메뉴 건너뛰기




Volumn 26, Issue 1, 2019, Pages 99-114

Pyroptosis versus necroptosis: similarities, differences, and crosstalk

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BIOLOGICAL FACTOR; CELL MEMBRANE PROTEIN; CRYOPYRIN; DAMAGE ASSOCIATED MOLECULAR PATTERN; GASDERMIN D; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HIGH MOBILITY GROUP B1 PROTEIN; INFLAMMASOME; INTERLEUKIN 1ALPHA; INTERLEUKIN 33; MITOCHONDRIAL DNA; MIXED LINEAGE KINASE DOMAIN LIKE PSEUDOKINASE; PROTEIN ASC; PROTEIN S 100; UNCLASSIFIED DRUG; URATE; ALARMIN; CYTOKINE; GSDMD PROTEIN, HUMAN; INTERLEUKIN 1BETA CONVERTING ENZYME; MLKL PROTEIN, HUMAN; PHOSPHATE BINDING PROTEIN; PROTEIN KINASE; SIGNAL PEPTIDE;

EID: 85055349234     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/s41418-018-0212-6     Document Type: Review
Times cited : (759)

References (168)
  • 1
    • 0001139444 scopus 로고
    • Programmed cell death--I. Cytology of degeneration in the intersegmental muscles of the Pernyi silkmoth
    • COI: 1:CAS:528:DyaF2MXmvVGhsQ%3D%3D
    • Lockshin RA, Williams CM. Programmed cell death--I. Cytology of degeneration in the intersegmental muscles of the Pernyi silkmoth. J Insect Physiol. 1965;11:123–33
    • (1965) J Insect Physiol , vol.11 , pp. 123-133
    • Lockshin, R.A.1    Williams, C.M.2
  • 2
    • 0015383455 scopus 로고
    • Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics
    • COI: 1:STN:280:DyaE3s%2FgsFSksw%3D%3D, PID: 4561027
    • Kerr JF, Wyllie AH, Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer. 1972;26:239–57
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 3
    • 85037705823 scopus 로고    scopus 로고
    • Autophagy induced during apoptosis degrades mitochondria and inhibits type I interferon secretion
    • Lindqvist LM, Frank D, McArthur K, Dite TA, Lazarou M, Oakhill JS, et al. Autophagy induced during apoptosis degrades mitochondria and inhibits type I interferon secretion. Cell Death Differ 2017;25:782–794
    • (2017) Cell Death Differ , vol.25 , pp. 782-794
    • Lindqvist, L.M.1    Frank, D.2    McArthur, K.3    Dite, T.A.4    Lazarou, M.5    Oakhill, J.S.6
  • 4
    • 84919884654 scopus 로고    scopus 로고
    • Apoptotic caspases suppress mtDNA-induced STING-mediated type I IFN production
    • COI: 1:CAS:528:DC%2BC2MXnslKqtA%3D%3D, PID: 25525874
    • White MJ, McArthur K, Metcalf D, Lane RM, Cambier JC, Herold MJ, et al. Apoptotic caspases suppress mtDNA-induced STING-mediated type I IFN production. Cell. 2014;159:1549–62
    • (2014) Cell , vol.159 , pp. 1549-1562
    • White, M.J.1    McArthur, K.2    Metcalf, D.3    Lane, R.M.4    Cambier, J.C.5    Herold, M.J.6
  • 5
    • 84919898250 scopus 로고    scopus 로고
    • Apoptotic caspases prevent the induction of type I interferons by mitochondrial DNA
    • COI: 1:CAS:528:DC%2BC2MXnslKqtg%3D%3D, PID: 4272443
    • Rongvaux A, Jackson R, Harman CC, Li T, West AP, de Zoete MR, et al. Apoptotic caspases prevent the induction of type I interferons by mitochondrial DNA. Cell. 2014;159:1563–77
    • (2014) Cell , vol.159 , pp. 1563-1577
    • Rongvaux, A.1    Jackson, R.2    Harman, C.C.3    Li, T.4    West, A.P.5    de Zoete, M.R.6
  • 6
    • 84945568831 scopus 로고    scopus 로고
    • An apoptotic ‘eat me’ signal: phosphatidylserine exposure
    • COI: 1:CAS:528:DC%2BC2MXhs1Sht7vP
    • Segawa K, Nagata S. An apoptotic ‘eat me’ signal: phosphatidylserine exposure. Trends Cell Biol. 2015;25:639–50
    • (2015) Trends Cell Biol , vol.25 , pp. 639-650
    • Segawa, K.1    Nagata, S.2
  • 7
    • 85006741530 scopus 로고    scopus 로고
    • Necroptosis in development, inflammation and disease
    • COI: 1:CAS:528:DC%2BC28XitFahtrrJ, PID: 27999438
    • Weinlich R, Oberst A, Beere HM, Green DR. Necroptosis in development, inflammation and disease. Nat Rev Mol Cell Biol. 2017;18:127–36
    • (2017) Nat Rev Mol Cell Biol , vol.18 , pp. 127-136
    • Weinlich, R.1    Oberst, A.2    Beere, H.M.3    Green, D.R.4
  • 8
    • 84931377023 scopus 로고    scopus 로고
    • The diverse role of RIP kinases in necroptosis and inflammation
    • COI: 1:CAS:528:DC%2BC2MXht1OmtL3E
    • Silke J, Rickard JA, Gerlic M. The diverse role of RIP kinases in necroptosis and inflammation. Nat Immunol. 2015;16:689–97
    • (2015) Nat Immunol , vol.16 , pp. 689-697
    • Silke, J.1    Rickard, J.A.2    Gerlic, M.3
  • 9
    • 85017142478 scopus 로고    scopus 로고
    • A mechanistic understanding of pyroptosis: the fiery death triggered by invasive infection
    • Liu X, Lieberman J. A mechanistic understanding of pyroptosis: the fiery death triggered by invasive infection. Adv Immunol. 2017;135:81–117
    • (2017) Adv Immunol , vol.135 , pp. 81-117
    • Liu, X.1    Lieberman, J.2
  • 10
    • 80052626087 scopus 로고    scopus 로고
    • The NLRP3 inflammasome in health and disease: the good, the bad and the ugly
    • COI: 1:CAS:528:DC%2BC3MXhtlSks7nK, PID: 3193914
    • Menu P, Vince JE. The NLRP3 inflammasome in health and disease: the good, the bad and the ugly. Clin Exp Immunol. 2011;166:1–15
    • (2011) Clin Exp Immunol , vol.166 , pp. 1-15
    • Menu, P.1    Vince, J.E.2
  • 11
    • 84981736924 scopus 로고    scopus 로고
    • The pseudokinase MLKL and the kinase RIPK3 have distinct roles in autoimmune disease caused by loss of death-receptor-induced apoptosis
    • COI: 1:CAS:528:DC%2BC28Xhtlaksb7L, PID: 5040700
    • Alvarez-Diaz S, Dillon CP, Lalaoui N, Tanzer MC, Rodriguez DA, Lin A, et al. The pseudokinase MLKL and the kinase RIPK3 have distinct roles in autoimmune disease caused by loss of death-receptor-induced apoptosis. Immunity. 2016;45:513–26
    • (2016) Immunity , vol.45 , pp. 513-526
    • Alvarez-Diaz, S.1    Dillon, C.P.2    Lalaoui, N.3    Tanzer, M.C.4    Rodriguez, D.A.5    Lin, A.6
  • 12
    • 84935699564 scopus 로고    scopus 로고
    • Necroptosis suppresses inflammation via termination of TNF- or LPS-induced cytokine and chemokine production
    • COI: 1:CAS:528:DC%2BC2MXhs1Sju7s%3D, PID: 4495357
    • Kearney CJ, Cullen SP, Tynan GA, Henry CM, Clancy D, Lavelle EC, et al. Necroptosis suppresses inflammation via termination of TNF- or LPS-induced cytokine and chemokine production. Cell Death Differ. 2015;22:1313–27
    • (2015) Cell Death Differ , vol.22 , pp. 1313-1327
    • Kearney, C.J.1    Cullen, S.P.2    Tynan, G.A.3    Henry, C.M.4    Clancy, D.5    Lavelle, E.C.6
  • 13
    • 84904792729 scopus 로고    scopus 로고
    • The neutrophil NLRC4 inflammasome selectively promotes IL-1beta maturation without pyroptosis during acute Salmonella challenge
    • COI: 1:CAS:528:DC%2BC2cXhtFyjtLzL
    • Chen KW, Gross CJ, Sotomayor FV, Stacey KJ, Tschopp J, Sweet MJ, et al. The neutrophil NLRC4 inflammasome selectively promotes IL-1beta maturation without pyroptosis during acute Salmonella challenge. Cell Rep. 2014;8:570–82
    • (2014) Cell Rep , vol.8 , pp. 570-582
    • Chen, K.W.1    Gross, C.J.2    Sotomayor, F.V.3    Stacey, K.J.4    Tschopp, J.5    Sweet, M.J.6
  • 14
    • 85043591156 scopus 로고    scopus 로고
    • Gasdermin D exerts anti-inflammatory effects by promoting neutrophil death
    • COI: 1:CAS:528:DC%2BC1cXkslSgtrs%3D, PID: 5878047
    • Kambara H, Liu F, Zhang X, Liu P, Bajrami B, Teng Y, et al. Gasdermin D exerts anti-inflammatory effects by promoting neutrophil death. Cell Rep. 2018;22:2924–36
    • (2018) Cell Rep , vol.22 , pp. 2924-2936
    • Kambara, H.1    Liu, F.2    Zhang, X.3    Liu, P.4    Bajrami, B.5    Teng, Y.6
  • 15
    • 85045460511 scopus 로고    scopus 로고
    • Caspase-8 deficiency in mouse embryos triggers chronic RIPK1-dependent activation of inflammatory genes, independently of RIPK3
    • COI: 1:CAS:528:DC%2BC1cXnvFClsrs%3D, PID: 5988659
    • Kang TB, Jeong JS, Yang SH, Kovalenko A, Wallach D. Caspase-8 deficiency in mouse embryos triggers chronic RIPK1-dependent activation of inflammatory genes, independently of RIPK3. Cell Death Differ. 2018;25:1107–17
    • (2018) Cell Death Differ , vol.25 , pp. 1107-1117
    • Kang, T.B.1    Jeong, J.S.2    Yang, S.H.3    Kovalenko, A.4    Wallach, D.5
  • 16
    • 84981703921 scopus 로고    scopus 로고
    • Necroptosis Promotes Staphylococcus aureus clearance by inhibiting excessive inflammatory signaling
    • COI: 1:CAS:528:DC%2BC28Xhtleis7%2FK, PID: 5001919
    • Kitur K, Wachtel S, Brown A, Wickersham M, Paulino F, Penaloza HF, et al. Necroptosis Promotes Staphylococcus aureus clearance by inhibiting excessive inflammatory signaling. Cell Rep. 2016;16:2219–30
    • (2016) Cell Rep , vol.16 , pp. 2219-2230
    • Kitur, K.1    Wachtel, S.2    Brown, A.3    Wickersham, M.4    Paulino, F.5    Penaloza, H.F.6
  • 17
    • 0026635783 scopus 로고
    • Shigella flexneri induces apoptosis in infected macrophages
    • COI: 1:STN:280:DyaK38zhtVGqtw%3D%3D
    • Zychlinsky A, Prevost MC, Sansonetti PJ. Shigella flexneri induces apoptosis in infected macrophages. Nature. 1992;358:167–9
    • (1992) Nature , vol.358 , pp. 167-169
    • Zychlinsky, A.1    Prevost, M.C.2    Sansonetti, P.J.3
  • 18
    • 0035283318 scopus 로고    scopus 로고
    • Pro-inflammatory programmed cell death
    • COI: 1:CAS:528:DC%2BD3MXlvFenu7g%3D
    • Cookson BT, Brennan MA. Pro-inflammatory programmed cell death. Trends Microbiol. 2001;9:113–4
    • (2001) Trends Microbiol , vol.9 , pp. 113-114
    • Cookson, B.T.1    Brennan, M.A.2
  • 19
    • 80455176839 scopus 로고    scopus 로고
    • Non-canonical inflammasome activation targets caspase-11
    • COI: 1:CAS:528:DC%2BC3MXhtlWksr7E
    • Kayagaki N, Warming S, Lamkanfi M, Vande Walle L, Louie S, Dong J, et al. Non-canonical inflammasome activation targets caspase-11. Nature. 2011;479:117–21
    • (2011) Nature , vol.479 , pp. 117-121
