A.2
  • 7
    • 79952622190 scopus 로고    scopus 로고
    • Dying for a cause: NETosis, mechanisms behind an antimicrobial cell death modality
    • Remijsen, Q., et al. Dying for a cause: NETosis, mechanisms behind an antimicrobial cell death modality. Cell Death Differ. 18, 581-588 (2011)
    • (2011) Cell Death Differ , vol.18 , pp. 581-588
    • Remijsen, Q.1
  • 8
    • 0029978844 scopus 로고    scopus 로고
    • Macrophage killing is an essential virulence mechanism of Salmonella typhimurium
    • Lindgren, S. W., Stojiljkovic, I., Heffron, F. Macrophage killing is an essential virulence mechanism of Salmonella typhimurium. Proc. Natl Acad. Sci. USA 93, 4197-4201 (1996)
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4197-4201
    • Lindgren, S.W.1    Stojiljkovic, I.2    Heffron, F.3
  • 9
    • 78449269290 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria
    • Miao, E. A., et al. Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat. Immunol. 11, 1136-1142 (2010)
    • (2010) Nat. Immunol , vol.11 , pp. 1136-1142
    • Miao, E.A.1
  • 10
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defence responses to infection
    • Dangl, J. L., Jones, J. D. G. Plant pathogens and integrated defence responses to infection. Nature 411, 826-833 (2001)
    • (2001) Nature , vol.411 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.G.2
  • 11
    • 0037155687 scopus 로고    scopus 로고
    • RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis
    • Mackey, D., Holt, B. F., Wiig, A., Dangl, J. L. RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis. Cell 108, 743-754 (2002)
    • (2002) Cell , vol.108 , pp. 743-754
    • Mackey, D.1    Holt, B.F.2    Wiig, A.3    Dangl, J.L.4
  • 12
    • 0037423306 scopus 로고    scopus 로고
    • Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance
    • Mackey, D., Belkhadir, Y., Alonso, J. M., Ecker, J. R., Dangl, J. L. Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance. Cell 112, 379-389 (2003)
    • (2003) Cell , vol.112 , pp. 379-389
    • Mackey, D.1    Belkhadir, Y.2    Alonso, J.M.3    Ecker, J.R.4    Dangl, J.L.5
  • 13
    • 84976516826 scopus 로고    scopus 로고
    • Inflammasomes: Mechanism of assembly, regulation and signalling
    • Broz, P., Dixit, V. M. Inflammasomes: mechanism of assembly, regulation and signalling. Nat. Rev. Immunol. 16, 407-420 (2016)
    • (2016) Nat. Rev. Immunol. , vol.16 , pp. 407-420
    • Broz, P.1    Dixit, V.M.2
  • 14
    • 80455176839 scopus 로고    scopus 로고
    • Non-canonical inflammasome activation targets caspase-11
    • Kayagaki, N., et al. Non-canonical inflammasome activation targets caspase-11. Nature 479, 117-121 (2011)
    • (2011) Nature , vol.479 , pp. 117-121
    • Kayagaki, N.1
  • 15
    • 84883790050 scopus 로고    scopus 로고
    • Cytoplasmic LPS activates caspase-11: Implications in TLR4-independent endotoxic shock
    • Hagar, J. A., Powell, D. A., Aachoui, Y., Ernst, R. K., Miao, E. A. Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock. Science 341, 1250-1253 (2013)
    • (2013) Science , vol.341 , pp. 1250-1253
    • Hagar, J.A.1    Powell, D.A.2    Aachoui, Y.3    Ernst, R.K.4    Miao, E.A.5
  • 16
    • 84883775365 scopus 로고    scopus 로고
    • Noncanonical inflammasome activation by intracellular LPS independent of TLR4
    • Kayagaki, N., et al. Noncanonical inflammasome activation by intracellular LPS independent of TLR4. Science 341, 1246-1249 (2013)
    • (2013) Science , vol.341 , pp. 1246-1249
    • Kayagaki, N.1
  • 17
    • 84906571225 scopus 로고    scopus 로고
    • Inflammatory caspases are innate immune receptors for intracellular LPS
    • Shi, J., et al. Inflammatory caspases are innate immune receptors for intracellular LPS. Nature 514, 187-192 (2014)
    • (2014) Nature , vol.514 , pp. 187-192
    • Shi, J.1
  • 18
    • 84874189388 scopus 로고    scopus 로고
    • Caspase-11 protects against bacteria that escape the vacuole
    • Aachoui, Y., et al. Caspase-11 protects against bacteria that escape the vacuole. Science 339, 975-978 (2013)
    • (2013) Science , vol.339 , pp. 975-978
    • Aachoui, Y.1
  • 19
    • 84941317034 scopus 로고    scopus 로고
    • Canonical inflammasomes drive IFN-? to prime caspase-11 in defense against a cytosol-invasive bacterium
    • Aachoui, Y., et al. Canonical inflammasomes drive IFN-? to prime caspase-11 in defense against a cytosol-invasive bacterium. Cell Host Microbe 18, 320-332 (2015)
    • (2015) Cell Host Microbe , vol.18 , pp. 320-332
    • Aachoui, Y.1
  • 20
    • 84877844771 scopus 로고    scopus 로고
    • The Shigella OspC3 effector inhibits caspase-4, antagonizes inflammatory cell death, and promotes epithelial infection
    • Kobayashi, T., et al. The Shigella OspC3 effector inhibits caspase-4, antagonizes inflammatory cell death, and promotes epithelial infection. Cell Host Microbe 13, 570-583 (2013)
    • (2013) Cell Host Microbe , vol.13 , pp. 570-583
    • Kobayashi, T.1
  • 21
    • 84942892037 scopus 로고    scopus 로고
    • Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
    • Shi, J., et al. Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature 526, 660-665 (2015)
    • (2015) Nature , vol.526 , pp. 660-665
    • Shi, J.1
  • 22
    • 84942856523 scopus 로고    scopus 로고
    • Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
    • Kayagaki, N., et al. Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature 526, 666-671 (2015)
    • (2015) Nature , vol.526 , pp. 666-671
    • Kayagaki, N.1
  • 23
    • 84949091051 scopus 로고    scopus 로고
    • Gasdermin D is an executor of pyroptosis and required for interleukin-1 secretion
    • He, W.-T., et al. Gasdermin D is an executor of pyroptosis and required for interleukin-1? secretion. Cell Res. 25, 1285-1298 (2015)
    • (2015) Cell Res , vol.25 , pp. 1285-1298
    • He, W.-T.1
  • 24
    • 77951805919 scopus 로고    scopus 로고
    • Inflammatory stimuli regulate caspase substrate profiles
    • Agard, N. J., Maltby, D., Wells, J. A. Inflammatory stimuli regulate caspase substrate profiles. Mol. Cell Proteom. 9, 880-893 (2010)
    • (2010) Mol. Cell Proteom , vol.9 , pp. 880-893
    • Agard, N.J.1    Maltby, D.2    Wells, J.A.3
  • 25
    • 84892030409 scopus 로고    scopus 로고
    • Gasdermin superfamily: A novel gene family functioning in epithelial cells
    • (eds Carrasco, J., Mota, M.