    • Kayagaki, N.1    Warming, S.2    Lamkanfi, M.3    Vande Walle, L.4    Louie, S.5    Dong, J.6
  • 20
    • 84906571225 scopus 로고    scopus 로고
    • Inflammatory caspases are innate immune receptors for intracellular LPS
    • COI: 1:CAS:528:DC%2BC2cXhslaqs77F, PID: 25119034
    • Shi J, Zhao Y, Wang Y, Gao W, Ding J, Li P, et al. Inflammatory caspases are innate immune receptors for intracellular LPS. Nature. 2014;514:187–92
    • (2014) Nature , vol.514 , pp. 187-192
    • Shi, J.1    Zhao, Y.2    Wang, Y.3    Gao, W.4    Ding, J.5    Li, P.6
  • 21
    • 85022210909 scopus 로고    scopus 로고
    • Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a gasdermin
    • COI: 1:CAS:528:DC%2BC2sXhtFaqt7nN
    • Wang Y, Gao W, Shi X, Ding J, Liu W, He H, et al. Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a gasdermin. Nature. 2017;547:99–103
    • (2017) Nature , vol.547 , pp. 99-103
    • Wang, Y.1    Gao, W.2    Shi, X.3    Ding, J.4    Liu, W.5    He, H.6
  • 22
    • 85008419254 scopus 로고    scopus 로고
    • Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death
    • COI: 1:CAS:528:DC%2BC2sXislWnsQ%3D%3D, PID: 5216131
    • Rogers C, Fernandes-Alnemri T, Mayes L, Alnemri D, Cingolani G, Alnemri ES. Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death. Nat Commun. 2017;8:14128
    • (2017) Nat Commun , vol.8
    • Rogers, C.1    Fernandes-Alnemri, T.2    Mayes, L.3    Alnemri, D.4    Cingolani, G.5    Alnemri, E.S.6
  • 23
    • 84942892037 scopus 로고    scopus 로고
    • Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
    • COI: 1:CAS:528:DC%2BC2MXhsFersL3M
    • Shi J, Zhao Y, Wang K, Shi X, Wang Y, Huang H, et al. Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature. 2015;526:660–5
    • (2015) Nature , vol.526 , pp. 660-665
    • Shi, J.1    Zhao, Y.2    Wang, K.3    Shi, X.4    Wang, Y.5    Huang, H.6
  • 24
    • 84942856523 scopus 로고    scopus 로고
    • Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
    • COI: 1:CAS:528:DC%2BC2MXhslCnu77N
    • Kayagaki N, Stowe IB, Lee BL, O’Rourke K, Anderson K, Warming S, et al. Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling. Nature. 2015;526:666–71
    • (2015) Nature , vol.526 , pp. 666-671
    • Kayagaki, N.1    Stowe, I.B.2    Lee, B.L.3    O’Rourke, K.4    Anderson, K.5    Warming, S.6
  • 25
    • 84978419608 scopus 로고    scopus 로고
    • Pore-forming activity and structural autoinhibition of the gasdermin family
    • COI: 1:CAS:528:DC%2BC28XpsVCqsLo%3D
    • Ding J, Wang K, Liu W, She Y, Sun Q, Shi J, et al. Pore-forming activity and structural autoinhibition of the gasdermin family. Nature. 2016;535:111–6
    • (2016) Nature , vol.535 , pp. 111-116
    • Ding, J.1    Wang, K.2    Liu, W.3    She, Y.4    Sun, Q.5    Shi, J.6
  • 27
    • 84982102736 scopus 로고    scopus 로고
    • GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death
    • COI: 1:CAS:528:DC%2BC28XhtFKktrjM, PID: 5010048
    • Sborgi L, Ruhl S, Mulvihill E, Pipercevic J, Heilig R, Stahlberg H, et al. GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death. EMBO J. 2016;35:1766–78
    • (2016) EMBO J , vol.35 , pp. 1766-1778
    • Sborgi, L.1    Ruhl, S.2    Mulvihill, E.3    Pipercevic, J.4    Heilig, R.5    Stahlberg, H.6
  • 28
    • 84978374487 scopus 로고    scopus 로고
    • Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores
    • COI: 1:CAS:528:DC%2BC28XhtFensL7K, PID: 5539988
    • Liu X, Zhang Z, Ruan J, Pan Y, Magupalli VG, Wu H, et al. Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores. Nature. 2016;535:153–8
    • (2016) Nature , vol.535 , pp. 153-158
    • Liu, X.1    Zhang, Z.2    Ruan, J.3    Pan, Y.4    Magupalli, V.G.5    Wu, H.6
  • 29
    • 84879596906 scopus 로고    scopus 로고
    • K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter
    • COI: 1:CAS:528:DC%2BC3sXhtVaitb3M, PID: 23809161
    • Munoz-Planillo R, Kuffa P, Martinez-Colon G, Smith BL, Rajendiran TM, Nunez G. K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity. 2013;38:1142–53
    • (2013) Immunity , vol.38 , pp. 1142-1153
    • Munoz-Planillo, R.1    Kuffa, P.2    Martinez-Colon, G.3    Smith, B.L.4    Rajendiran, T.M.5    Nunez, G.6
  • 30
    • 84943199941 scopus 로고    scopus 로고
    • NLRP3 inflammasome activation downstream of cytoplasmic LPS recognition by both caspase-4 and caspase-5
    • COI: 1:CAS:528:DC%2BC2MXhtlOgt7jJ
    • Baker PJ, Boucher D, Bierschenk D, Tebartz C, Whitney PG, D’Silva DB, et al. NLRP3 inflammasome activation downstream of cytoplasmic LPS recognition by both caspase-4 and caspase-5. Eur J Immunol. 2015;45:2918–26
    • (2015) Eur J Immunol , vol.45 , pp. 2918-2926
    • Baker, P.J.1    Boucher, D.2    Bierschenk, D.3    Tebartz, C.4    Whitney, P.G.5    D’Silva, D.B.6
  • 31
    • 78449269290 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria
    • COI: 1:CAS:528:DC%2BC3cXhtl2jtrrK, PID: 21057511
    • Miao EA, Leaf IA, Treuting PM, Mao DP, Dors M, Sarkar A, et al. Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat Immunol. 2010;11:1136–42
    • (2010) Nat Immunol , vol.11 , pp. 1136-1142
    • Miao, E.A.1    Leaf, I.A.2    Treuting, P.M.3    Mao, D.P.4    Dors, M.5    Sarkar, A.6
  • 32
    • 84988813074 scopus 로고    scopus 로고
    • Pyroptosis triggers pore-induced intracellular traps (PITs) that capture bacteria and lead to their clearance by efferocytosis
    • COI: 1:CAS:528:DC%2BC2sXhsVygtr0%3D, PID: 5030797
    • Jorgensen I, Zhang Y, Krantz BA, Miao EA. Pyroptosis triggers pore-induced intracellular traps (PITs) that capture bacteria and lead to their clearance by efferocytosis. J Exp Med. 2016;213:2113–28
    • (2016) J Exp Med , vol.213 , pp. 2113-2128
    • Jorgensen, I.1    Zhang, Y.2    Krantz, B.A.3    Miao, E.A.4
  • 33
    • 84976516826 scopus 로고    scopus 로고
    • Inflammasomes: mechanism of assembly, regulation and signalling
    • COI: 1:CAS:528:DC%2BC28Xps1Srt7k%3D, PID: 27291964
    • Broz P, Dixit VM. Inflammasomes: mechanism of assembly, regulation and signalling. Nat Rev Immunol. 2016;16:407–20
    • (2016) Nat Rev Immunol , vol.16 , pp. 407-420
    • Broz, P.1    Dixit, V.M.2
  • 34
    • 84958971929 scopus 로고    scopus 로고
    • NEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux
    • COI: 1:CAS:528:DC%2BC28XhsFyitbY%3D, PID: 4810788
    • He Y, Zeng MY, Yang D, Motro B, Nunez G. NEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux. Nature. 2016;530:354–7
    • (2016) Nature , vol.530 , pp. 354-357
    • He, Y.1    Zeng, M.Y.2    Yang, D.3    Motro, B.4    Nunez, G.5
  • 35
    • 85042868319 scopus 로고    scopus 로고
    • Caspase-1 self-cleavage is an intrinsic mechanism to terminate inflammasome activity
    • COI: 1:CAS:528:DC%2BC1cXhslakur7J, PID: 5839769
    • Boucher D, Monteleone M, Coll RC, Chen KW, Ross CM, Teo JL, et al. Caspase-1 self-cleavage is an intrinsic mechanism to terminate inflammasome activity. J Exp Med. 2018;215:827–40
    • (2018) J Exp Med , vol.215 , pp. 827-840
    • Boucher, D.1    Monteleone, M.2    Coll, R.C.3    Chen, K.W.4    Ross, C.M.5    Teo, J.L.6
  • 36
    • 85046620741 scopus 로고    scopus 로고
    • Extensive peptide and natural protein substrate screens reveal that mouse caspase-11 has much narrower substrate specificity than caspase-1
    • PID: 5936834
    • Ramirez MLG, Poreba M, Snipas SJ, Groborz K, Drag M, Salvesen GS. Extensive peptide and natural protein substrate screens reveal that mouse caspase-11 has much narrower substrate specificity than caspase-1. J Biol Chem. 2018;293:7058–67
    • (2018) J Biol Chem , vol.293 , pp. 7058-7067
    • Ramirez, M.L.G.1    Poreba, M.2    Snipas, S.J.3    Groborz, K.4    Drag, M.5    Salvesen, G.S.6
  • 37
    • 84943200249 scopus 로고    scopus 로고
    • Caspase-11 activates a canonical NLRP3 inflammasome by promoting K(+) efflux
    • Ruhl S, Broz P. Caspase-11 activates a canonical NLRP3 inflammasome by promoting K(+) efflux. Eur J Immunol. 2015;45:2927–36
    • (2015) Eur J Immunol , vol.45 , pp. 2927-2936
    • Ruhl, S.1    Broz, P.2
  • 38
    • 85011632943 scopus 로고    scopus 로고
    • Active MLKL triggers the NLRP3 inflammasome in a cell-intrinsic manner
    • COI: 1:CAS:528:DC%2BC2sXhtFars78%3D
    • Conos SA, Chen KW, De Nardo D, Hara H, Whitehead L, Nunez G, et al. Active MLKL triggers the NLRP3 inflammasome in a cell-intrinsic manner. Proc Natl Acad Sci USA. 2017;114:E961–E969
    • (2017) Proc Natl Acad Sci USA , vol.114 , pp. E961-E969
    • Conos, S.A.1    Chen, K.W.2    De Nardo, D.3    Hara, H.4    Whitehead, L.5    Nunez, G.6
  • 39
    • 85014931414 scopus 로고    scopus 로고
    • MLKL activation triggers NLRP3-mediated processing and release of IL-1beta independently of gasdermin-D
    • COI: 1:CAS:528:DC%2BC2sXjtVamtrY%3D, PID: 5321867
    • Gutierrez KD, Davis MA, Daniels BP, Olsen TM, Ralli-Jain P, Tait SW, et al. MLKL activation triggers NLRP3-mediated processing and release of IL-1beta independently of gasdermin-D. J Immunol. 2017;198:2156–64
    • (2017) J Immunol , vol.198 , pp. 2156-2164
    • Gutierrez, K.D.1    Davis, M.A.2    Daniels, B.P.3    Olsen, T.M.4    Ralli-Jain, P.5    Tait, S.W.6
  • 40
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • COI: 1:CAS:528:DC%2BD3cXoslyru74%3D, PID: 11101870
    • Holler N, Zaru R, Micheau O, Thome M, Attinger A, Valitutti S, et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat Immunol. 2000;1:489–95
    • (2000) Nat Immunol , vol.1 , pp. 489-495
    • Holler, N.1    Zaru, R.2    Micheau, O.3    Thome, M.4    Attinger, A.5    Valitutti, S.6
  • 41
    • 33644840693 scopus 로고    scopus 로고
    • Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
    • COI: 1:CAS:528:DC%2BD2MXls1OmsLg%3D, PID: 16408008