    • Saeki, N., Sasaki, H. Gasdermin superfamily: A novel gene family functioning in epithelial cells in Endothelium and Epithelium (eds Carrasco, J., Mota, M. ) 193-211 (2012)
    • (2012) Endothelium and Epithelium , pp. 193-211
    • Saeki, N.1    Sasaki, H.2
  • 26
    • 84978419608 scopus 로고    scopus 로고
    • Pore-forming activity and structural autoinhibition of the gasdermin family
    • Ding, J., et al. Pore-forming activity and structural autoinhibition of the gasdermin family. Nature 535, 111-116 (2016)
    • (2016) Nature , vol.535 , pp. 111-116
    • Ding, J.1
  • 27
    • 84978128481 scopus 로고    scopus 로고
    • GsdmD p30 elicited by caspase-11 during pyroptosis forms pores in membranes
    • Aglietti, R. A., et al. GsdmD p30 elicited by caspase-11 during pyroptosis forms pores in membranes. Proc. Natl Acad. Sci. USA 113, 7858-7863 (2016)
    • (2016) Proc. Natl Acad. Sci. USA , vol.113 , pp. 7858-7863
    • Aglietti, R.A.1
  • 28
    • 84978374487 scopus 로고    scopus 로고
    • Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores
    • Liu, X., et al. Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores. Nature 535, 153-158 (2016)
    • (2016) Nature , vol.535 , pp. 153-158
    • Liu, X.1
  • 29
    • 84982102736 scopus 로고    scopus 로고
    • GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death
    • Sborgi, L., et al. GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death. EMBO J. 35, 1766-1778 (2016)
    • (2016) EMBO J , vol.35 , pp. 1766-1778
    • Sborgi, L.1
  • 30
    • 55949107533 scopus 로고    scopus 로고
    • Physiology of cell volume regulation in vertebrates
    • Hoffmann, E. K., Lambert, I. H., Pedersen, S. F. Physiology of cell volume regulation in vertebrates. Physiol. Rev. 89, 193-277 (2009)
    • (2009) Physiol. Rev , vol.89 , pp. 193-277
    • Hoffmann, E.K.1    Lambert, I.H.2    Pedersen, S.F.3
  • 31
    • 20344402550 scopus 로고    scopus 로고
    • An emergency response team for membrane repair
    • McNeil, P. L., Kirchhausen, T. An emergency response team for membrane repair. Nat. Rev. Mol. Cell Biol. 6, 499-505 (2005)
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 499-505
    • McNeil, P.L.1    Kirchhausen, T.2
  • 32
    • 84984822442 scopus 로고    scopus 로고
    • Pyroptosis is driven by non-selective gasdermin-D pore and its morphology is different from MLKL channel-mediated necroptosis
    • Chen, X., et al. Pyroptosis is driven by non-selective gasdermin-D pore and its morphology is different from MLKL channel-mediated necroptosis. Cell Res. 26, 1007-1020 (2016)
    • (2016) Cell Res , vol.26 , pp. 1007-1020
    • Chen, X.1
  • 33
    • 80052687210 scopus 로고    scopus 로고
    • Coordinated host responses during pyroptosis: Caspase-1-dependent lysosome exocytosis and inflammatory cytokine maturation
    • Bergsbaken, T., Fink, S. L., Hartigh, den, A. B., Loomis, W. P., Cookson, B. T. Coordinated host responses during pyroptosis: caspase-1-dependent lysosome exocytosis and inflammatory cytokine maturation. J. Immunol. 187, 2748-2754 (2011)
    • (2011) J. Immunol , vol.187 , pp. 2748-2754
    • Bergsbaken, T.1    Fink, S.L.2    Hartigh Den, A.B.3    Loomis, W.P.4    Cookson, B.T.5
  • 34
    • 84867063450 scopus 로고    scopus 로고
    • Rapid induction of inflammatory lipid mediators by the inflammasome in vivo
    • Moltke, Von, J., et al. Rapid induction of inflammatory lipid mediators by the inflammasome in vivo. Nature 490, 107-111 (2012)
    • (2012) Nature , vol.490 , pp. 107-111
    • Von Moltke, J.1
  • 35
    • 84995483254 scopus 로고    scopus 로고
    • IL-1? IL-18, and eicosanoids promote neutrophil recruitment to pore-induced intracellular traps following pyroptosis
    • Jorgensen, I., Lopez, J. P., Laufer, S. A., Miao, E. A. IL-1?, IL-18, and eicosanoids promote neutrophil recruitment to pore-induced intracellular traps following pyroptosis. Eur. J. Immunol. 46, 2761-2766 (2016)
    • (2016) Eur. J. Immunol , vol.46 , pp. 2761-2766
    • Jorgensen, I.1    Lopez, J.P.2    Laufer, S.A.3    Miao, E.A.4
  • 36
    • 77649241461 scopus 로고    scopus 로고
    • Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome
    • Miao, E. A., et al. Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome. Proc. Natl Acad. Sci. USA 107, 3076-3080 (2010)
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 3076-3080
    • Miao, E.A.1
  • 37
    • 79961065571 scopus 로고    scopus 로고
    • Listeria monocytogenes engineered to activate the Nlrc4 inflammasome are severely attenuated and are poor inducers of protective immunity
    • Sauer, J.-D., et al. Listeria monocytogenes engineered to activate the Nlrc4 inflammasome are severely attenuated and are poor inducers of protective immunity. Proc. Natl Acad. Sci. USA 108, 12419-12424 (2011)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 12419-12424
    • Sauer, J.-D.1
  • 38
    • 79959756849 scopus 로고    scopus 로고
    • Generation of a Listeria vaccine strain by enhanced caspase-1 activation
    • Warren, S. E., et al. Generation of a Listeria vaccine strain by enhanced caspase-1 activation. Eur. J. Immunol. 41, 1934-1940 (2011)
    • (2011) Eur. J. Immunol , vol.41 , pp. 1934-1940
    • Warren, S.E.1
  • 39
    • 84947416929 scopus 로고    scopus 로고
    • Inflammasomes coordinate pyroptosis and natural killer cell cytotoxicity to clear infection by a ubiquitous environmental bacterium
    • Maltez, V. I., et al. Inflammasomes coordinate pyroptosis and natural killer cell cytotoxicity to clear infection by a ubiquitous environmental bacterium. Immunity 43, 987-997 (2015)
    • (2015) Immunity , vol.43 , pp. 987-997
    • Maltez, V.I.1
  • 40
    • 84988813074 scopus 로고    scopus 로고
    • Pyroptosis triggers pore-induced intracellular traps (PITs) that capture bacteria and lead to their clearance by efferocytosis
    • Jorgensen, I., Zhang, Y., Krantz, B. A., Miao, E. A. Pyroptosis triggers pore-induced intracellular traps (PITs) that capture bacteria and lead to their clearance by efferocytosis. J. Exp. Med. 213, 2113-2128 (2016)
    • (2016) J. Exp. Med , vol.213 , pp. 2113-2128
    • Jorgensen, I.1    Zhang, Y.2    Krantz, B.A.3    Miao, E.A.4
  • 41
    • 26844452231 scopus 로고    scopus 로고
    • Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis
    • Mariathasan, S., Weiss, D. S., Dixit, V. M., Monack, D. M. Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis. J. Exp. Med. 202, 1043-1049 (2005)
    • (2005) J. Exp. Med , vol.202 , pp. 1043-1049
    • Mariathasan, S.1    Weiss, D.S.2    Dixit, V.M.3    Monack, D.M.4
  • 42
    • 84855272667 scopus 로고    scopus 로고
    • Inflammasome-dependent pyroptosis and IL-18 protect against Burkholderia pseudomallei lung infection while IL-1 is deleterious
    • Ceballos-Olvera, I., Sahoo, M., Miller, M. A., Del Barrio, L., Re, F. Inflammasome-dependent pyroptosis and IL-18 protect against Burkholderia pseudomallei lung infection while IL-1? is deleterious. PLoS Pathog. 7, e1002452 (2011)
    • (2011) PLoS Pathog , vol.7 , pp. e1002452
    • Ceballos-Olvera, I.1    Sahoo, M.2    Miller, M.A.3    Del Barrio, L.4    Re, F.5
  • 43
    • 84881542521 scopus 로고    scopus 로고
    • Inflammasome-mediated pyroptotic and apoptotic cell death, and defense against infection
    • Aachoui, Y., Sagulenko, V., Miao, E. A., Stacey, K. J. Inflammasome-mediated pyroptotic and apoptotic cell death, and defense against infection. Curr. Opin. Microbiol. 16, 319-326 (2013)
    • (2013) Curr. Opin. Microbiol , vol.16 , pp. 319-326
    • Aachoui, Y.1    Sagulenko, V.2    Miao, E.A.3    Stacey, K.J.4
  • 44
    • 84957618366 scopus 로고    scopus 로고
    • Reassessing the evolutionary importance of inflammasomes
    • Maltez, V. I., Miao, E. A. Reassessing the evolutionary importance of inflammasomes. J. Immunol. 196, 956-962 (2016)
    • (2016) J. Immunol. , vol.196 , pp. 956-962
    • Maltez, V.I.1    Miao, E.A.2
  • 45
    • 84908024529 scopus 로고    scopus 로고
    • Epithelium-intrinsic NAIP/NLRC4 inflammasome drives infected enterocyte expulsion to restrict Salmonella replication in the intestinal mucosa
    • Sellin, M. E., et al. Epithelium-intrinsic NAIP/NLRC4 inflammasome drives infected enterocyte expulsion to restrict Salmonella replication in the intestinal mucosa. Cell Host Microbe 16, 237-248 (2014)