    • Degterev A, Huang Z, Boyce M, Li Y, Jagtap P, Mizushima N, et al. Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nat Chem Biol. 2005;1:112–9
    • (2005) Nat Chem Biol , vol.1 , pp. 112-119
    • Degterev, A.1    Huang, Z.2    Boyce, M.3    Li, Y.4    Jagtap, P.5    Mizushima, N.6
  • 43
    • 85017108918 scopus 로고    scopus 로고
    • ESCRT-III acts downstream of MLKL to regulate necroptotic cell death and its consequences
    • COI: 1:CAS:528:DC%2BC2sXlvVKiu7c%3D, PID: 5443414, e16
    • Gong YN, Guy C, Olauson H, Becker JU, Yang M, Fitzgerald P, et al. ESCRT-III acts downstream of MLKL to regulate necroptotic cell death and its consequences. Cell. 2017;169:286–300.e16
    • (2017) Cell , vol.169 , pp. 286-300
    • Gong, Y.N.1    Guy, C.2    Olauson, H.3    Becker, J.U.4    Yang, M.5    Fitzgerald, P.6
  • 44
    • 85021357052 scopus 로고    scopus 로고
    • Initiation and execution mechanisms of necroptosis: an overview
    • COI: 1:CAS:528:DC%2BC2sXhtVOjsLjL, PID: 28498367
    • Grootjans S, Vanden Berghe T, Vandenabeele P. Initiation and execution mechanisms of necroptosis: an overview. Cell Death Differ. 2017;24:1184–95
    • (2017) Cell Death Differ , vol.24 , pp. 1184-1195
    • Grootjans, S.1    Vanden Berghe, T.2    Vandenabeele, P.3
  • 45
    • 85045427291 scopus 로고    scopus 로고
    • The structure of the necrosome RIPK1-RIPK3 core, a human hetero-amyloid signaling complex
    • COI: 1:CAS:528:DC%2BC1cXotFejtrw%3D
    • Mompean M, Li W, Li J, Laage S, Siemer AB, Bozkurt G, et al. The structure of the necrosome RIPK1-RIPK3 core, a human hetero-amyloid signaling complex. Cell. 2018;173:1244–53.e10
    • (2018) Cell , vol.173 , pp. 1244-1253
    • Mompean, M.1    Li, W.2    Li, J.3    Laage, S.4    Siemer, A.B.5    Bozkurt, G.6
  • 46
    • 84862907788 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase
    • COI: 1:CAS:528:DC%2BC38XhtFKgsLY%3D
    • Sun L, Wang H, Wang Z, He S, Chen S, Liao D, et al. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell. 2012;148:213–27
    • (2012) Cell , vol.148 , pp. 213-227
    • Sun, L.1    Wang, H.2    Wang, Z.3    He, S.4    Chen, S.5    Liao, D.6
  • 47
    • 84859467770 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis
    • COI: 1:CAS:528:DC%2BC38XlslOjs70%3D
    • Zhao J, Jitkaew S, Cai Z, Choksi S, Li Q, Luo J, et al. Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis. Proc Natl Acad Sci USA. 2012;109:5322–7
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 5322-5327
    • Zhao, J.1    Jitkaew, S.2    Cai, Z.3    Choksi, S.4    Li, Q.5    Luo, J.6
  • 48
    • 84874263775 scopus 로고    scopus 로고
    • Necroptosis: the release of damage-associated molecular patterns and its physiological relevance
    • COI: 1:CAS:528:DC%2BC3sXjtVeht7k%3D, PID: 23438821
    • Kaczmarek A, Vandenabeele P, Krysko DV. Necroptosis: the release of damage-associated molecular patterns and its physiological relevance. Immunity. 2013;38:209–23
    • (2013) Immunity , vol.38 , pp. 209-223
    • Kaczmarek, A.1    Vandenabeele, P.2    Krysko, D.V.3
  • 50
    • 85000542319 scopus 로고    scopus 로고
    • RIPK1 counteracts ZBP1-mediated necroptosis to inhibit inflammation
    • COI: 1:CAS:528:DC%2BC28XhvFylsLjK, PID: 5755685
    • Lin J, Kumari S, Kim C, Van TM, Wachsmuth L, Polykratis A, et al. RIPK1 counteracts ZBP1-mediated necroptosis to inhibit inflammation. Nature. 2016;540:124–8
    • (2016) Nature , vol.540 , pp. 124-128
    • Lin, J.1    Kumari, S.2    Kim, C.3    Van, T.M.4    Wachsmuth, L.5    Polykratis, A.6
  • 51
    • 84888805473 scopus 로고    scopus 로고
    • More to life than death: molecular determinants of necroptotic and non-necroptotic RIP3 kinase signaling
    • COI: 1:CAS:528:DC%2BC2cXislKrtrk%3D
    • Khan N, Lawlor KE, Murphy JM, Vince JE. More to life than death: molecular determinants of necroptotic and non-necroptotic RIP3 kinase signaling. Curr Opin Immunol. 2014;26:76–89
    • (2014) Curr Opin Immunol , vol.26 , pp. 76-89
    • Khan, N.1    Lawlor, K.E.2    Murphy, J.M.3    Vince, J.E.4
  • 52
    • 85006760644 scopus 로고    scopus 로고
    • Controlled detonation: evolution of necroptosis in pathogen defense
    • COI: 1:CAS:528:DC%2BC28XitFCmsLvE, PID: 27909314
    • Brault M, Oberst A. Controlled detonation: evolution of necroptosis in pathogen defense. Immunol Cell Biol. 2017;95:131–6
    • (2017) Immunol Cell Biol , vol.95 , pp. 131-136
    • Brault, M.1    Oberst, A.2
  • 53
    • 85040963891 scopus 로고    scopus 로고
    • Targeting apoptosis pathways in infections
    • COI: 1:CAS:528:DC%2BC1cXjtlyqur8%3D
    • Naderer T, Fulcher MC. Targeting apoptosis pathways in infections. J Leukoc Biol. 2018;103:275–85
    • (2018) J Leukoc Biol , vol.103 , pp. 275-285
    • Naderer, T.1    Fulcher, M.C.2
  • 55
    • 79952810024 scopus 로고    scopus 로고
    • Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis
    • COI: 1:CAS:528:DC%2BC3MXis1Crsrs%3D, PID: 3077893
    • Oberst A, Dillon CP, Weinlich R, McCormick LL, Fitzgerald P, Pop C, et al. Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis. Nature. 2011;471:363–7
    • (2011) Nature , vol.471 , pp. 363-367
    • Oberst, A.1    Dillon, C.P.2    Weinlich, R.3    McCormick, L.L.4    Fitzgerald, P.5    Pop, C.6
  • 56
    • 84891343566 scopus 로고    scopus 로고
    • Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis
    • COI: 1:CAS:528:DC%2BC3sXhvV2hsb3E, PID: 24316671
    • Cai Z, Jitkaew S, Zhao J, Chiang HC, Choksi S, Liu J, et al. Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nat Cell Biol. 2014;16:55–65
    • (2014) Nat Cell Biol , vol.16 , pp. 55-65
    • Cai, Z.1    Jitkaew, S.2    Zhao, J.3    Chiang, H.C.4    Choksi, S.5    Liu, J.6
  • 57
    • 84891739370 scopus 로고    scopus 로고
    • Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death
    • COI: 1:CAS:528:DC%2BC2cXpsVyr, PID: 24366341
    • Chen X, Li W, Ren J, Huang D, He WT, Song Y, et al. Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death. Cell Res. 2014;24:105–21
    • (2014) Cell Res , vol.24 , pp. 105-121
    • Chen, X.1    Li, W.2    Ren, J.3    Huang, D.4    He, W.T.5    Song, Y.6
  • 58
    • 84908072785 scopus 로고    scopus 로고
    • Activation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell death
    • COI: 1:CAS:528:DC%2BC2cXhs1yhtLnJ
    • Hildebrand JM, Tanzer MC, Lucet IS, Young SN, Spall SK, Sharma P, et al. Activation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell death. Proc Natl Acad Sci USA. 2014;111:15072–7
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 15072-15077
    • Hildebrand, J.M.1    Tanzer, M.C.2    Lucet, I.S.3    Young, S.N.4    Spall, S.K.5    Sharma, P.6
  • 59
    • 84984822442 scopus 로고    scopus 로고
    • Pyroptosis is driven by non-selective gasdermin-D pore and its morphology is different from MLKL channel-mediated necroptosis
    • COI: 1:CAS:528:DC%2BC28XhsVels7zE, PID: 5034106
    • Chen X, He WT, Hu L, Li J, Fang Y, Wang X, et al. Pyroptosis is driven by non-selective gasdermin-D pore and its morphology is different from MLKL channel-mediated necroptosis. Cell Res. 2016;26:1007–20
    • (2016) Cell Res , vol.26 , pp. 1007-1020
    • Chen, X.1    He, W.T.2    Hu, L.3    Li, J.4    Fang, Y.5    Wang, X.6
  • 60
    • 85045422074 scopus 로고    scopus 로고
    • Single-cell analysis of pyroptosis dynamics reveals conserved GSDMD-mediated subcellular events that precede plasma membrane rupture
    • de Vasconcelos NM, Van Opdenbosch N, Van Gorp H, Parthoens E, Lamkanfi M. Single-cell analysis of pyroptosis dynamics reveals conserved GSDMD-mediated subcellular events that precede plasma membrane rupture. Cell Death Differ 2018 10.1038/s41418-018-0106-7
    • (2018) Cell Death Differ
    • de Vasconcelos, N.M.1    van Opdenbosch, N.2    van Gorp, H.3    Parthoens, E.4    Lamkanfi, M.5
  • 61
    • 85061560626 scopus 로고    scopus 로고
    • The pore-forming protein gasdermin D regulates interleukin-1 secretion from living macrophages
    • COI: 1:CAS:528:DC%2BC2sXhvVOrurnN, e6
    • Evavold CL, Ruan J, Tan Y, Xia S, Wu H, Kagan JC. The pore-forming protein gasdermin D regulates interleukin-1 secretion from living macrophages. Immunity. 2018;48:35–44.e6
    • (2018) Immunity , vol.48 , pp. 35-44
    • Evavold, C.L.1    Ruan, J.2    Tan, Y.3    Xia, S.4    Wu, H.5    Kagan, J.C.6
  • 62
    • 85040539132 scopus 로고    scopus 로고
    • The gasdermin-D pore acts as a conduit for IL-1beta secretion in mice
    • COI: 1:CAS:528:DC%2BC1cXntlCltw%3D%3D
    • Heilig R, Dick MS, Sborgi L, Meunier E, Hiller S, Broz P. The gasdermin-D pore acts as a conduit for IL-1beta secretion in mice. Eur J Immunol. 2018;48:584–92
    • (2018) Eur J Immunol , vol.48 , pp. 584-592
    • Heilig, R.1    Dick, M.S.2    Sborgi, L.3    Meunier, E.4    Hiller, S.5    Broz, P.6
  • 63
    • 84983776563 scopus 로고    scopus 로고
    • Active caspase-1 induces plasma membrane pores that precede pyroptotic lysis and are blocked by lanthanides
    • COI: 1:CAS:528:DC%2BC28Xht1yrtrbM, PID: 4976007
    • Russo HM, Rathkey J, Boyd-Tressler A, Katsnelson MA, Abbott DW, Dubyak GR. Active caspase-1 induces plasma membrane pores that precede pyroptotic lysis and are blocked by lanthanides. J Immunol. 2016;197:1353–67
    • (2016) J Immunol , vol.197 , pp. 1353-1367
    • Russo, H.M.1    Rathkey, J.2    Boyd-Tressler, A.3    Katsnelson, M.A.4    Abbott, D.W.5    Dubyak, G.R.6
  • 64
    • 84978476553 scopus 로고    scopus 로고
    • Cell death is not essential for caspase-1-mediated interleukin-1beta activation and secretion
    • COI: 1:CAS:528:DC%2BC28XhslSnsbnL, PID: 5071572
    • Conos SA, Lawlor KE, Vaux DL, Vince JE, Lindqvist LM. Cell death is not essential for caspase-1-mediated interleukin-1beta activation and secretion. Cell Death Differ. 2016;23:1827–38
    • (2016) Cell Death Differ , vol.23 , pp. 1827-1838
    • Conos, S.A.1    Lawlor, K.E.2    Vaux, D.L.3    Vince, J.E.4    Lindqvist, L.M.5
  • 65
    • 84962219519 scopus 로고    scopus 로고
    • Human monocytes engage an alternative inflammasome pathway
    • COI: 1:CAS:528:DC%2BC28XltVejtr0%3D, PID: 27037191
    • Gaidt MM, Ebert TS, Chauhan D, Schmidt T, Schmid-Burgk JL, Rapino F, et al. Human monocytes engage an alternative inflammasome pathway. Immunity. 2016;44:833–46
    • (2016) Immunity , vol.44 , pp. 833-846
    • Gaidt, M.M.1    Ebert, T.S.2    Chauhan, D.3    Schmidt, T.4    Schmid-Burgk, J.L.5    Rapino, F.6
  • 66
    • 85050821468 scopus 로고    scopus 로고
    • Interleukin-1beta maturation triggers its relocation to the plasma membrane for gasdermin-D-dependent and -independent secretion
    • COI: 1:CAS:528:DC%2BC1cXhsVKrtLbP
    • Monteleone M, Stanley AC, Chen KW, Brown DL, Bezbradica JS, von Pein JB, et al. Interleukin-1beta maturation triggers its relocation to the plasma membrane for gasdermin-D-dependent and -independent secretion. Cell Rep. 2018;24:1425–33
    • (2018) Cell Rep , vol.24 , pp. 1425-1433
    • Monteleone, M.1    Stanley, A.C.2    Chen, K.W.3    Brown, D.L.4    Bezbradica, J.S.5    von Pein, J.B.6
  • 67
    • 85046437366 scopus 로고    scopus 로고
    • Cryo-EM structure of the gasdermin A3 membrane pore
    • COI: 1:CAS:528:DC%2BC1cXptVWku78%3D
    • Ruan J, Xia S, Liu X, Lieberman J, Wu H. Cryo-EM structure of the gasdermin A3 membrane pore. Nature. 2018;557:62–7
    • (2018) Nature , vol.557 , pp. 62-67
    • Ruan, J.1    Xia, S.2    Liu, X.3    Lieberman, J.4    Wu, H.5
  • 68
    • 84898027331 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3
    • COI: 1:CAS:528:DC%2BC2cXls1emsro%3D, PID: 24703947
    • Wang H, Sun L, Su L, Rizo J, Liu L, Wang LF, et al. Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3. Mol Cell. 2014;54:133–46
    • (2014) Mol Cell , vol.54 , pp. 133-146
    • Wang, H.1    Sun, L.2    Su, L.3    Rizo, J.4    Liu, L.5    Wang, L.F.6
  • 69
    • 84901280344 scopus 로고    scopus 로고
    • MLKL compromises plasma membrane integrity by binding to phosphatidylinositol phosphates
    • COI: 1:CAS:528:DC%2BC2cXnslGnu78%3D, PID: 24813885
    • Dondelinger Y, Declercq W, Montessuit S, Roelandt R, Goncalves A, Bruggeman I, et al. MLKL compromises plasma membrane integrity by binding to phosphatidylinositol phosphates. Cell Rep. 2014;7:971–81
    • (2014) Cell Rep , vol.7 , pp. 971-981
    • Dondelinger, Y.1    Declercq, W.2    Montessuit, S.3    Roelandt, R.4    Goncalves, A.5    Bruggeman, I.6
  • 70
    • 84958122344 scopus 로고    scopus 로고
    • Sequential engagement of distinct MLKL phosphatidylinositol-binding sites executes necroptosis
    • COI: 1:CAS:528:DC%2BC28XitFCktbw%3D, PID: 4769881
    • Quarato G, Guy CS, Grace CR, Llambi F, Nourse A, Rodriguez DA, et al. Sequential engagement of distinct MLKL phosphatidylinositol-binding sites executes necroptosis. Mol Cell. 2016;61:589–601
    • (2016) Mol Cell , vol.61 , pp. 589-601
    • Quarato, G.1    Guy, C.S.2    Grace, C.R.3    Llambi, F.4    Nourse, A.5    Rodriguez, D.A.6
  • 71
    • 85016964802 scopus 로고    scopus 로고
    • Necroptosis execution is mediated by plasma membrane nanopores independent of calcium
    • COI: 1:CAS:528:DC%2BC2sXls1Kltr4%3D, PID: 5465952
    • Ros U, Pena-Blanco A, Hanggi K, Kunzendorf U, Krautwald S, Wong WW, et al. Necroptosis execution is mediated by plasma membrane nanopores independent of calcium. Cell Rep. 2017;19:175–87
    • (2017) Cell Rep , vol.19 , pp. 175-187
    • Ros, U.1    Pena-Blanco, A.2    Hanggi, K.3    Kunzendorf, U.4    Krautwald, S.5    Wong, W.W.6
  • 72
    • 84962124841 scopus 로고    scopus 로고
    • MLKL forms cation channels
    • COI: 1:CAS:528:DC%2BC28XlvVahtL8%3D, PID: 4856759
    • Xia B, Fang S, Chen X, Hu H, Chen P, Wang H, et al. MLKL forms cation channels. Cell Res. 2016;26:517–28
    • (2016) Cell Res , vol.26 , pp. 517-528
    • Xia, B.1    Fang, S.2    Chen, X.3    Hu, H.4    Chen, P.5    Wang, H.6
  • 73
    • 85029218179 scopus 로고    scopus 로고
    • MLKL forms disulfide bond-dependent amyloid-like polymers to induce necroptosis
    • COI: 1:CAS:528:DC%2BC2sXhtlOhtbbO
    • Liu S, Liu H, Johnston A, Hanna-Addams S, Reynoso E, Xiang Y, et al. MLKL forms disulfide bond-dependent amyloid-like polymers to induce necroptosis. Proc Natl Acad Sci USA. 2017;114:E7450–9
    • (2017) Proc Natl Acad Sci USA , vol.114 , pp. E7450-E7459
    • Liu, S.1    Liu, H.2    Johnston, A.3    Hanna-Addams, S.4    Reynoso, E.5    Xiang, Y.6
  • 74
    • 85021629176 scopus 로고    scopus 로고
    • Phosphatidylserine externalization, “necroptotic bodies” release, and phagocytosis during necroptosis
    • PID: 5501695
    • Zargarian S, Shlomovitz I, Erlich Z, Hourizadeh A, Ofir-Birin Y, Croker BA, et al. Phosphatidylserine externalization, “necroptotic bodies” release, and phagocytosis during necroptosis. PLoS Biol. 2017;15:e2002711
    • (2017) PLoS Biol , vol.15
    • Zargarian, S.1    Shlomovitz, I.2    Erlich, Z.3    Hourizadeh, A.4    Ofir-Birin, Y.5    Croker, B.A.6
  • 75
    • 84878434348 scopus 로고    scopus 로고
    • Pyroptotic cells externalize eat-me and release find-me signals and are efficiently engulfed by macrophages
    • COI: 1:CAS:528:DC%2BC3sXotFyiur0%3D
    • Wang Q, Imamura R, Motani K, Kushiyama H, Nagata S, Suda T. Pyroptotic cells externalize eat-me and release find-me signals and are efficiently engulfed by macrophages. Int Immunol. 2013;25:363–72
    • (2013) Int Immunol , vol.25 , pp. 363-372
    • Wang, Q.1    Imamura, R.2    Motani, K.3    Kushiyama, H.4    Nagata, S.5    Suda, T.6
  • 77
    • 85049713923 scopus 로고    scopus 로고
    • Nuclear RIPK3 and MLKL contribute to cytosolic necrosome formation and necroptosis
    • PID: 6123744
    • Weber K, Roelandt R, Bruggeman I, Estornes Y, Vandenabeele P. Nuclear RIPK3 and MLKL contribute to cytosolic necrosome formation and necroptosis. Commun Biol. 2018;1:6
    • (2018) Commun Biol , vol.1 , pp. 6
    • Weber, K.1    Roelandt, R.2    Bruggeman, I.3    Estornes, Y.4    Vandenabeele, P.5
  • 78
    • 85040783179 scopus 로고    scopus 로고
    • RIP3 targets pyruvate dehydrogenase complex to increase aerobic respiration in TNF-induced necroptosis
    • COI: 1:CAS:528:DC%2BC1cXkslGisL8%3D
    • Yang Z, Wang Y, Zhang Y, He X, Zhong CQ, Ni H, et al. RIP3 targets pyruvate dehydrogenase complex to increase aerobic respiration in TNF-induced necroptosis. Nat Cell Biol. 2018;20:186–97
    • (2018) Nat Cell Biol , vol.20 , pp. 186-197
    • Yang, Z.1    Wang, Y.2    Zhang, Y.3    He, X.4    Zhong, C.Q.5    Ni, H.6
  • 79
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • COI: 1:CAS:528:DC%2BD1MXos1Sqt7Y%3D, PID: 19498109
    • Zhang DW, Shao J, Lin J, Zhang N, Lu BJ, Lin SC, et al. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science. 2009;325:332–6
    • (2009) Science , vol.325 , pp. 332-336
    • Zhang, D.W.1    Shao, J.2    Lin, J.3    Zhang, N.4    Lu, B.J.5    Lin, S.C.6
  • 80
    • 77952236200 scopus 로고    scopus 로고
    • Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features
    • COI: 1:CAS:528:DC%2BC3cXlslygsrg%3D
    • Vanden Berghe T, Vanlangenakker N, Parthoens E, Deckers W, Devos M, Festjens N, et al. Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features. Cell Death Differ. 2010;17:922–30
    • (2010) Cell Death Differ , vol.17 , pp. 922-930
    • Vanden Berghe, T.1    Vanlangenakker, N.2    Parthoens, E.3    Deckers, W.4    Devos, M.5    Festjens, N.6
  • 81
    • 85021771054 scopus 로고    scopus 로고
    • MLKL, the protein that mediates necroptosis, also regulates endosomal trafficking and extracellular vesicle generation
    • COI: 1:CAS:528:DC%2BC2sXhtVyhur%2FE, e7
    • Yoon S, Kovalenko A, Bogdanov K, Wallach D. MLKL, the protein that mediates necroptosis, also regulates endosomal trafficking and extracellular vesicle generation. Immunity. 2017;47:51–65.e7
    • (2017) Immunity , vol.47 , pp. 51-65
    • Yoon, S.1    Kovalenko, A.2    Bogdanov, K.3    Wallach, D.4
  • 82
    • 85048103635 scopus 로고    scopus 로고
    • GSDMD is critical for autoinflammatory pathology in a mouse model of Familial Mediterranean Fever
    • COI: 1:CAS:528:DC%2BC1cXhvVakt7jE, PID: 5987922
    • Kanneganti A, Malireddi RKS, Saavedra PHV, Vande Walle L, Van Gorp H, Kambara H, et al. GSDMD is critical for autoinflammatory pathology in a mouse model of Familial Mediterranean Fever. J Exp Med. 2018;215:1519–29
    • (2018) J Exp Med , vol.215 , pp. 1519-1529
    • Kanneganti, A.1    Malireddi, R.K.S.2    Saavedra, P.H.V.3    Vande Walle, L.4    Van Gorp, H.5    Kambara, H.6
  • 84
    • 84870950668 scopus 로고    scopus 로고
    • NLRP1 inflammasome activation induces pyroptosis of hematopoietic progenitor cells
    • COI: 1:CAS:528:DC%2BC38Xhsl2lu7%2FP, PID: 23219391
    • Masters SL, Gerlic M, Metcalf D, Preston S, Pellegrini M, O’Donnell JA, et al. NLRP1 inflammasome activation induces pyroptosis of hematopoietic progenitor cells. Immunity. 2012;37:1009–23
    • (2012) Immunity , vol.37 , pp. 1009-1023
    • Masters, S.L.1    Gerlic, M.2    Metcalf, D.3    Preston, S.4    Pellegrini, M.5    O’Donnell, J.A.6
  • 85
    • 84892739389 scopus 로고    scopus 로고
    • Cell death by pyroptosis drives CD4 T-cell depletion in HIV-1 infection
    • COI: 1:CAS:528:DC%2BC2cXhtFOls7o%3D, PID: 4047036
    • Doitsh G, Galloway NL, Geng X, Yang Z, Monroe KM, Zepeda O, et al. Cell death by pyroptosis drives CD4 T-cell depletion in HIV-1 infection. Nature. 2014;505:509–14
    • (2014) Nature , vol.505 , pp. 509-514