    • (2014) Cell Host Microbe , vol.16 , pp. 237-248
    • Sellin, M.E.1
  • 46
    • 84911992879 scopus 로고    scopus 로고
    • Noncanonical inflammasome activation of caspase-4/caspase-11 mediates epithelial defenses against enteric bacterial pathogens
    • Knodler, L. A., et al. Noncanonical inflammasome activation of caspase-4/caspase-11 mediates epithelial defenses against enteric bacterial pathogens. Cell Host Microbe 16, 249-256 (2014)
    • (2014) Cell Host Microbe , vol.16 , pp. 249-256
    • Knodler, L.A.1
  • 47
    • 77951269392 scopus 로고    scopus 로고
    • The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
    • Rathinam, V. A. K., et al. The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses. Nat. Immunol. 11, 395-402 (2010)
    • (2010) Nat. Immunol , vol.11 , pp. 395-402
    • Rathinam, V.A.K.1
  • 48
    • 79956061094 scopus 로고    scopus 로고
    • IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi Sarcoma-associated herpesvirus infection
    • Kerur, N., et al. IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi Sarcoma-associated herpesvirus infection. Cell Host Microbe 9, 363-375 (2011)
    • (2011) Cell Host Microbe , vol.9 , pp. 363-375
    • Kerur, N.1
  • 49
    • 84892739389 scopus 로고    scopus 로고
    • Cell death by pyroptosis drives CD4 T-cell depletion in HIV-1 infection
    • Doitsh, G., et al. Cell death by pyroptosis drives CD4 T-cell depletion in HIV-1 infection. Nature 505, 509-514 (2014)
    • (2014) Nature , vol.505 , pp. 509-514
    • Doitsh, G.1
  • 50
    • 84892946076 scopus 로고    scopus 로고
    • IFI16 DNA sensor is required for death of lymphoid CD4 T cells abortively infected with HIV
    • Monroe, K. M., et al. IFI16 DNA sensor is required for death of lymphoid CD4 T cells abortively infected with HIV. Science 343, 428-432 (2014)
    • (2014) Science , vol.343 , pp. 428-432
    • Monroe, K.M.1
  • 51
    • 84888002403 scopus 로고    scopus 로고
    • From the cover: IFI16 senses DNA forms of the lentiviral replication cycle and controls HIV-1 replication
    • Jakobsen, M. R., et al. From the cover: IFI16 senses DNA forms of the lentiviral replication cycle and controls HIV-1 replication. Proc. Natl Acad. Sci. USA 110, E4571-E4580 (2013)
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E4571-E4580
    • Jakobsen, M.R.1
  • 52
    • 84858420051 scopus 로고    scopus 로고
    • DAI/ZBP1/DLM-1 complexes with RIP3 to mediate virus-induced programmed necrosis that is targeted by murine cytomegalovirus vIRA
    • Upton, J. W., Kaiser, W. J., Mocarski, E. S. DAI/ZBP1/DLM-1 complexes with RIP3 to mediate virus-induced programmed necrosis that is targeted by murine cytomegalovirus vIRA. Cell Host Microbe 11, 290-297 (2012)
    • (2012) Cell Host Microbe , vol.11 , pp. 290-297
    • Upton, J.W.1    Kaiser, W.J.2    Mocarski, E.S.3
  • 53
    • 85022040336 scopus 로고    scopus 로고
    • ZBP1/DAI is an innate sensor of influenza virus triggering the NLRP3 inflammasome and programmed cell death pathways
    • Kuriakose, T., et al. ZBP1/DAI is an innate sensor of influenza virus triggering the NLRP3 inflammasome and programmed cell death pathways. Sci. Immunol. 1, aag2045 (2016)
    • (2016) Sci. Immunol , vol.1 , pp. aag2045
    • Kuriakose, T.1
  • 54
    • 84994731750 scopus 로고    scopus 로고
    • DAI senses influenza A virus genomic RNA and activates RIPK3-dependent cell death
    • Thapa, R. J., et al. DAI senses influenza A virus genomic RNA and activates RIPK3-dependent cell death. Cell Host Microbe 20, 674-681 (2016)
    • (2016) Cell Host Microbe , vol.20 , pp. 674-681
    • Thapa, R.J.1
  • 55
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • Zhang, D.-W., et al. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science 325, 332-336 (2009)
    • (2009) Science , vol.325 , pp. 332-336
    • Zhang, D.-W.1
  • 56
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • Cho, Y. S., et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 137, 1112-1123 (2009)
    • (2009) Cell , vol.137 , pp. 1112-1123
    • Cho, Y.S.1
  • 57
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-?
    • He, S., et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-?. Cell 137, 1100-1111 (2009)
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1
  • 58
    • 84862907788 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase
    • Sun, L., et al. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell 148, 213-227 (2012)
    • (2012) Cell , vol.148 , pp. 213-227
    • Sun, L.1
  • 59
    • 84884308522 scopus 로고    scopus 로고
    • The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism
    • Murphy, J. M., et al. The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism. Immunity 39, 443-453 (2013)
    • (2013) Immunity , vol.39 , pp. 443-453
    • Murphy, J.M.1
  • 60
    • 84901280344 scopus 로고    scopus 로고
    • MLKL compromises plasma membrane integrity by binding to phosphatidylinositol phosphates
    • Dondelinger, Y., et al. MLKL compromises plasma membrane integrity by binding to phosphatidylinositol phosphates. Cell Rep. 7, 971-981 (2014)
    • (2014) Cell Rep , vol.7 , pp. 971-981
    • Dondelinger, Y.1
  • 61
    • 84898027331 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3
    • Wang, H., et al. Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3. Mol. Cell 54, 133-146 (2014)
    • (2014) Mol. Cell , vol.54 , pp. 133-146
    • Wang, H.1
  • 62
    • 84891343566 scopus 로고    scopus 로고
    • Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis
    • Cai, Z., et al. Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nat. Cell Biol. 16, 55-65 (2014)
    • (2014) Nat. Cell Biol , vol.16 , pp. 55-65
    • Cai, Z.1
  • 63
    • 84943329766 scopus 로고    scopus 로고
    • Necroptosis signalling is tuned by phosphorylation of MLKL residues outside the pseudokinase domain activation loop
    • Tanzer, M. C., et al. Necroptosis signalling is tuned by phosphorylation of MLKL residues outside the pseudokinase domain activation loop. Biochem. J. 471, 255-265 (2015)
    • (2015) Biochem. J , vol.471 , pp. 255-265
    • Tanzer, M.C.1
  • 64
    • 84978648026 scopus 로고    scopus 로고
    • RIPK3 activates parallel pathways of MLKL-driven necroptosis and FADD-mediated apoptosis to protect against influenza A virus
    • Nogusa, S., et al. RIPK3 activates parallel pathways of MLKL-driven necroptosis and FADD-mediated apoptosis to protect against influenza A virus. Cell Host Microbe 20, 13-24 (2016)
    • (2016) Cell Host Microbe , vol.20 , pp. 13-24
    • Nogusa, S.1
  • 65
    • 84968538437 scopus 로고    scopus 로고
    • RIPK3 deficiency or catalytically inactive RIPK1 provides greater benefit than MLKL deficiency in mouse models of inflammation and tissue injury
    • Newton, K., et al. RIPK3 deficiency or catalytically inactive RIPK1 provides greater benefit than MLKL deficiency in mouse models of inflammation and tissue injury. Cell Death Differ. 23, 1565-1576 (2016)
    • (2016) Cell Death Differ , vol.23 , pp. 1565-1576
    • Newton, K.1
  • 66
    • 84922925361 scopus 로고    scopus 로고
    • Herpes simplex virus suppresses necroptosis in human cells
    • Guo, H., et al. Herpes simplex virus suppresses necroptosis in human cells. Cell Host Microbe 17, 243-251 (2015)
    • (2015) Cell Host Microbe , vol.17 , pp. 243-251
    • Guo, H.1
  • 67
    • 84954115107 scopus 로고    scopus 로고
    • Herpes simplex virus 1 (HSV-1) and HSV-2 mediate species-specific modulations of programmed necrosis through the viral ribonucleotide reductase large subunit R1
    • Yu, X., et al. Herpes simplex virus 1 (HSV-1) and HSV-2 mediate species-specific modulations of programmed necrosis through the viral ribonucleotide reductase large subunit R1. J. Virol. 90, 1088-1095 (2016)
    • (2016) J. Virol , vol.90 , pp. 1088-1095
    • Yu, X.1
  • 68
    • 84922895437 scopus 로고    scopus 로고
    • RIP1/RIP3 binding to HSV-1 ICP6 initiates necroptosis to restrict virus propagation in mice
    • Huang, Z., et al. RIP1/RIP3 binding to HSV-1 ICP6 initiates necroptosis to restrict virus propagation in mice. Cell Host Microbe 17, 229-242 (2015)
    • (2015) Cell Host Microbe , vol.17 , pp. 229-242
    • Huang, Z.1
  • 69
    • 84908544668 scopus 로고    scopus 로고
    • Direct activation of RIP3/MLKL-dependent necrosis by herpes simplex virus 1 (HSV-1) protein ICP6 triggers host antiviral defense
    • Wang, X., et al. Direct activation of RIP3/MLKL-dependent necrosis by herpes simplex virus 1 (HSV-1) protein ICP6 triggers host antiviral defense. Proc. Natl Acad. Sci. USA 111, 15438-15443 (2014)
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 15438-15443
    • Wang, X.1
  • 70
    • 84892608467 scopus 로고    scopus 로고
    • Cellular inhibitor of apoptosis protein cIAP2 protects against pulmonary tissue necrosis during influenza virus infection to promote host survival
    • Rodrigue-Gervais, I. G., et al. Cellular inhibitor of apoptosis protein cIAP2 protects against pulmonary tissue necrosis during influenza virus infection to promote host survival. Cell Host Microbe 15, 23-35 (2014)
    • (2014) Cell Host Microbe , vol.15 , pp. 23-35
    • Rodrigue-Gervais, I.G.1
  • 71
    • 80053087284 scopus 로고    scopus 로고
    • Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity
    • Lu, J. V., et al. Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity. Proc. Natl Acad. Sci. USA 108, 15312-15317 (2011)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 15312-15317
    • Lu, J.V.1
  • 72
    • 84866544929 scopus 로고    scopus 로고
    • Type i interferon induces necroptosis in macrophages during infection with Salmonella enterica serovar Typhimurium
    • Robinson, N., et al. Type I interferon induces necroptosis in macrophages during infection with Salmonella enterica serovar Typhimurium. Nat. Immunol. 13, 954-962 (2012)
    • (2012) Nat. Immunol. , vol.13 , pp. 954-962
    • Robinson, N.1
  • 73
    • 77149132187 scopus 로고    scopus 로고
    • Induction of IFN- enables Listeria monocytogenes to suppress macrophage activation by IFN
    • Rayamajhi, M., Humann, J., Penheiter, K., Andreasen, K., Lenz, L. L. Induction of IFN- enables Listeria monocytogenes to suppress macrophage activation by IFN-. J. Exp. Med. 207, 327-337 (2010)
    • (2010) J. Exp. Med , vol.207 , pp. 327-337
    • Rayamajhi, M.1    Humann, J.2    Penheiter, K.3    Andreasen, K.4    Lenz, L.L.5
  • 74
    • 84901020402 scopus 로고    scopus 로고
    • Caspase-8 mediates caspase-1 processing and innate immune defense in response to bacterial blockade of NF-?B and MAPK signaling
    • Philip, N. H., et al. Caspase-8 mediates caspase-1 processing and innate immune defense in response to bacterial blockade of NF-?B and MAPK signaling. Proc. Natl Acad. Sci. USA 111, 7385-7390 (2014)
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 7385-7390
    • Philip, N.H.1
  • 75
    • 84894271641 scopus 로고    scopus 로고
    • FADD and caspase-8 mediate priming and activation of the canonical and noncanonical Nlrp3 inflammasomes
    • Gurung, P., et al. FADD and caspase-8 mediate priming and activation of the canonical and noncanonical Nlrp3 inflammasomes. J. Immunol. 192, 1835-1846 (2014)
    • (2014) J. Immunol , vol.192 , pp. 1835-1846
    • Gurung, P.1
  • 76
    • 84901045151 scopus 로고    scopus 로고
    • Caspase-8 and RIP kinases regulate bacteria-induced innate immune responses and cell death
    • Weng, D., et al. Caspase-8 and RIP kinases regulate bacteria-induced innate immune responses and cell death. Proc. Natl Acad. Sci. USA 111, 7391-7396 (2014)
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 7391-7396
    • Weng, D.1
  • 77
    • 84981703921 scopus 로고    scopus 로고
    • Necroptosis promotes Staphylococcus aureus clearance by inhibiting excessive inflammatory signaling
    • Kitur, K., et al. Necroptosis promotes Staphylococcus aureus clearance by inhibiting excessive inflammatory signaling. Cell Rep. 16, 2219-2230 (2016)
    • (2016) Cell Rep , vol.16 , pp. 2219-2230
    • Kitur, K.1
  • 78
    • 84929494277 scopus 로고    scopus 로고
    • Toxin-induced necroptosis is a major mechanism of Staphylococcus aureus lung damage
    • Kitur, K., et al. Toxin-induced necroptosis is a major mechanism of Staphylococcus aureus lung damage. PLoS Pathog. 11, e1004820 (2015)
    • (2015) PLoS Pathog , vol.11 , pp. e1004820
    • Kitur, K.1
  • 79
    • 84953310309 scopus 로고    scopus 로고
    • Pore-forming toxins induce macrophage necroptosis during acute bacterial pneumonia
    • Gonzlez-Juarbe, N., et al. Pore-forming toxins induce macrophage necroptosis during acute bacterial pneumonia. PLoS Pathog. 11, e1005337 (2015)
    • (2015) PLoS Pathog , vol.11 , pp. e1005337
    • Gonzlez-Juarbe, N.1
  • 80
    • 84896690342 scopus 로고    scopus 로고
    • Apoptotic cell clearance: Basic biology and therapeutic potential
    • Poon, I. K. H., Lucas, C. D., Rossi, A. G., Ravichandran, K. S. Apoptotic cell clearance: basic biology and therapeutic potential. Nat. Rev. Immunol. 14, 166-180 (2014)
    • (2014) Nat. Rev. Immunol , vol.14 , pp. 166-180
    • Poon, I.K.H.1    Lucas, C.D.2    Rossi, A.G.3    Ravichandran, K.S.4
  • 81
    • 77958184901 scopus 로고    scopus 로고
    • Manipulation of host cell death pathways during microbial infections
    • Lamkanfi, M., Dixit, V. M. Manipulation of host cell death pathways during microbial infections. Cell Host Microbe 8, 44-54 (2010)
    • (2010) Cell Host Microbe , vol.8 , pp. 44-54
    • Lamkanfi, M.1    Dixit, V.M.2
  • 82
    • 84964607369 scopus 로고    scopus 로고
    • The commonalities in bacterial effector inhibition of apoptosis
    • Robinson, K. S., Aw, R. The commonalities in bacterial effector inhibition of apoptosis. Trends Microbiol. 24, 665-680 (2016)
    • (2016) Trends Microbiol , vol.24 , pp. 665-680
    • Robinson, K.S.1    Aw, R.2
  • 83
    • 84979058863 scopus 로고    scopus 로고
    • Discoveries and controversies in BCL-2 protein-mediated apoptosis
    • Zheng, J. H., Viacava Follis, A., Kriwacki, R. W., Moldoveanu, T. Discoveries and controversies in BCL-2 protein-mediated apoptosis. FEBS J. 283, 2690-2700 (2016)
    • (2016) FEBS J , vol.283 , pp. 2690-2700
    • Zheng, J.H.1    Viacava Follis, A.2    Kriwacki, R.W.3    Moldoveanu, T.4
  • 84
    • 70350025502 scopus 로고    scopus 로고
    • Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis
    • Dewson, G., Kluck, R. M. Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis. J. Cell. Sci. 122, 2801-2808 (2009)
    • (2009) J. Cell. Sci , vol.122 , pp. 2801-2808
    • Dewson, G.1    Kluck, R.M.2
  • 85
    • 84919884654 scopus 로고    scopus 로고
    • Apoptotic caspases suppress mtDNA-induced STING-mediated type i IFN production
    • White, M. J., et al. Apoptotic caspases suppress mtDNA-induced STING-mediated type I IFN production. Cell 159, 1549-1562 (2014)
    • (2014) Cell , vol.159 , pp. 1549-1562
    • White, M.J.1
  • 86
    • 84919898250 scopus 로고    scopus 로고
    • Apoptotic caspases prevent the induction of type i interferons by mitochondrial DNA
    • Rongvaux, A., et al. Apoptotic caspases prevent the induction of type I interferons by mitochondrial DNA. Cell 159, 1563-1577 (2014)
    • (2014) Cell , vol.159 , pp. 1563-1577
    • Rongvaux, A.1
  • 87
    • 84884151651 scopus 로고    scopus 로고
    • Masters marionettes and modulators: Intersection of pathogen virulence factors and mammalian death receptor signaling
    • Silke, J., Hartland, E. L. Masters, marionettes and modulators: intersection of pathogen virulence factors and mammalian death receptor signaling. Curr. Opin. Immunol. 25, 436-440 (2013)
    • (2013) Curr. Opin. Immunol , vol.25 , pp. 436-440
    • Silke, J.1    Hartland, E.L.2
  • 88
    • 79952811804 scopus 로고    scopus 로고
    • RIP3 mediates the embryonic lethality of caspase-8-deficient mice
    • Kaiser, W. J., et al. RIP3 mediates the embryonic lethality of caspase-8-deficient mice. Nature 471, 368-372 (2011)
    • (2011) Nature , vol.471 , pp. 368-372
    • Kaiser, W.J.1
  • 89
    • 79952810024 scopus 로고    scopus 로고
    • Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis
    • Oberst, A., et al. Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis. Nature 471, 363-367 (2011)
    • (2011) Nature , vol.471 , pp. 363-367
    • Oberst, A.1
  • 90
    • 84897088275 scopus 로고    scopus 로고
    • Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis
    • Newton, K., et al. Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis. Science 343, 1357-1360 (2014)