    • Doitsh, G.1    Galloway, N.L.2    Geng, X.3    Yang, Z.4    Monroe, K.M.5    Zepeda, O.6
  • 86
    • 84941317034 scopus 로고    scopus 로고
    • Canonical inflammasomes drive IFN-gamma to prime caspase-11 in defense against a cytosol-invasive bacterium
    • COI: 1:CAS:528:DC%2BC2MXhsVajs73K, PID: 4567510
    • Aachoui Y, Kajiwara Y, Leaf IA, Mao D, Ting JP, Coers J, et al. Canonical inflammasomes drive IFN-gamma to prime caspase-11 in defense against a cytosol-invasive bacterium. Cell Host Microbe. 2015;18:320–32
    • (2015) Cell Host Microbe , vol.18 , pp. 320-332
    • Aachoui, Y.1    Kajiwara, Y.2    Leaf, I.A.3    Mao, D.4    Ting, J.P.5    Coers, J.6
  • 87
    • 84947416929 scopus 로고    scopus 로고
    • Inflammasomes coordinate pyroptosis and natural killer cell cytotoxicity to clear infection by a ubiquitous environmental bacterium
    • COI: 1:CAS:528:DC%2BC2MXhvVSgtbnM, PID: 4654968
    • Maltez VI, Tubbs AL, Cook KD, Aachoui Y, Falcone EL, Holland SM, et al. Inflammasomes coordinate pyroptosis and natural killer cell cytotoxicity to clear infection by a ubiquitous environmental bacterium. Immunity. 2015;43:987–97
    • (2015) Immunity , vol.43 , pp. 987-997
    • Maltez, V.I.1    Tubbs, A.L.2    Cook, K.D.3    Aachoui, Y.4    Falcone, E.L.5    Holland, S.M.6
  • 88
    • 84874189388 scopus 로고    scopus 로고
    • Caspase-11 protects against bacteria that escape the vacuole
    • COI: 1:CAS:528:DC%2BC3sXis1Oisbc%3D, PID: 3697099
    • Aachoui Y, Leaf IA, Hagar JA, Fontana MF, Campos CG, Zak DE, et al. Caspase-11 protects against bacteria that escape the vacuole. Science. 2013;339:975–8
    • (2013) Science , vol.339 , pp. 975-978
    • Aachoui, Y.1    Leaf, I.A.2    Hagar, J.A.3    Fontana, M.F.4    Campos, C.G.5    Zak, D.E.6
  • 89
    • 85010270989 scopus 로고    scopus 로고
    • Eliminating Legionella by inhibiting BCL-XL to induce macrophage apoptosis
    • COI: 1:CAS:528:DC%2BC2sXkvF2js7Y%3D
    • Speir M, Lawlor KE, Glaser SP, Abraham G, Chow S, Vogrin A, et al. Eliminating Legionella by inhibiting BCL-XL to induce macrophage apoptosis. Nat Microbiol. 2016;1:15034
    • (2016) Nat Microbiol , vol.1 , pp. 15034
    • Speir, M.1    Lawlor, K.E.2    Glaser, S.P.3    Abraham, G.4    Chow, S.5    Vogrin, A.6
  • 90
    • 84884151651 scopus 로고    scopus 로고
    • Masters, marionettes and modulators: intersection of pathogen virulence factors and mammalian death receptor signaling
    • COI: 1:CAS:528:DC%2BC3sXhtVWgsbvP, PID: 23800628
    • Silke J, Hartland EL. Masters, marionettes and modulators: intersection of pathogen virulence factors and mammalian death receptor signaling. Curr Opin Immunol. 2013;25:436–40
    • (2013) Curr Opin Immunol , vol.25 , pp. 436-440
    • Silke, J.1    Hartland, E.L.2
  • 91
    • 85020853020 scopus 로고    scopus 로고
    • Apoptosis and necroptosis as host defense strategies to prevent viral infection
    • COI: 1:CAS:528:DC%2BC2sXpvVKiu70%3D, PID: 28642032
    • Orzalli MH, Kagan JC. Apoptosis and necroptosis as host defense strategies to prevent viral infection. Trends Cell Biol. 2017;27:800–9
    • (2017) Trends Cell Biol , vol.27 , pp. 800-809
    • Orzalli, M.H.1    Kagan, J.C.2
  • 93
    • 84862175306 scopus 로고    scopus 로고
    • Dichotomy between RIP1- and RIP3-mediated necroptosis in tumor necrosis factor-alpha-induced shock
    • COI: 1:CAS:528:DC%2BC38XhtVGmurnL, PID: 3388137
    • Linkermann A, Brasen JH, De Zen F, Weinlich R, Schwendener RA, Green DR, et al. Dichotomy between RIP1- and RIP3-mediated necroptosis in tumor necrosis factor-alpha-induced shock. Mol Med. 2012;18:577–86
    • (2012) Mol Med , vol.18 , pp. 577-586
    • Linkermann, A.1    Brasen, J.H.2    De Zen, F.3    Weinlich, R.4    Schwendener, R.A.5    Green, D.R.6
  • 94
    • 84897088275 scopus 로고    scopus 로고
    • Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis
    • COI: 1:CAS:528:DC%2BC2cXktl2gs7g%3D
    • Newton K, Dugger DL, Wickliffe KE, Kapoor N, de Almagro MC, Vucic D, et al. Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis. Science. 2014;343:1357–60
    • (2014) Science , vol.343 , pp. 1357-1360
    • Newton, K.1    Dugger, D.L.2    Wickliffe, K.E.3    Kapoor, N.4    de Almagro, M.C.5    Vucic, D.6
  • 95
    • 84859299752 scopus 로고    scopus 로고
    • Rip1 (receptor-interacting protein kinase 1) mediates necroptosis and contributes to renal ischemia/reperfusion injury
    • COI: 1:CAS:528:DC%2BC38XkvV2rtbo%3D, PID: 22237751
    • Linkermann A, Brasen JH, Himmerkus N, Liu S, Huber TB, Kunzendorf U, et al. Rip1 (receptor-interacting protein kinase 1) mediates necroptosis and contributes to renal ischemia/reperfusion injury. Kidney Int. 2012;81:751–61
    • (2012) Kidney Int , vol.81 , pp. 751-761
    • Linkermann, A.1    Brasen, J.H.2    Himmerkus, N.3    Liu, S.4    Huber, T.B.5    Kunzendorf, U.6
  • 96
    • 84886796430 scopus 로고    scopus 로고
    • RIPK3-mediated necroptosis promotes donor kidney inflammatory injury and reduces allograft survival
    • COI: 1:CAS:528:DC%2BC3sXhslSqurzL
    • Lau A, Wang S, Jiang J, Haig A, Pavlosky A, Linkermann A, et al. RIPK3-mediated necroptosis promotes donor kidney inflammatory injury and reduces allograft survival. Am J Transplant. 2013;13:2805–18
    • (2013) Am J Transplant , vol.13 , pp. 2805-2818
    • Lau, A.1    Wang, S.2    Jiang, J.3    Haig, A.4    Pavlosky, A.5    Linkermann, A.6
  • 97
    • 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
    • COI: 1:CAS:528:DC%2BC28XotV2it7c%3D, PID: 5072432
    • Newton K, Dugger DL, Maltzman A, Greve JM, Hedehus M, Martin-McNulty B, 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. 2016;23:1565–76
    • (2016) Cell Death Differ , vol.23 , pp. 1565-1576
    • Newton, K.1    Dugger, D.L.2    Maltzman, A.3    Greve, J.M.4    Hedehus, M.5    Martin-McNulty, B.6
  • 98
    • 84857404572 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation
    • COI: 1:CAS:528:DC%2BC38XjtFSmsbw%3D, PID: 22365665
    • Vince JE, Wong WW, Gentle I, Lawlor KE, Allam R, O’Reilly L, et al. Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation. Immunity. 2012;36:215–27
    • (2012) Immunity , vol.36 , pp. 215-227
    • Vince, J.E.1    Wong, W.W.2    Gentle, I.3    Lawlor, K.E.4    Allam, R.5    O’Reilly, L.6
  • 99
    • 84903480849 scopus 로고    scopus 로고
    • XIAP restricts TNF- and RIP3-dependent cell death and inflammasome activation
    • COI: 1:CAS:528:DC%2BC2cXpslCgu7s%3D, PID: 24882010
    • Yabal M, Muller N, Adler H, Knies N, Gross CJ, Damgaard RB, et al. XIAP restricts TNF- and RIP3-dependent cell death and inflammasome activation. Cell Rep. 2014;7:1796–808
    • (2014) Cell Rep , vol.7 , pp. 1796-1808
    • Yabal, M.1    Muller, N.2    Adler, H.3    Knies, N.4    Gross, C.J.5    Damgaard, R.B.6
  • 100
    • 85025097192 scopus 로고    scopus 로고
    • XIAP loss triggers RIPK3- and caspase-8-driven IL-1beta activation and cell death as a consequence of TLR-MyD88-induced cIAP1-TRAF2 degradation
    • COI: 1:CAS:528:DC%2BC2sXhtF2qur3O, PID: 28723569
    • Lawlor KE, Feltham R, Yabal M, Conos SA, Chen KW, Ziehe S, et al. XIAP loss triggers RIPK3- and caspase-8-driven IL-1beta activation and cell death as a consequence of TLR-MyD88-induced cIAP1-TRAF2 degradation. Cell Rep. 2017;20:668–82
    • (2017) Cell Rep , vol.20 , pp. 668-682
    • Lawlor, K.E.1    Feltham, R.2    Yabal, M.3    Conos, S.A.4    Chen, K.W.5    Ziehe, S.6
  • 101
    • 84921305910 scopus 로고    scopus 로고
    • A20 restricts ubiquitination of pro-interleukin-1beta protein complexes and suppresses NLRP3 inflammasome activity
    • COI: 1:CAS:528:DC%2BC2MXhtlOmsrg%3D, PID: 25607459
    • Duong BH, Onizawa M, Oses-Prieto JA, Advincula R, Burlingame A, Malynn BA, et al. A20 restricts ubiquitination of pro-interleukin-1beta protein complexes and suppresses NLRP3 inflammasome activity. Immunity. 2015;42:55–67
    • (2015) Immunity , vol.42 , pp. 55-67
    • Duong, B.H.1    Onizawa, M.2    Oses-Prieto, J.A.3    Advincula, R.4    Burlingame, A.5    Malynn, B.A.6
  • 102
    • 84923674191 scopus 로고    scopus 로고
    • RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL
    • COI: 1:CAS:528:DC%2BC2MXhtF2itLrK, PID: 25693118
    • Lawlor KE, Khan N, Mildenhall A, Gerlic M, Croker BA, D’Cruz AA, et al. RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL. Nat Commun. 2015;6:6282
    • (2015) Nat Commun , vol.6
    • Lawlor, K.E.1    Khan, N.2    Mildenhall, A.3    Gerlic, M.4    Croker, B.A.5    D’Cruz, A.A.6
  • 103
    • 84872764927 scopus 로고    scopus 로고
    • Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome
    • COI: 1:CAS:528:DC%2BC38XhvVOqsL3F, PID: 23260196
    • Kang TB, Yang SH, Toth B, Kovalenko A, Wallach D. Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome. Immunity. 2013;38:27–40
    • (2013) Immunity , vol.38 , pp. 27-40
    • Kang, T.B.1    Yang, S.H.2    Toth, B.3    Kovalenko, A.4    Wallach, D.5
  • 104
    • 85041851801 scopus 로고    scopus 로고
    • Non-hematopoietic MLKL protects against salmonella mucosal infection by enhancing inflammasome activation
    • PID: 29456533
    • Yu SX, Chen W, Liu ZZ, Zhou FH, Yan SQ, Hu GQ, et al. Non-hematopoietic MLKL protects against salmonella mucosal infection by enhancing inflammasome activation. Front Immunol. 2018;9:119
    • (2018) Front Immunol , vol.9 , pp. 119
    • Yu, S.X.1    Chen, W.2    Liu, Z.Z.3    Zhou, F.H.4    Yan, S.Q.5    Hu, G.Q.6
  • 105
    • 84929494277 scopus 로고    scopus 로고
    • Toxin-induced necroptosis is a major mechanism of Staphylococcus aureus lung damage
    • PID: 25880560
    • Kitur K, Parker D, Nieto P, Ahn DS, Cohen TS, Chung S, et al. Toxin-induced necroptosis is a major mechanism of Staphylococcus aureus lung damage. PLoS Pathog. 2015;11:e1004820