    • (2014) Science , vol.343 , pp. 1357-1360
    • Newton, K.1
  • 91
    • 84912106351 scopus 로고    scopus 로고
    • RIP3 induces apoptosis independent of pronecrotic kinase activity
    • Mandal, P., et al. RIP3 induces apoptosis independent of pronecrotic kinase activity. Mol. Cell 56, 481-495 (2014)
    • (2014) Mol. Cell , vol.56 , pp. 481-495
    • Mandal, P.1
  • 92
    • 84901422731 scopus 로고    scopus 로고
    • RIPK1 regulates RIPK3-MLKL-driven systemic inflammation and emergency hematopoiesis
    • Rickard, J. A., et al. RIPK1 regulates RIPK3-MLKL-driven systemic inflammation and emergency hematopoiesis. Cell 157, 1175-1188 (2014)
    • (2014) Cell , vol.157 , pp. 1175-1188
    • Rickard, J.A.1
  • 93
    • 84901386193 scopus 로고    scopus 로고
    • RIPK1 blocks early postnatal lethality mediated by caspase-8 and RIPK3
    • Dillon, C. P., et al. RIPK1 blocks early postnatal lethality mediated by caspase-8 and RIPK3. Cell 157, 1189-1202 (2014)
    • (2014) Cell , vol.157 , pp. 1189-1202
    • Dillon, C.P.1
  • 94
    • 84901649808 scopus 로고    scopus 로고
    • RIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition
    • Kaiser, W. J., et al. RIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition. Proc. Natl Acad. Sci. USA 111, 7753-7758 (2014)
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 7753-7758
    • Kaiser, W.J.1
  • 95
    • 85000542319 scopus 로고    scopus 로고
    • RIPK1 counteracts ZBP1-mediated necroptosis to inhibit inflammation
    • Lin, J., et al. RIPK1 counteracts ZBP1-mediated necroptosis to inhibit inflammation. Nature 540, 124-128 (2016)
    • (2016) Nature , vol.540 , pp. 124-128
    • Lin, J.1
  • 96
    • 85000659718 scopus 로고    scopus 로고
    • RIPK1 inhibits ZBP1-driven necroptosis during development
    • Newton, K., et al. RIPK1 inhibits ZBP1-driven necroptosis during development. Nature 540, 129-133 (2016)
    • (2016) Nature , vol.540 , pp. 129-133
    • Newton, K.1
  • 97
    • 27744561393 scopus 로고    scopus 로고
    • Rip1 mediates the Trif-dependent toll-like receptor 3-and 4-induced NF-?B activation but does not contribute to interferon regulatory factor 3 activation
    • Cusson-Hermance, N., Khurana, S., Lee, T. H., Fitzgerald, K. A., Kelliher, M. A. Rip1 mediates the Trif-dependent toll-like receptor 3-and 4-induced NF-?B activation but does not contribute to interferon regulatory factor 3 activation. J. Biol. Chem. 280, 36560-36566 (2005)
    • (2005) J. Biol. Chem , vol.280 , pp. 36560-36566
    • Cusson-Hermance, N.1    Khurana, S.2    Lee, T.H.3    Fitzgerald, K.A.4    Kelliher, M.A.5
  • 98
    • 2442642691 scopus 로고    scopus 로고
    • RIP1 is an essential mediator of Toll-like receptor 3-induced NF-?B activation
    • Meylan, E., et al. RIP1 is an essential mediator of Toll-like receptor 3-induced NF-?B activation. Nat. Immunol. 5, 503-507 (2004)
    • (2004) Nat. Immunol , vol.5 , pp. 503-507
    • Meylan, E.1
  • 99
    • 84908128377 scopus 로고    scopus 로고
    • The necroptosis adaptor RIPK3 promotes injury-induced cytokine expression and tissue repair
    • Moriwaki, K., et al. The necroptosis adaptor RIPK3 promotes injury-induced cytokine expression and tissue repair. Immunity 41, 567-578 (2014)
    • (2014) Immunity , vol.41 , pp. 567-578
    • Moriwaki, K.1
  • 100
    • 84932601454 scopus 로고    scopus 로고
    • Caspase-8 scaffolding function and MLKL regulate NLRP3 inflammasome activation downstream of TLR3
    • Kang, S., et al. Caspase-8 scaffolding function and MLKL regulate NLRP3 inflammasome activation downstream of TLR3. Nat. Commun. 6, 7515 (2015)
    • (2015) Nat. Commun , vol.6 , pp. 7515
    • Kang, S.1
  • 101
    • 1542287347 scopus 로고    scopus 로고
    • Neutrophil extracellular traps kill bacteria
    • Brinkmann, V., et al. Neutrophil extracellular traps kill bacteria. Science 303, 1532-1535 (2004)
    • (2004) Science , vol.303 , pp. 1532-1535
    • Brinkmann, V.1
  • 102
    • 84908135568 scopus 로고    scopus 로고
    • Neutrophils sense microbe size and selectively release neutrophil extracellular traps in response to large pathogens
    • Branzk, N., et al. Neutrophils sense microbe size and selectively release neutrophil extracellular traps in response to large pathogens. Nat. Immunol. 15, 1017-1025 (2014)
    • (2014) Nat. Immunol , vol.15 , pp. 1017-1025
    • Branzk, N.1
  • 103
    • 34147188469 scopus 로고    scopus 로고
    • Platelet TLR4 activates neutrophil extracellular traps to ensnare bacteria in septic blood
    • Clark, S. R., et al. Platelet TLR4 activates neutrophil extracellular traps to ensnare bacteria in septic blood. Nat. Med. 13, 463-469 (2007)
    • (2007) Nat. Med , vol.13 , pp. 463-469
    • Clark, S.R.1
  • 104
    • 84866177387 scopus 로고    scopus 로고
    • Requirements for NADPH oxidase and myeloperoxidase in neutrophil extracellular trap formation differ depending on the stimulus
    • Parker, H., Dragunow, M., Hampton, M. B., Kettle, A. J., Winterbourn, C. C. Requirements for NADPH oxidase and myeloperoxidase in neutrophil extracellular trap formation differ depending on the stimulus. J. Leukoc. Biol. 92, 841-849 (2012)
    • (2012) J. Leukoc. Biol , vol.92 , pp. 841-849
    • Parker, H.1    Dragunow, M.2    Hampton, M.B.3    Kettle, A.J.4    Winterbourn, C.C.5
  • 105
    • 78049496216 scopus 로고    scopus 로고
    • Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps
    • Papayannopoulos, V., Metzler, K. D., Hakkim, A., Zychlinsky, A. Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps. J. Cell Biol. 191, 677-691 (2010)
    • (2010) J. Cell Biol , vol.191 , pp. 677-691
    • Papayannopoulos, V.1    Metzler, K.D.2    Hakkim, A.3    Zychlinsky, A.4
  • 106
    • 84868632379 scopus 로고    scopus 로고
    • Infection-induced NETosis is a dynamic process involving neutrophil multitasking in vivo
    • Yipp, B. G., et al. Infection-induced NETosis is a dynamic process involving neutrophil multitasking in vivo. Nat. Med. 18, 1386-1393 (2012)
    • (2012) Nat. Med , vol.18 , pp. 1386-1393
    • Yipp, B.G.1
  • 107
    • 84887439544 scopus 로고    scopus 로고
    • Salmonella infection induces recruitment of caspase-8 to the inflammasome to modulate IL-1 production
    • Man, S. M., et al. Salmonella infection induces recruitment of caspase-8 to the inflammasome to modulate IL-1? production. J. Immunol. 191, 5239-5246 (2013)
    • (2013) J. Immunol , vol.191 , pp. 5239-5246
    • Man, S.M.1
  • 108
    • 84907033643 scopus 로고    scopus 로고
    • Caspase-8 modulates dectin-1 and complement receptor 3-driven IL-1 production in response to -glucans and the fungal pathogen Candida albicans
    • Ganesan, S., et al. Caspase-8 modulates dectin-1 and complement receptor 3-driven IL-1? production in response to ?-glucans and the fungal pathogen Candida albicans. J. Immunol. 193, 2519-2530 (2014)
    • (2014) J. Immunol , vol.193 , pp. 2519-2530
    • Ganesan, S.1
  • 109
    • 84906852294 scopus 로고    scopus 로고
    • Mitochondrial apoptosis is dispensable for NLRP3 inflammasome activation but non-apoptotic caspase-8 is required for inflammasome priming
    • Allam, R., et al. Mitochondrial apoptosis is dispensable for NLRP3 inflammasome activation but non-apoptotic caspase-8 is required for inflammasome priming. EMBO Rep. 15, 982-990 (2014)
    • (2014) EMBO Rep , vol.15 , pp. 982-990
    • Allam, R.1
  • 110
    • 84872764927 scopus 로고    scopus 로고
    • Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome
    • Kang, T.-B., Yang, S.-H., Toth, B., Kovalenko, A., Wallach, D. Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome. Immunity 38, 27-40 (2012)
    • (2012) Immunity , vol.38 , pp. 27-40
    • Kang, T.-B.1    Yang, S.-H.2    Toth, B.3    Kovalenko, A.4    Wallach, D.5
  • 111
    • 84873834109 scopus 로고    scopus 로고
    • Deubiquitinases regulate the activity of caspase-1 and interleukin-1 secretion via assembly of the inflammasome
    • Lopez-Castejon, G., et al. Deubiquitinases regulate the activity of caspase-1 and interleukin-1? secretion via assembly of the inflammasome. J. Biol. Chem. 288, 2721-2733 (2013)
    • (2013) J. Biol. Chem , vol.288 , pp. 2721-2733
    • Lopez-Castejon, G.1
  • 112
    • 84867770402 scopus 로고    scopus 로고
    • Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation
    • Juliana, C., et al. Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation. J. Biol. Chem. 287, 36617-36622 (2012)
    • (2012) J. Biol. Chem , vol.287 , pp. 36617-36622
    • Juliana, C.1
  • 113
    • 84872782298 scopus 로고    scopus 로고
    • Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity
    • Py, B. F., Kim, M.-S., Vakifahmetoglu-Norberg, H., Yuan, J. Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity. Mol. Cell 49, 331-338 (2013)
    • (2013) Mol. Cell , vol.49 , pp. 331-338
    • Py, B.F.1    Kim, M.-S.2    Vakifahmetoglu-Norberg, H.3    Yuan, J.4
  • 114
    • 84923674191 scopus 로고    scopus 로고
    • RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL
    • Lawlor, K. E., et al. RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL. Nat. Commun. 6, 6282 (2015)
    • (2015) Nat. Commun , vol.6 , pp. 6282
    • Lawlor, K.E.1
  • 115
    • 84896381627 scopus 로고    scopus 로고
    • Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation
    • Cai, X., et al. Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation. Cell 156, 1207-1222 (2014)
    • (2014) Cell , vol.156 , pp. 1207-1222
    • Cai, X.1
  • 116
    • 84896332642 scopus 로고    scopus 로고
    • Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes
    • Lu, A., et al. Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes. Cell 156, 1193-1206 (2014)
    • (2014) Cell , vol.156 , pp. 1193-1206
    • Lu, A.1
  • 117
    • 84866087868 scopus 로고    scopus 로고
    • AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages
    • Pierini, R., et al. AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages. Cell Death Differ. 19, 1709-1721 (2012)
    • (2012) Cell Death Differ , vol.19 , pp. 1709-1721
    • Pierini, R.1
  • 118
    • 84882280029 scopus 로고    scopus 로고
    • AIM2 and NLRP3 inflammasomes activate both apoptotic and pyroptotic death pathways via ASC
    • Sagulenko, V., et al. AIM2 and NLRP3 inflammasomes activate both apoptotic and pyroptotic death pathways via ASC. Cell Death Differ. 20, 1149-1160 (2013)
    • (2013) Cell Death Differ , vol.20 , pp. 1149-1160
    • Sagulenko, V.1
  • 119
    • 84951814419 scopus 로고    scopus 로고
    • The inflammasome adaptor ASC induces procaspase-8 death effector domain filaments
    • Vajjhala, P. R., et al. The inflammasome adaptor ASC induces procaspase-8 death effector domain filaments. J. Biol. Chem. 290, 29217-29230 (2015)
    • (2015) J. Biol. Chem , vol.290 , pp. 29217-29230
    • Vajjhala, P.R.1
  • 120
    • 84871001488 scopus 로고    scopus 로고
    • The Yersinia virulence effector YopM binds caspase-1 to arrest inflammasome assembly and processing
    • LaRock, C. N., Cookson, B. T. The Yersinia virulence effector YopM binds caspase-1 to arrest inflammasome assembly and processing. Cell Host Microbe 12, 799-805 (2012)
    • (2012) Cell Host Microbe , vol.12 , pp. 799-805
    • LaRock, C.N.1    Cookson, B.T.2
  • 121
    • 84885136821 scopus 로고    scopus 로고
    • ASC controls IFN- levels in an IL-18-dependent manner in caspase-1-deficient mice infected with Francisella novicida
    • Pierini, R., et al. ASC controls IFN-? levels in an IL-18-dependent manner in caspase-1-deficient mice infected with Francisella novicida. J. Immunol. 191, 3847-3857 (2013)
    • (2013) J. Immunol , vol.191 , pp. 3847-3857
    • Pierini, R.1
  • 122
    • 51049100571 scopus 로고    scopus 로고
    • Stimulation of Toll-like receptor 3 and 4 induces interleukin-1 maturation by caspase-8
    • Maelfait, J., et al. Stimulation of Toll-like receptor 3 and 4 induces interleukin-1? maturation by caspase-8. J. Exp. Med. 205, 1967-1973 (2008)
    • (2008) J. Exp. Med , vol.205 , pp. 1967-1973
    • Maelfait, J.1
  • 123
    • 84871125002 scopus 로고    scopus 로고
    • Cutting edge: FAS (CD95) mediates noncanonical IL-1? and IL-18 maturation via caspase-8 in an RIP3-independent manner
    • Bossaller, L., et al. Cutting edge: FAS (CD95) mediates noncanonical IL-1? and IL-18 maturation via caspase-8 in an RIP3-independent manner. J. Immunol. 189, 5508-5512 (2012)
    • (2012) J. Immunol , vol.189 , pp. 5508-5512
    • Bossaller, L.1
  • 124
    • 84939608936 scopus 로고    scopus 로고
    • Caspase-8 as an effector andregulator of NLRP3 inflammasome signaling
    • Antonopoulos, C., et al. Caspase-8 as an effector andregulator of NLRP3 inflammasome signaling. J. Biol. Chem. 290, 20167-20184 (2015)
    • (2015) J. Biol. Chem , vol.290 , pp. 20167-20184
    • Antonopoulos, C.1
  • 125
    • 84857404572 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation
    • Vince, J. E., et al. Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation. Immunity 36, 215-227 (2012)
    • (2012) Immunity , vol.36 , pp. 215-227
    • Vince, J.E.1
  • 126
    • 0028608085 scopus 로고
    • CD8+ T cell-mediated protection against an intracellular bacterium by perforin-dependent cytotoxicity
    • K?gi, D., Ledermann, B., B?rki, K., Hengartner, H., Zinkernagel, R. M. CD8+ T cell-mediated protection against an intracellular bacterium by perforin-dependent cytotoxicity. Eur. J. Immunol. 24, 3068-3072 (1994)
    • (1994) Eur. J. Immunol , vol.24 , pp. 3068-3072
    • Kgi, D.1    Ledermann, B.2    Brki, K.3    Hengartner, H.4    Zinkernagel, R.M.5
  • 127
    • 0031013561 scopus 로고    scopus 로고
    • Perforin, a cytotoxic molecule which mediates cell necrosis, is not required for the early control of mycobacterial infection in mice
    • Laochumroonvorapong, P., et al. Perforin, a cytotoxic molecule which mediates cell necrosis, is not required for the early control of mycobacterial infection in mice. Infect. Immun. 65, 127-132 (1997)
    • (1997) Infect. Immun , vol.65 , pp. 127-132
    • Laochumroonvorapong, P.1
  • 128
    • 84978796164 scopus 로고    scopus 로고
    • An NK cell perforin response elicited via IL-18 controls mucosal inflammation kinetics during Salmonella gut infection
    • M?ller, A. A., et al. An NK cell perforin response elicited via IL-18 controls mucosal inflammation kinetics during Salmonella gut infection. PLoS Pathog. 12, e1005723-e1005730 (2016)
    • (2016) PLoS Pathog , vol.12 , pp. e1005723-e1005730
    • Mller, A.A.1
  • 129
    • 84961250343 scopus 로고    scopus 로고
    • Lack of the programmed death-1 receptor renders host susceptible to enteric microbial infection through impairing the production of the mucosal natural killer cell effector molecules
    • Solaymani-Mohammadi, S., et al. Lack of the programmed death-1 receptor renders host susceptible to enteric microbial infection through impairing the production of the mucosal natural killer cell effector molecules. J. Leukoc. Biol. 99, 475-482 (2016)
    • (2016) J. Leukoc. Biol , vol.99 , pp. 475-482
    • Solaymani-Mohammadi, S.1
  • 130
    • 84902108865 scopus 로고    scopus 로고
    • Cytotoxic cells kill intracellular bacteria through granulysin-mediated delivery of granzymes
    • Walch, M., et al. Cytotoxic cells kill intracellular bacteria through granulysin-mediated delivery of granzymes. Cell 157, 1309-1323 (2014)
    • (2014) Cell , vol.157 , pp. 1309-1323
    • Walch, M.1
  • 131
    • 84957441649 scopus 로고    scopus 로고
    • Killer lymphocytes use granulysin, perforin and granzymes to kill intracellular parasites
    • Dotiwala, F., et al. Killer lymphocytes use granulysin, perforin and granzymes to kill intracellular parasites. Nat. Med. 22, 210-216 (2016)
    • (2016) Nat. Med , vol.22 , pp. 210-216
    • Dotiwala, F.1
  • 132
    • 0031133280 scopus 로고    scopus 로고
    • Programmed cell death of Mycobacterium avium serovar 4-infected human macrophages prevents the mycobacteria from spreading and induces mycobacterial growth inhibition by freshly added, uninfected macrophages
    • Fratazzi, C., Arbeit, R. D., Carini, C., Remold, H. G. Programmed cell death of Mycobacterium avium serovar 4-infected human macrophages prevents the mycobacteria from spreading and induces mycobacterial growth inhibition by freshly added, uninfected macrophages. J. Immunol. 158, 4320-4327 (1997)
    • (1997) J. Immunol , vol.158 , pp. 4320-4327
    • Fratazzi, C.1    Arbeit, R.D.2    Carini, C.3    Remold, H.G.4
  • 133
    • 77955661920 scopus 로고    scopus 로고
    • Evasion of innate immunity by Mycobacterium tuberculosis: Is death an exit strategy?