    • (2015) PLoS Pathog , vol.11
    • Kitur, K.1    Parker, D.2    Nieto, P.3    Ahn, D.S.4    Cohen, T.S.5    Chung, S.6
  • 107
    • 80052800427 scopus 로고    scopus 로고
    • Heat shock proteins and high mobility group box 1 protein lack cytokine function
    • COI: 1:CAS:528:DC%2BC3MXnsFKqurw%3D
    • Tsan MF. Heat shock proteins and high mobility group box 1 protein lack cytokine function. J Leukoc Biol. 2011;89:847–53
    • (2011) J Leukoc Biol , vol.89 , pp. 847-853
    • Tsan, M.F.1
  • 108
    • 84948614431 scopus 로고    scopus 로고
    • The HMGB1/RAGE axis triggers neutrophil-mediated injury amplification following necrosis
    • PID: 25562324
    • Huebener P, Pradere JP, Hernandez C, Gwak GY, Caviglia JM, Mu X, et al. The HMGB1/RAGE axis triggers neutrophil-mediated injury amplification following necrosis. J Clin Invest. 2015;125:539–50
    • (2015) J Clin Invest , vol.125 , pp. 539-550
    • Huebener, P.1    Pradere, J.P.2    Hernandez, C.3    Gwak, G.Y.4    Caviglia, J.M.5    Mu, X.6
  • 109
  • 110
    • 84893525976 scopus 로고    scopus 로고
    • Simultaneous targeting of IL-1 and IL-18 is required for protection against inflammatory and septic shock
    • COI: 1:CAS:528:DC%2BC2cXmtVeltbg%3D
    • Vanden Berghe T, Demon D, Bogaert P, Vandendriessche B, Goethals A, Depuydt B, et al. Simultaneous targeting of IL-1 and IL-18 is required for protection against inflammatory and septic shock. Am J Respir Crit Care Med. 2014;189:282–91
    • (2014) Am J Respir Crit Care Med , vol.189 , pp. 282-291
    • Vanden Berghe, T.1    Demon, D.2    Bogaert, P.3    Vandendriessche, B.4    Goethals, A.5    Depuydt, B.6
  • 111
    • 77958125448 scopus 로고    scopus 로고
    • Inflammasome-dependent release of the alarmin HMGB1 in endotoxemia
    • COI: 1:CAS:528:DC%2BC3cXhtFyis77O, PID: 3428148
    • Lamkanfi M, Sarkar A, Vande Walle L, Vitari AC, Amer AO, Wewers MD, et al. Inflammasome-dependent release of the alarmin HMGB1 in endotoxemia. J Immunol. 2010;185:4385–92
    • (2010) J Immunol , vol.185 , pp. 4385-4392
    • Lamkanfi, M.1    Sarkar, A.2    Vande Walle, L.3    Vitari, A.C.4    Amer, A.O.5    Wewers, M.D.6
  • 112
    • 78649821588 scopus 로고    scopus 로고
    • IL-33 is a crucial amplifier of innate rather than acquired immunity
    • COI: 1:CAS:528:DC%2BC3cXhtl2ktrvF
    • Oboki K, Ohno T, Kajiwara N, Arae K, Morita H, Ishii A, et al. IL-33 is a crucial amplifier of innate rather than acquired immunity. Proc Natl Acad Sci USA. 2010;107:18581–6
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 18581-18586
    • Oboki, K.1    Ohno, T.2    Kajiwara, N.3    Arae, K.4    Morita, H.5    Ishii, A.6
  • 114
    • 0033538467 scopus 로고    scopus 로고
    • HMG-1 as a late mediator of endotoxin lethality in mice
    • COI: 1:CAS:528:DyaK1MXks1Sjtb0%3D
    • Wang H, Bloom O, Zhang M, Vishnubhakat JM, Ombrellino M, Che J, et al. HMG-1 as a late mediator of endotoxin lethality in mice. Science. 1999;285:248–51
    • (1999) Science , vol.285 , pp. 248-251
    • Wang, H.1    Bloom, O.2    Zhang, M.3    Vishnubhakat, J.M.4    Ombrellino, M.5    Che, J.6
  • 115
    • 85025124336 scopus 로고    scopus 로고
    • Therapeutic targeting of HMGB1 during experimental sepsis modulates the inflammatory cytokine profile to one associated with improved clinical outcomes
    • PID: 28724977
    • Stevens NE, Chapman MJ, Fraser CK, Kuchel TR, Hayball JD, Diener KR. Therapeutic targeting of HMGB1 during experimental sepsis modulates the inflammatory cytokine profile to one associated with improved clinical outcomes. Sci Rep. 2017;7:5850
    • (2017) Sci Rep , vol.7
    • Stevens, N.E.1    Chapman, M.J.2    Fraser, C.K.3    Kuchel, T.R.4    Hayball, J.D.5    Diener, K.R.6
  • 116
    • 84872842379 scopus 로고    scopus 로고
    • TLR activation regulates damage-associated molecular pattern isoforms released during pyroptosis
    • Nystrom S, Antoine DJ, Lundback P, Lock JG, Nita AF, Hogstrand K, et al. TLR activation regulates damage-associated molecular pattern isoforms released during pyroptosis. EMBO J. 2013;32:86–99
    • (2013) EMBO J , vol.32 , pp. 86-99
    • Nystrom, S.1    Antoine, D.J.2    Lundback, P.3    Lock, J.G.4    Nita, A.F.5    Hogstrand, K.6
  • 117
    • 84905053185 scopus 로고    scopus 로고
    • Macrophage endocytosis of high-mobility group box 1 triggers pyroptosis
    • COI: 1:CAS:528:DC%2BC2cXntlejsLg%3D, PID: 4085529
    • Xu J, Jiang Y, Wang J, Shi X, Liu Q, Liu Z, et al. Macrophage endocytosis of high-mobility group box 1 triggers pyroptosis. Cell Death Differ. 2014;21:1229–39
    • (2014) Cell Death Differ , vol.21 , pp. 1229-1239
    • Xu, J.1    Jiang, Y.2    Wang, J.3    Shi, X.4    Liu, Q.5    Liu, Z.6
  • 118
    • 84965131629 scopus 로고    scopus 로고
    • Contribution of RIP3 and MLKL to immunogenic cell death signaling in cancer chemotherapy
    • PID: 4938314
    • Yang H, Ma Y, Chen G, Zhou H, Yamazaki T, Klein C, et al. Contribution of RIP3 and MLKL to immunogenic cell death signaling in cancer chemotherapy. Oncoimmunology. 2016;5:e1149673
    • (2016) Oncoimmunology , vol.5
    • Yang, H.1    Ma, Y.2    Chen, G.3    Zhou, H.4    Yamazaki, T.5    Klein, C.6
  • 119
    • 0037062934 scopus 로고    scopus 로고
    • Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
    • COI: 1:CAS:528:DC%2BD38XltFGlsro%3D
    • Scaffidi P, Misteli T, Bianchi ME. Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature. 2002;418:191–5
    • (2002) Nature , vol.418 , pp. 191-195
    • Scaffidi, P.1    Misteli, T.2    Bianchi, M.E.3
  • 120
    • 84901422731 scopus 로고    scopus 로고
    • RIPK1 regulates RIPK3-MLKL-driven systemic inflammation and emergency hematopoiesis
    • COI: 1:CAS:528:DC%2BC2cXnslGms78%3D, PID: 24813849
    • Rickard JA, O’Donnell JA, Evans JM, Lalaoui N, Poh AR, Rogers T, et al. RIPK1 regulates RIPK3-MLKL-driven systemic inflammation and emergency hematopoiesis. Cell. 2014;157:1175–88
    • (2014) Cell , vol.157 , pp. 1175-1188
    • Rickard, J.A.1    O’Donnell, J.A.2    Evans, J.M.3    Lalaoui, N.4    Poh, A.R.5    Rogers, T.6
  • 121
    • 84959552077 scopus 로고    scopus 로고
    • Tissue damage negatively regulates LPS-induced macrophage necroptosis
    • COI: 1:CAS:528:DC%2BC28XktVOgsrs%3D, PID: 5072421
    • Li Z, Scott MJ, Fan EK, Li Y, Liu J, Xiao G, et al. Tissue damage negatively regulates LPS-induced macrophage necroptosis. Cell Death Differ. 2016;23:1428–47
    • (2016) Cell Death Differ , vol.23 , pp. 1428-1447
    • Li, Z.1    Scott, M.J.2    Fan, E.K.3    Li, Y.4    Liu, J.5    Xiao, G.6
  • 122
    • 84945232013 scopus 로고    scopus 로고
    • RIPK1 and NF-kappaB signaling in dying cells determines cross-priming of CD8(+) T cells
    • COI: 1:CAS:528:DC%2BC2MXhs1ChsL3J, PID: 26405229
    • Yatim N, Jusforgues-Saklani H, Orozco S, Schulz O, Barreira da Silva R, Reis e Sousa C, et al. RIPK1 and NF-kappaB signaling in dying cells determines cross-priming of CD8(+) T cells. Science. 2015;350:328–34
    • (2015) Science , vol.350 , pp. 328-334
    • Yatim, N.1    Jusforgues-Saklani, H.2    Orozco, S.3    Schulz, O.4    Barreira da Silva, R.5    Reis e Sousa, C.6
  • 123
    • 84969595271 scopus 로고    scopus 로고
    • The caspase-8 inhibitor emricasan combines with the SMAC mimetic birinapant to induce necroptosis and treat acute myeloid leukemia
    • Brumatti G, Ma C, Lalaoui N, Nguyen NY, Navarro M, Tanzer MC, et al. The caspase-8 inhibitor emricasan combines with the SMAC mimetic birinapant to induce necroptosis and treat acute myeloid leukemia. Sci Transl Med. 2016;8:339ra369
    • (2016) Sci Transl Med , vol.8 , pp. 339ra369
    • Brumatti, G.1    Ma, C.2    Lalaoui, N.3    Nguyen, N.Y.4    Navarro, M.5    Tanzer, M.C.6
  • 124
    • 84969626016 scopus 로고    scopus 로고
    • Activation of concurrent apoptosis and necroptosis by SMAC mimetics for the treatment of refractory and relapsed ALL
    • McComb S, Aguade-Gorgorio J, Harder L, Marovca B, Cario G, Eckert C, et al. Activation of concurrent apoptosis and necroptosis by SMAC mimetics for the treatment of refractory and relapsed ALL. Sci Transl Med. 2016;8:339ra370
    • (2016) Sci Transl Med , vol.8 , pp. 339ra370
    • McComb, S.1    Aguade-Gorgorio, J.2    Harder, L.3    Marovca, B.4    Cario, G.5    Eckert, C.6
  • 125
    • 77955630643 scopus 로고    scopus 로고
    • HMGB1 contributes to kidney ischemia reperfusion injury
    • COI: 1:CAS:528:DC%2BC3cXhsFCnsrbP, PID: 3014003
    • Wu H, Ma J, Wang P, Corpuz TM, Panchapakesan U, Wyburn KR, et al. HMGB1 contributes to kidney ischemia reperfusion injury. J Am Soc Nephrol. 2010;21:1878–90
    • (2010) J Am Soc Nephrol , vol.21 , pp. 1878-1890
    • Wu, H.1    Ma, J.2    Wang, P.3    Corpuz, T.M.4    Panchapakesan, U.5    Wyburn, K.R.6
  • 126
    • 84904692363 scopus 로고    scopus 로고
    • The adaptor ASC has extracellular and ‘prionoid’ activities that propagate inflammation
    • COI: 1:CAS:528:DC%2BC2cXhtVais7zI, PID: 4116676
    • Franklin BS, Bossaller L, De Nardo D, Ratter JM, Stutz A, Engels G, et al. The adaptor ASC has extracellular and ‘prionoid’ activities that propagate inflammation. Nat Immunol. 2014;15:727–37
    • (2014) Nat Immunol , vol.15 , pp. 727-737
    • Franklin, B.S.1    Bossaller, L.2    De Nardo, D.3    Ratter, J.M.4    Stutz, A.5    Engels, G.6
  • 127
    • 84904646033 scopus 로고    scopus 로고
    • The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response
    • COI: 1:CAS:528:DC%2BC2cXhtVais7zK
    • Baroja-Mazo A, Martin-Sanchez F, Gomez AI, Martinez CM, Amores-Iniesta J, Compan V, et al. The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response. Nat Immunol. 2014;15:738–48
    • (2014) Nat Immunol , vol.15 , pp. 738-748
    • Baroja-Mazo, A.1    Martin-Sanchez, F.2    Gomez, A.I.3    Martinez, C.M.4    Amores-Iniesta, J.5    Compan, V.6
  • 129
    • 70350484946 scopus 로고    scopus 로고
    • Caspase-8 deficiency in epidermal keratinocytes triggers an inflammatory skin disease
    • COI: 1:CAS:528:DC%2BD1MXht1SrtbjK, PID: 2757876
    • Kovalenko A, Kim JC, Kang TB, Rajput A, Bogdanov K, Dittrich-Breiholz O, et al. Caspase-8 deficiency in epidermal keratinocytes triggers an inflammatory skin disease. J Exp Med. 2009;206:2161–77
    • (2009) J Exp Med , vol.206 , pp. 2161-2177
    • Kovalenko, A.1    Kim, J.C.2    Kang, T.B.3    Rajput, A.4    Bogdanov, K.5    Dittrich-Breiholz, O.6
  • 130
    • 34347347039 scopus 로고    scopus 로고
    • Endogenous signals released from necrotic cells augment inflammatory responses to bacterial endotoxin
    • COI: 1:CAS:528:DC%2BD2sXnsFKmsbc%3D, PID: 3034364
    • El Mezayen R, El Gazzar M, Seeds MC, McCall CE, Dreskin SC, Nicolls MR. Endogenous signals released from necrotic cells augment inflammatory responses to bacterial endotoxin. Immunol Lett. 2007;111:36–44
    • (2007) Immunol Lett , vol.111 , pp. 36-44
    • El Mezayen, R.1    El Gazzar, M.2    Seeds, M.C.3    McCall, C.E.4    Dreskin, S.C.5    Nicolls, M.R.6
  • 131
    • 34247265509 scopus 로고    scopus 로고
    • A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses
    • COI: 1:CAS:528:DC%2BD2sXkt1Khtrg%3D
    • Mayor A, Martinon F, De Smedt T, Petrilli V, Tschopp J. A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses. Nat Immunol. 2007;8:497–503
    • (2007) Nat Immunol , vol.8 , pp. 497-503
    • Mayor, A.1    Martinon, F.2    De Smedt, T.3    Petrilli, V.4    Tschopp, J.5
  • 132
    • 84955109392 scopus 로고    scopus 로고
    • HSP90 activity is required for MLKL oligomerisation and membrane translocation and the induction of necroptotic cell death
    • COI: 1:STN:280:DC%2BC28nhsVChtQ%3D%3D, PID: 4816171
    • Jacobsen AV, Lowes KN, Tanzer MC, Lucet IS, Hildebrand JM, Petrie EJ, et al. HSP90 activity is required for MLKL oligomerisation and membrane translocation and the induction of necroptotic cell death. Cell Death Dis. 2016;7:e2051
    • (2016) Cell Death Dis , vol.7
    • Jacobsen, A.V.1    Lowes, K.N.2    Tanzer, M.C.3    Lucet, I.S.4    Hildebrand, J.M.5    Petrie, E.J.6
  • 134
    • 45849102043 scopus 로고    scopus 로고
    • ATP is released by monocytes stimulated with pathogen-sensing receptor ligands and induces IL-1beta and IL-18 secretion in an autocrine way
    • COI: 1:CAS:528:DC%2BD1cXns1elsLs%3D
    • Piccini A, Carta S, Tassi S, Lasiglie D, Fossati G, Rubartelli A. ATP is released by monocytes stimulated with pathogen-sensing receptor ligands and induces IL-1beta and IL-18 secretion in an autocrine way. Proc Natl Acad Sci USA. 2008;105:8067–72
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8067-8072
    • Piccini, A.1    Carta, S.2    Tassi, S.3    Lasiglie, D.4    Fossati, G.5    Rubartelli, A.6
  • 135
    • 84994791054 scopus 로고    scopus 로고
    • Alternative inflammasome activation enables IL-1beta release from living cells
    • PID: 5894802
    • Gaidt MM, Hornung V. Alternative inflammasome activation enables IL-1beta release from living cells. Curr Opin Immunol. 2016;44:7–13
    • (2016) Curr Opin Immunol , vol.44 , pp. 7-13
    • Gaidt, M.M.1    Hornung, V.2
  • 136
    • 70350569295 scopus 로고    scopus 로고
    • Activation of the NLRP3 inflammasome in dendritic cells induces IL-1beta-dependent adaptive immunity against tumors
    • COI: 1:CAS:528:DC%2BD1MXhtFGjt7rK
    • Ghiringhelli F, Apetoh L, Tesniere A, Aymeric L, Ma Y, Ortiz C, et al. Activation of the NLRP3 inflammasome in dendritic cells induces IL-1beta-dependent adaptive immunity against tumors. Nat Med. 2009;15:1170–8
    • (2009) Nat Med , vol.15 , pp. 1170-1178
    • Ghiringhelli, F.1    Apetoh, L.2    Tesniere, A.3    Aymeric, L.4    Ma, Y.5    Ortiz, C.6
  • 137
    • 73949118676 scopus 로고    scopus 로고
    • Necrotic cells trigger a sterile inflammatory response through the Nlrp3 inflammasome
    • COI: 1:CAS:528:DC%2BC3cXjtFWjsA%3D%3D
    • Iyer SS, Pulskens WP, Sadler JJ, Butter LM, Teske GJ, Ulland TK, et al. Necrotic cells trigger a sterile inflammatory response through the Nlrp3 inflammasome. Proc Natl Acad Sci USA. 2009;106:20388–93
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20388-20393
    • Iyer, S.S.1    Pulskens, W.P.2    Sadler, J.J.3    Butter, L.M.4    Teske, G.J.5    Ulland, T.K.6
  • 138
    • 84862777872 scopus 로고    scopus 로고
    • Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
    • COI: 1:CAS:528:DC%2BC38XisFajsL0%3D, PID: 3312986
    • Shimada K, Crother TR, Karlin J, Dagvadorj J, Chiba N, Chen S, et al. Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis. Immunity. 2012;36:401–14
    • (2012) Immunity , vol.36 , pp. 401-414
    • Shimada, K.1    Crother, T.R.2    Karlin, J.3    Dagvadorj, J.4    Chiba, N.5    Chen, S.6
  • 139
    • 79951642032 scopus 로고    scopus 로고
    • Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
    • COI: 1:CAS:528:DC%2BC3cXhsFGgtrzE
    • Nakahira K, Haspel JA, Rathinam VA, Lee SJ, Dolinay T, Lam HC, et al. Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat Immunol. 2011;12:222–30
    • (2011) Nat Immunol , vol.12 , pp. 222-230
    • Nakahira, K.1    Haspel, J.A.2    Rathinam, V.A.3    Lee, S.J.4    Dolinay, T.5    Lam, H.C.6
  • 140
    • 85031296044 scopus 로고    scopus 로고
    • Oxysterol restraint of cholesterol synthesis prevents AIM2 inflammasome activation
    • COI: 1:CAS:528:DC%2BC2sXhs1GjsrnJ, PID: 5693620
    • Dang EV, McDonald JG, Russell DW, Cyster JG. Oxysterol restraint of cholesterol synthesis prevents AIM2 inflammasome activation. Cell. 2017;171:1057–71.e11
    • (2017) Cell , vol.171 , pp. 1057-1071
    • Dang, E.V.1    McDonald, J.G.2    Russell, D.W.3    Cyster, J.G.4
  • 141
    • 84906852294 scopus 로고    scopus 로고
    • Mitochondrial apoptosis is dispensable for NLRP3 inflammasome activation but non-apoptotic caspase-8 is required for inflammasome priming
    • COI: 1:CAS:528:DC%2BC2cXhvV2nsLjF, PID: 4198042
    • Allam R, Lawlor KE, Yu EC, Mildenhall AL, Moujalled DM, Lewis RS, et al. Mitochondrial apoptosis is dispensable for NLRP3 inflammasome activation but non-apoptotic caspase-8 is required for inflammasome priming. EMBO Rep. 2014;15:982–90
    • (2014) EMBO Rep , vol.15 , pp. 982-990
    • Allam, R.1    Lawlor, K.E.2    Yu, E.C.3    Mildenhall, A.L.4    Moujalled, D.M.5    Lewis, R.S.6
  • 142
    • 84908544666 scopus 로고    scopus 로고
    • Inflammasome activation leads to Caspase-1-dependent mitochondrial damage and block of mitophagy
    • COI: 1:CAS:528:DC%2BC2cXhslelsb%2FP
    • Yu J, Nagasu H, Murakami T, Hoang H, Broderick L, Hoffman HM, et al. Inflammasome activation leads to Caspase-1-dependent mitochondrial damage and block of mitophagy. Proc Natl Acad Sci USA. 2014;111:15514–9
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 15514-15519
    • Yu, J.1    Nagasu, H.2    Murakami, T.3    Hoang, H.4    Broderick, L.5    Hoffman, H.M.6
  • 143
    • 84905503923 scopus 로고    scopus 로고
    • Mitochondria released by cells undergoing TNF-alpha-induced necroptosis act as danger signals
    • COI: 1:CAS:528:DC%2BC2cXhtFWisbbN, PID: 4123071
    • Maeda A, Fadeel B. Mitochondria released by cells undergoing TNF-alpha-induced necroptosis act as danger signals. Cell Death Dis. 2014;5:e1312
    • (2014) Cell Death Dis , vol.5
    • Maeda, A.1    Fadeel, B.2
  • 144
    • 77950275298 scopus 로고    scopus 로고
    • Circulating mitochondrial DAMPs cause inflammatory responses to injury
    • COI: 1:CAS:528:DC%2BC3cXislaiurk%3D, PID: 20203610
    • Zhang Q, Raoof M, Chen Y, Sumi Y, Sursal T, Junger W, et al. Circulating mitochondrial DAMPs cause inflammatory responses to injury. Nature. 2010;464:104–7
    • (2010) Nature , vol.464 , pp. 104-107
    • Zhang, Q.1    Raoof, M.2    Chen, Y.3    Sumi, Y.4    Sursal, T.5    Junger, W.6
  • 145
    • 34447116244 scopus 로고    scopus 로고
    • Identification of a key pathway required for the sterile inflammatory response triggered by dying cells
    • COI: 1:CAS:528:DC%2BD2sXnsFWmtrk%3D
    • Chen CJ, Kono H, Golenbock D, Reed G, Akira S, Rock KL. Identification of a key pathway required for the sterile inflammatory response triggered by dying cells. Nat Med. 2007;13:851–6
    • (2007) Nat Med , vol.13 , pp. 851-856
    • Chen, C.J.1    Kono, H.2    Golenbock, D.3    Reed, G.4    Akira, S.5    Rock, K.L.6
  • 146
    • 84858761335 scopus 로고    scopus 로고
    • Inflammasome activators induce interleukin-1alpha secretion via distinct pathways with differential requirement for the protease function of caspase-1
    • COI: 1:CAS:528:DC%2BC38XksVCmt7o%3D, PID: 22444631
    • Gross O, Yazdi AS, Thomas CJ, Masin M, Heinz LX, Guarda G, et al. Inflammasome activators induce interleukin-1alpha secretion via distinct pathways with differential requirement for the protease function of caspase-1. Immunity. 2012;36:388–400
    • (2012) Immunity , vol.36 , pp. 388-400
    • Gross, O.1    Yazdi, A.S.2    Thomas, C.J.3    Masin, M.4    Heinz, L.X.5    Guarda, G.6
  • 147
    • 84874248044 scopus 로고    scopus 로고
    • Intracellular interleukin-1 receptor 2 binding prevents cleavage and activity of interleukin-1alpha, controlling necrosis-induced sterile inflammation
    • COI: 1:CAS:528:DC%2BC3sXit1emt7s%3D, PID: 3659285
    • Zheng Y, Humphry M, Maguire JJ, Bennett MR, Clarke MC. Intracellular interleukin-1 receptor 2 binding prevents cleavage and activity of interleukin-1alpha, controlling necrosis-induced sterile inflammation. Immunity. 2013;38:285–95