    • Behar, S. M., Divangahi, M., Remold, H. G. Evasion of innate immunity by Mycobacterium tuberculosis: is death an exit strategy? Nat. Rev. Microbiol. 8, 668-674 (2010)
    • (2010) Nat. Rev. Microbiol , vol.8 , pp. 668-674
    • Behar, S.M.1    Divangahi, M.2    Remold, H.G.3
  • 134
    • 84866403046 scopus 로고    scopus 로고
    • Efferocytosis Is an Innate Antibacterial Mechanism
    • Martin, C. J., et al. Efferocytosis Is an Innate Antibacterial Mechanism. Cell Host Microbe 12, 289-300 (2012)
    • (2012) Cell Host Microbe , vol.12 , pp. 289-300
    • Martin, C.J.1
  • 135
    • 84866348007 scopus 로고    scopus 로고
    • Neutrophils exert protection in the early tuberculous granuloma by oxidative killing of mycobacteria phagocytosed from infected macrophages
    • Yang, C.-T., et al. Neutrophils exert protection in the early tuberculous granuloma by oxidative killing of mycobacteria phagocytosed from infected macrophages. Cell Host Microbe 12, 301-312 (2012)
    • (2012) Cell Host Microbe , vol.12 , pp. 301-312
    • Yang, C.-T.1
  • 136
    • 81355132255 scopus 로고    scopus 로고
    • Interactions between na?ve and infected macrophages reduce Mycobacterium tuberculosis viability
    • Hartman, M. L., Kornfeld, H. Interactions between na?ve and infected macrophages reduce Mycobacterium tuberculosis viability. PLoS ONE 6, e27972 (2011)
    • (2011) PLoS ONE , vol.6 , pp. e27972
    • Hartman, M.L.1    Kornfeld, H.2
  • 137
    • 84899912557 scopus 로고    scopus 로고
    • Listeria monocytogenes exploits efferocytosis to promote cell-to-cell spread
    • Czuczman, M. A., et al. Listeria monocytogenes exploits efferocytosis to promote cell-to-cell spread. Nature 509, 230-234 (2014)
    • (2014) Nature , vol.509 , pp. 230-234
    • Czuczman, M.A.1
  • 138
    • 0034054028 scopus 로고    scopus 로고
    • Virus clearance through apoptosis-dependent phagocytosis of influenza A virus-infected cells by macrophages
    • Fujimoto, I., Pan, J., Takizawa, T., Nakanishi, Y. Virus clearance through apoptosis-dependent phagocytosis of influenza A virus-infected cells by macrophages. J. Virol. 74, 3399-3403 (2000)
    • (2000) J. Virol , vol.74 , pp. 3399-3403
    • Fujimoto, I.1    Pan, J.2    Takizawa, T.3    Nakanishi, Y.4
  • 139
  • 140
    • 32944463724 scopus 로고    scopus 로고
    • Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms
    • Urban, C. F., Reichard, U., Brinkmann, V., Zychlinsky, A. Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms. Cell. Microbiol. 8, 668-676 (2006)
    • (2006) Cell. Microbiol , vol.8 , pp. 668-676
    • Urban, C.F.1    Reichard, U.2    Brinkmann, V.3    Zychlinsky, A.4
  • 141
    • 84856598960 scopus 로고    scopus 로고
    • Killing by neutrophil extracellular traps: Fact or folklore?
    • Menegazzi, R., Decleva, E., Dri, P. Killing by neutrophil extracellular traps: fact or folklore? Blood 119, 1214-1216 (2012)
    • (2012) Blood , vol.119 , pp. 1214-1216
    • Menegazzi, R.1    Decleva, E.2    Dri, P.3
  • 142
    • 84891505072 scopus 로고    scopus 로고
    • NETosis: How vital is it?
    • Yipp, B. G., Kubes, P. NETosis: how vital is it? Blood 122, 2784-2794 (2013)
    • (2013) Blood , vol.122 , pp. 2784-2794
    • Yipp, B.G.1    Kubes, P.2
  • 143
    • 84866386143 scopus 로고    scopus 로고
    • Intravascular neutrophil extracellular traps capture bacteria from the bloodstream during sepsis
    • McDonald, B., Urrutia, R., Yipp, B. G., Jenne, C. N., Kubes, P. Intravascular neutrophil extracellular traps capture bacteria from the bloodstream during sepsis. Cell Host Microbe 12, 324-333 (2012)
    • (2012) Cell Host Microbe , vol.12 , pp. 324-333
    • McDonald, B.1    Urrutia, R.2    Yipp, B.G.3    Jenne, C.N.4    Kubes, P.5
  • 144
    • 62449323653 scopus 로고    scopus 로고
    • M1 protein allows Group A streptococcal survival in phagocyte extracellular traps through cathelicidin inhibition
    • Lauth, X., et al. M1 protein allows Group A streptococcal survival in phagocyte extracellular traps through cathelicidin inhibition. J. Innate Immun. 1, 202-214 (2009)
    • (2009) J. Innate Immun , vol.1 , pp. 202-214
    • Lauth, X.1
  • 145
    • 84987815185 scopus 로고    scopus 로고
    • Pondering neutrophil extracellular traps with healthy skepticism
    • Nauseef, W. M., Kubes, P. Pondering neutrophil extracellular traps with healthy skepticism. Cell. Microbiol. 18, 1349-1357 (2016)
    • (2016) Cell. Microbiol , vol.18 , pp. 1349-1357
    • Nauseef, W.M.1    Kubes, P.2
  • 146
    • 32944482526 scopus 로고    scopus 로고
    • An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps
    • Beiter, K., et al. An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps. Curr. Biol. 16, 401-407 (2006)
    • (2006) Curr. Biol , vol.16 , pp. 401-407
    • Beiter, K.1
  • 147
    • 84884679672 scopus 로고    scopus 로고
    • Vibrio cholerae evades neutrophil extracellular traps by the activity of two extracellular nucleases
    • Seper, A., et al. Vibrio cholerae evades neutrophil extracellular traps by the activity of two extracellular nucleases. PLoS Pathog. 9, e1003614 (2013)
    • (2013) PLoS Pathog , vol.9 , pp. e1003614
    • Seper, A.1
  • 148
    • 84982104146 scopus 로고    scopus 로고
    • Yersinia enterocolitica-mediated degradation of neutrophil extracellular traps (NETs
    • Mllerherm, H., et al. Yersinia enterocolitica-mediated degradation of neutrophil extracellular traps (NETs). FEMS Microbiology Letters 362, fnv192 (2015)
    • (2015) FEMS Microbiology Letters , vol.362 , pp. fnv192
    • Mllerherm, H.1
  • 149
    • 84936884538 scopus 로고    scopus 로고
    • A thermonuclease of Neisseria gonorrhoeae enhances bacterial escape from killing by neutrophil extracellular traps
    • Juneau, R. A., Stevens, J. S., Apicella, M. A., Criss, A. K. A thermonuclease of Neisseria gonorrhoeae enhances bacterial escape from killing by neutrophil extracellular traps. J. Infect. Dis. 212, 316-324 (2015)
    • (2015) J. Infect. Dis , vol.212 , pp. 316-324
    • Juneau, R.A.1    Stevens, J.S.2    Apicella, M.A.3    Criss, A.K.4
  • 150
    • 68049125271 scopus 로고    scopus 로고
    • Survival of bacterial biofilms within neutrophil extracellular traps promotes nontypeable Haemophilus influenzae persistence in the chinchilla model for otitis media
    • Hong, W., Juneau, R. A., Pang, B., Swords, W. E. Survival of bacterial biofilms within neutrophil extracellular traps promotes nontypeable Haemophilus influenzae persistence in the chinchilla model for otitis media. J. Innate Immun. 1, 215-224 (2009)
    • (2009) J. Innate Immun , vol.1 , pp. 215-224
    • Hong, W.1    Juneau, R.A.2    Pang, B.3    Swords, W.E.4
  • 151
    • 84903692703 scopus 로고    scopus 로고
    • Regulation of biofilm formation in Pseudomonas and Burkholderia species
    • Fazli, M., et al. Regulation of biofilm formation in Pseudomonas and Burkholderia species. Environ. Microbiol. 16, 1961-1981 (2014)
    • (2014) Environ. Microbiol , vol.16 , pp. 1961-1981
    • Fazli, M.1
  • 152
    • 65649114348 scopus 로고    scopus 로고
    • Streptococcus pneumoniae forms surface-attached communities in the middle ear of experimentally infected chinchillas
    • Reid, S. D., et al. Streptococcus pneumoniae forms surface-attached communities in the middle ear of experimentally infected chinchillas. J. Infect. Dis. 199, 786-794 (2009)
    • (2009) J. Infect. Dis , vol.199 , pp. 786-794
    • Reid, S.D.1
  • 153
    • 34047259058 scopus 로고    scopus 로고
    • Capsule and D-alanylated lipoteichoic acids protect Streptococcus pneumoniae against neutrophil extracellular traps
    • Wartha, F., et al. Capsule and D-alanylated lipoteichoic acids protect Streptococcus pneumoniae against neutrophil extracellular traps. Cell. Microbiol. 9, 1162-1171 (2007)
    • (2007) Cell. Microbiol , vol.9 , pp. 1162-1171
    • Wartha, F.1
  • 154
    • 79952159557 scopus 로고    scopus 로고
    • M protein and hyaluronic acid capsule are essential for in vivo selection of covRS mutations characteristic of invasive serotype M1T1 group A Streptococcus
    • Cole, J. N., et al. M protein and hyaluronic acid capsule are essential for in vivo selection of covRS mutations characteristic of invasive serotype M1T1 group A Streptococcus. mBio 1, e00191 (2010)
    • (2010) MBio , vol.1 , pp. e00191
    • Cole, J.N.1
  • 155
    • 84964318498 scopus 로고    scopus 로고
    • Interaction of bacterial exotoxins with neutrophil extracellular traps: Impact for the infected host
    • Kockritz-Blickwede, von, M., Blodkamp, S., Nizet, V. Interaction of bacterial exotoxins with neutrophil extracellular traps: impact for the infected host. Front. Microbiol. 7, 402 (2016)