    • (2013) Immunity , vol.38 , pp. 285-295
    • Zheng, Y.1    Humphry, M.2    Maguire, J.J.3    Bennett, M.R.4    Clarke, M.C.5
  • 148
    • 77951800951 scopus 로고    scopus 로고
    • NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals
    • COI: 1:CAS:528:DC%2BC3cXltl2mu7w%3D, PID: 20428172
    • Duewell P, Kono H, Rayner KJ, Sirois CM, Vladimer G, Bauernfeind FG, et al. NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals. Nature. 2010;464:1357–61
    • (2010) Nature , vol.464 , pp. 1357-1361
    • Duewell, P.1    Kono, H.2    Rayner, K.J.3    Sirois, C.M.4    Vladimer, G.5    Bauernfeind, F.G.6
  • 149
    • 84979645446 scopus 로고    scopus 로고
    • Interleukin 1alpha and the inflammatory process
    • PID: 27434011
    • Di Paolo NC, Shayakhmetov DM. Interleukin 1alpha and the inflammatory process. Nat Immunol. 2016;17:906–13
    • (2016) Nat Immunol , vol.17 , pp. 906-913
    • Di Paolo, N.C.1    Shayakhmetov, D.M.2
  • 150
    • 84873152891 scopus 로고    scopus 로고
    • A role of RIP3-mediated macrophage necrosis in atherosclerosis development
    • COI: 1:CAS:528:DC%2BC3sXht1Gjtr8%3D, PID: 23333278
    • Lin J, Li H, Yang M, Ren J, Huang Z, Han F, et al. A role of RIP3-mediated macrophage necrosis in atherosclerosis development. Cell Rep. 2013;3:200–10
    • (2013) Cell Rep , vol.3 , pp. 200-210
    • Lin, J.1    Li, H.2    Yang, M.3    Ren, J.4    Huang, Z.5    Han, F.6
  • 151
    • 84903127232 scopus 로고    scopus 로고
    • A tissue-specific role for Nlrp3 in tubular epithelial repair after renal ischemia/reperfusion
    • COI: 1:CAS:528:DC%2BC2cXhtVarsrrI, PID: 5707188
    • Bakker PJ, Butter LM, Claessen N, Teske GJ, Sutterwala FS, Florquin S, et al. A tissue-specific role for Nlrp3 in tubular epithelial repair after renal ischemia/reperfusion. Am J Pathol. 2014;184:2013–22
    • (2014) Am J Pathol , vol.184 , pp. 2013-2022
    • Bakker, P.J.1    Butter, L.M.2    Claessen, N.3    Teske, G.J.4    Sutterwala, F.S.5    Florquin, S.6
  • 152
    • 78650659200 scopus 로고    scopus 로고
    • An inflammasome-independent role for epithelial-expressed Nlrp3 in renal ischemia-reperfusion injury
    • COI: 1:CAS:528:DC%2BC3cXhtlOhsbnL, PID: 3020135
    • Shigeoka AA, Mueller JL, Kambo A, Mathison JC, King AJ, Hall WF, et al. An inflammasome-independent role for epithelial-expressed Nlrp3 in renal ischemia-reperfusion injury. J Immunol. 2010;185:6277–85
    • (2010) J Immunol , vol.185 , pp. 6277-6285
    • Shigeoka, A.A.1    Mueller, J.L.2    Kambo, A.3    Mathison, J.C.4    King, A.J.5    Hall, W.F.6
  • 153
    • 84855504820 scopus 로고    scopus 로고
    • Sterile inflammation of endothelial cell-derived apoptotic bodies is mediated by interleukin-1alpha
    • COI: 1:CAS:528:DC%2BC38Xkt1Kqsg%3D%3D
    • Berda-Haddad Y, Robert S, Salers P, Zekraoui L, Farnarier C, Dinarello CA, et al. Sterile inflammation of endothelial cell-derived apoptotic bodies is mediated by interleukin-1alpha. Proc Natl Acad Sci USA. 2011;108:20684–9
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 20684-20689
    • Berda-Haddad, Y.1    Robert, S.2    Salers, P.3    Zekraoui, L.4    Farnarier, C.5    Dinarello, C.A.6
  • 154
    • 84901422731 scopus 로고    scopus 로고
    • RIPK1 regulates RIPK3-MLKL driven systemic inflammation and emergency hematopoiesis
    • COI: 1:CAS:528:DC%2BC2cXnslGms78%3D, PID: 24813849
    • Rickard JA, O’Donnell JA, Evans JM, Lalaoui N, Poh AR, Rogers TW, et al. RIPK1 regulates RIPK3-MLKL driven systemic inflammation and emergency hematopoiesis. Cell. 2014;157:1175–88
    • (2014) Cell , vol.157 , pp. 1175-1188
    • Rickard, J.A.1    O’Donnell, J.A.2    Evans, J.M.3    Lalaoui, N.4    Poh, A.R.5    Rogers, T.W.6
  • 155
    • 51049100571 scopus 로고    scopus 로고
    • Stimulation of Toll-like receptor 3 and 4 induces interleukin-1beta maturation by caspase-8
    • COI: 1:CAS:528:DC%2BD1cXhtV2isrbI, PID: 2526192
    • Maelfait J, Vercammen E, Janssens S, Schotte P, Haegman M, Magez S, et al. Stimulation of Toll-like receptor 3 and 4 induces interleukin-1beta maturation by caspase-8. J Exp Med. 2008;205:1967–73
    • (2008) J Exp Med , vol.205 , pp. 1967-1973
    • Maelfait, J.1    Vercammen, E.2    Janssens, S.3    Schotte, P.4    Haegman, M.5    Magez, S.6
  • 156
    • 84881184694 scopus 로고    scopus 로고
    • Mlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosis
    • COI: 1:CAS:528:DC%2BC3sXht1Wltb7F, PID: 3731568
    • Wu J, Huang Z, Ren J, Zhang Z, He P, Li Y, et al. Mlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosis. Cell Res. 2013;23:994–1006
    • (2013) Cell Res , vol.23 , pp. 994-1006
    • Wu, J.1    Huang, Z.2    Ren, J.3    Zhang, Z.4    He, P.5    Li, Y.6
  • 157
    • 68249137289 scopus 로고    scopus 로고
    • Suppression of interleukin-33 bioactivity through proteolysis by apoptotic caspases
    • COI: 1:CAS:528:DC%2BD1MXpsFOgurk%3D
    • Luthi AU, Cullen SP, McNeela EA, Duriez PJ, Afonina IS, Sheridan C, et al. Suppression of interleukin-33 bioactivity through proteolysis by apoptotic caspases. Immunity. 2009;31:84–98
    • (2009) Immunity , vol.31 , pp. 84-98
    • Luthi, A.U.1    Cullen, S.P.2    McNeela, E.A.3    Duriez, P.J.4    Afonina, I.S.5    Sheridan, C.6
  • 158
    • 27744446058 scopus 로고    scopus 로고
    • IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST2 and induces T helper type 2-associated cytokines
    • COI: 1:CAS:528:DC%2BD2MXht12msr7K
    • Schmitz J, Owyang A, Oldham E, Song Y, Murphy E, McClanahan TK, et al. IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST2 and induces T helper type 2-associated cytokines. Immunity. 2005;23:479–90
    • (2005) Immunity , vol.23 , pp. 479-490
    • Schmitz, J.1    Owyang, A.2    Oldham, E.3    Song, Y.4    Murphy, E.5    McClanahan, T.K.6
  • 159
    • 67651053209 scopus 로고    scopus 로고
    • Interleukin-33 is biologically active independently of caspase-1 cleavage
    • COI: 1:CAS:528:DC%2BD1MXot12kuro%3D, PID: 2740567
    • Talabot-Ayer D, Lamacchia C, Gabay C, Palmer G. Interleukin-33 is biologically active independently of caspase-1 cleavage. J Biol Chem. 2009;284:19420–6
    • (2009) J Biol Chem , vol.284 , pp. 19420-19426
    • Talabot-Ayer, D.1    Lamacchia, C.2    Gabay, C.3    Palmer, G.4
  • 160
    • 67049158193 scopus 로고    scopus 로고
    • The IL-1-like cytokine IL-33 is inactivated after maturation by caspase-1
    • COI: 1:CAS:528:DC%2BD1MXntlyhtbY%3D
    • Cayrol C, Girard JP. The IL-1-like cytokine IL-33 is inactivated after maturation by caspase-1. Proc Natl Acad Sci USA. 2009;106:9021–6
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9021-9026
    • Cayrol, C.1    Girard, J.P.2
  • 161
    • 84939631887 scopus 로고    scopus 로고
    • Caspase-1 activation by NLRP3 inflammasome dampens IL-33-dependent house dust mite-induced allergic lung inflammation
    • COI: 1:CAS:528:DC%2BC28XitFWks73N
    • Madouri F, Guillou N, Fauconnier L, Marchiol T, Rouxel N, Chenuet P, et al. Caspase-1 activation by NLRP3 inflammasome dampens IL-33-dependent house dust mite-induced allergic lung inflammation. J Mol Cell Biol. 2015;7:351–65
    • (2015) J Mol Cell Biol , vol.7 , pp. 351-365
    • Madouri, F.1    Guillou, N.2    Fauconnier, L.3    Marchiol, T.4    Rouxel, N.5    Chenuet, P.6
  • 163
    • 85018941706 scopus 로고    scopus 로고
    • Role of NLRP3 inflammasomes in atherosclerosis
    • COI: 1:CAS:528:DC%2BC1cXitlGitb3N, PID: 5429158
    • Karasawa T, Takahashi M. Role of NLRP3 inflammasomes in atherosclerosis. J Atheroscler Thromb. 2017;24:443–51
    • (2017) J Atheroscler Thromb , vol.24 , pp. 443-451
    • Karasawa, T.1    Takahashi, M.2
  • 164
    • 85029568219 scopus 로고    scopus 로고
    • Antiinflammatory therapy with canakinumab for atherosclerotic disease
    • COI: 1:CAS:528:DC%2BC2sXhsFOqurnE, PID: 28845751
    • Ridker PM, Everett BM, Thuren T, MacFadyen JG, Chang WH, Ballantyne C, et al. Antiinflammatory therapy with canakinumab for atherosclerotic disease. N Engl J Med. 2017;377:1119–31
    • (2017) N Engl J Med , vol.377 , pp. 1119-1131
    • Ridker, P.M.1    Everett, B.M.2    Thuren, T.3    MacFadyen, J.G.4    Chang, W.H.5    Ballantyne, C.6
  • 165
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NALP3 inflammasome
    • COI: 1:CAS:528:DC%2BD28XitFGitLg%3D
    • Martinon F, Pétrilli V, Mayor A, Tardivel A, Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature. 2006;440:237–41
    • (2006) Nature , vol.440 , pp. 237-241
    • Martinon, F.1    Pétrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 167
    • 84937577488 scopus 로고    scopus 로고
    • Diverse activators of the NLRP3 inflammasome promote IL-1beta secretion by triggering necrosis
    • COI: 1:CAS:528:DC%2BC2MXpt1Sks7g%3D, PID: 26027935
    • Cullen SP, Kearney CJ, Clancy DM, Martin SJ. Diverse activators of the NLRP3 inflammasome promote IL-1beta secretion by triggering necrosis. Cell Rep. 2015;11:1535–48
    • (2015) Cell Rep , vol.11 , pp. 1535-1548
    • Cullen, S.P.1    Kearney, C.J.2    Clancy, D.M.3    Martin, S.J.4
  • 168
    • 85039941671 scopus 로고    scopus 로고
    • The inflammasome drives GSDMD-independent secondary pyroptosis and IL-1 release in the absence of caspase-1 protease activity
    • COI: 1:CAS:528:DC%2BC2sXitVeksb%2FE, PID: 5750195
    • Schneider KS, Gross CJ, Dreier RF, Saller BS, Mishra R, Gorka O, et al. The inflammasome drives GSDMD-independent secondary pyroptosis and IL-1 release in the absence of caspase-1 protease activity. Cell Rep. 2017;21:3846–59
    • (2017) Cell Rep , vol.21 , pp. 3846-3859
    • Schneider, K.S.1    Gross, C.J.2    Dreier, R.F.3    Saller, B.S.4    Mishra, R.5    Gorka, O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.