    • (2016) Front. Microbiol. , vol.7 , pp. 402
    • Von Kockritz-Blickwede, M.1    Blodkamp, S.2    Nizet, V.3
  • 157
    • 84967189059 scopus 로고    scopus 로고
    • Evasion and interference: Intracellular pathogens modulate caspase-dependent inflammatory responses
    • Stewart, M. K., Cookson, B. T. Evasion and interference: intracellular pathogens modulate caspase-dependent inflammatory responses. Nat. Rev. Microbiol. 14, 346-359 (2016)
    • (2016) Nat. Rev. Microbiol , vol.14 , pp. 346-359
    • Stewart, M.K.1    Cookson, B.T.2
  • 159
    • 84876416949 scopus 로고    scopus 로고
    • Glanders in animals: A review on epidemiology, clinical presentation, diagnosis and countermeasures
    • Khan, I., et al. Glanders in animals: a review on epidemiology, clinical presentation, diagnosis and countermeasures. Transbound Emerg. Dis. 60, 204-221 (2013)
    • (2013) Transbound Emerg. Dis , vol.60 , pp. 204-221
    • Khan, I.1
  • 160
    • 79952780505 scopus 로고    scopus 로고
    • Functional complementation between FADD and RIP1 in embryos and lymphocytes
    • Zhang, H., et al. Functional complementation between FADD and RIP1 in embryos and lymphocytes. Nature 471, 373-376 (2011)
    • (2011) Nature , vol.471 , pp. 373-376
    • Zhang, H.1
  • 161
    • 84861712290 scopus 로고    scopus 로고
    • Survival function of the FADD-CASPASE-8-cFLIPL complex
    • Dillon, C. P., et al. Survival function of the FADD-CASPASE-8-cFLIPL complex. Cell Rep. 1, 401-407 (2012)
    • (2012) Cell Rep , vol.1 , pp. 401-407
    • Dillon, C.P.1
  • 162
    • 84879596906 scopus 로고    scopus 로고
    • K+ efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter
    • Mu?oz-Planillo, R., et al. K+ efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity 38, 1142-1153 (2013)
    • (2013) Immunity , vol.38 , pp. 1142-1153
    • Muoz-Planillo, R.1
  • 163
    • 84884332722 scopus 로고    scopus 로고
    • Mechanisms of NOD-like receptor-associated inflammasome activation
    • Wen, H., Miao, E. A., Ting, J. P.-Y. Mechanisms of NOD-like receptor-associated inflammasome activation. Immunity 39, 432-441 (2013)
    • (2013) Immunity , vol.39 , pp. 432-441
    • Wen, H.1    Miao, E.A.2    Ting, J.P.-Y.3
  • 164
    • 84943200249 scopus 로고    scopus 로고
    • Caspase-11 activates a canonical NLRP3 inflammasome by promoting K+ efflux
    • R?hl, S., Broz, P. Caspase-11 activates a canonical NLRP3 inflammasome by promoting K+ efflux. Eur. J. Immunol. 45, 2927-2936 (2015)
    • (2015) Eur. J. Immunol , vol.45 , pp. 2927-2936
    • Rhl, S.1    Broz, P.2
  • 165
    • 84943198707 scopus 로고    scopus 로고
    • Caspase-4 mediates non-canonical activation of the NLRP3 inflammasome in human myeloid cells
    • Schmid-Burgk, J. L., et al. Caspase-4 mediates non-canonical activation of the NLRP3 inflammasome in human myeloid cells. Eur. J. Immunol. 45, 2911-2917 (2015)
    • (2015) Eur. J. Immunol , vol.45 , pp. 2911-2917
    • Schmid-Burgk, J.L.1
  • 166
    • 84911192502 scopus 로고    scopus 로고
    • RNA viruses promote activation of the NLRP3 inflammasome through a RIP1-RIP3-DRP1 signaling pathway
    • Wang, X., et al. RNA viruses promote activation of the NLRP3 inflammasome through a RIP1-RIP3-DRP1 signaling pathway. Nat. Immunol. 15, 1126-1133 (2014)
    • (2014) Nat. Immunol , vol.15 , pp. 1126-1133
    • Wang, X.1
  • 167
    • 84870275730 scopus 로고    scopus 로고
    • Extensive evolutionary and functional diversity among mammalian AIM2-like receptors
    • Brunette, R. L., et al. Extensive evolutionary and functional diversity among mammalian AIM2-like receptors. J. Exp. Med. 209, 1969-1983 (2012)
    • (2012) J. Exp. Med , vol.209 , pp. 1969-1983
    • Brunette, R.L.1
  • 168
    • 84907270863 scopus 로고    scopus 로고
    • Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome
    • Xu, H., et al. Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome. Nature 513, 237-241 (2014)
    • (2014) Nature , vol.513 , pp. 237-241
    • Xu, H.1
  • 169
    • 80053349020 scopus 로고    scopus 로고
    • The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
    • Zhao, Y., et al. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature 477, 596-600 (2011)
    • (2011) Nature , vol.477 , pp. 596-600
    • Zhao, Y.1
  • 170
    • 80053379974 scopus 로고    scopus 로고
    • Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
    • Kofoed, E. M., Vance, R. E. Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature 477, 592-595 (2011)
    • (2011) Nature , vol.477 , pp. 592-595
    • Kofoed, E.M.1    Vance, R.E.2
  • 171
    • 84861214708 scopus 로고    scopus 로고
    • Anthrax lethal factor cleavage of nlrp1 is required for activation of the inflammasome
    • Levinsohn, J. L., et al. Anthrax lethal factor cleavage of nlrp1 is required for activation of the inflammasome. PLoS Pathog. 8, e1002638 (2012)
    • (2012) PLoS Pathog , vol.8 , pp. e1002638
    • Levinsohn, J.L.1
  • 172
    • 84879508269 scopus 로고    scopus 로고
    • Direct proteolytic cleavage of NLRP1B is necessary and sufficient for inflammasome activation by anthrax lethal factor
    • Chavarr?a-Smith, J., Vance, R. E. Direct proteolytic cleavage of NLRP1B is necessary and sufficient for inflammasome activation by anthrax lethal factor. PLoS Pathog. 9, e1003452 (2013)
    • (2013) PLoS Pathog , vol.9 , pp. e1003452
    • Chavarra-Smith, J.1    Vance, R.E.2
  • 173
    • 4344622049 scopus 로고    scopus 로고
    • Signaling of apoptosis through TLRs critically involves toll/IL-1 receptor domain-containing adapter inducing IFN-beta, but not MyD88, in bacteria-infected murine macrophages
    • Ruckdeschel, K., et al. Signaling of apoptosis through TLRs critically involves toll/IL-1 receptor domain-containing adapter inducing IFN-beta, but not MyD88, in bacteria-infected murine macrophages. J. Immunol. 173, 3320-3328 (2004)
    • (2004) J. Immunol , vol.173 , pp. 3320-3328
    • Ruckdeschel, K.1
  • 174
    • 2442605662 scopus 로고    scopus 로고
    • Mechanisms of the TRIF-induced interferon-stimulated response element and NF-?B activation and apoptosis pathways
    • Han, K.-J., et al. Mechanisms of the TRIF-induced interferon-stimulated response element and NF-?B activation and apoptosis pathways. J. Biol. Chem. 279, 15652-15661 (2004)
    • (2004) J. Biol. Chem , vol.279 , pp. 15652-15661
    • Han, K.-J.1
  • 175
    • 17144413785 scopus 로고    scopus 로고
    • Apoptosis induced by the toll-like receptor adaptor TRIF is dependent on its receptor interacting protein homotypic interaction motif
    • 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)
    • (2005) J. Immunol , vol.174 , pp. 4942-4952
    • Kaiser, W.J.1    Offermann, M.K.2
  • 176
    • 0033214236 scopus 로고    scopus 로고
    • Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis
    • Lin, Y., Devin, A., Rodriguez, Y., Liu, Z. G. Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev. 13, 2514-2526 (1999)
    • (1999) Genes Dev , vol.13 , pp. 2514-2526
    • Lin, Y.1    Devin, A.2    Rodriguez, Y.3    Liu, Z.G.4
  • 177
    • 34548437549 scopus 로고    scopus 로고
    • Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
    • Feng, S., et al. Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain. Cell. Signall. 19, 2056-2067 (2007)
    • (2007) Cell. Signall , vol.19 , pp. 2056-2067
    • Feng, S.1
  • 178
    • 79960922705 scopus 로고    scopus 로고
    • CIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms
    • Feoktistova, M., et al. cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol. Cell 43, 449-463 (2011)
    • (2011) Mol. Cell , vol.43 , pp. 449-463
    • Feoktistova, M.1
  • 179
    • 84055181328 scopus 로고    scopus 로고
    • Toll-like receptors activate programmed necrosis in macrophages through a receptor-interacting kinase-3-mediated pathway
    • He, S., Liang, Y., Shao, F., Wang, X. Toll-like receptors activate programmed necrosis in macrophages through a receptor-interacting kinase-3-mediated pathway. Proc. Natl Acad. Sci. USA 108, 20054-20059 (2011)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 20054-20059
    • He, S.1    Liang, Y.2    Shao, F.3    Wang, X.4
  • 180
    • 84886656964 scopus 로고    scopus 로고
    • Toll-like receptor 3-mediated necrosis via TRIF RIP3, and MLKL
    • Kaiser, W. J., et al. Toll-like receptor 3-mediated necrosis via TRIF, RIP3, and MLKL. J. Biol. Chem. 288, 31268-31279 (2013)
    • (2013) J. Biol. Chem , vol.288 , pp. 31268-31279
    • Kaiser, W.J.1


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