Caspase-8 Blocks Kinase RIPK3-Mediated Activation of the NLRP3 Inflammasome
Open accessAbstract
Caspase-8 deficiency in certain cells prompts chronic inflammation. One mechanism suggested to account for this inflammation is enhanced signaling for necrotic cell death, mediated by the protein kinases RIPK1 and RIPK3 that caspase-8 can cleave. We describe an activity of caspase-8 in dendritic cells that controls the initiation of inflammation in another way. Caspase-8 deficiency in these cells facilitated lipopolysaccharide-induced assembly and function of the NLRP3 inflammasome. This effect depended on the functions of RIPK1 and RIPK3, as well as of MLKL and PGAM5, two signaling proteins recently shown to contribute to RIPK3-mediated induction of necrosis. However, although enhancement of inflammasome assembly in the caspase-8-deficient cells shares proximal signaling events with the induction of necrosis, it occurred independently of cell death. These findings provide new insight into potentially pathological inflammatory processes to which RIPK1- and RIPK3-mediated signaling contributes.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Multiple components of molecular machinery for necroptosis-including ZBP1, RIPK3, MLKL, and TNFR1 (mainly via NF-κB)-impinge on control of inflammasome, a supramolecular platform for activation of CASP1 and consequent secretion of mature IL1B and IL18.
“Importantly, multiple components of the molecular machinery for necroptosis—including ZBP1, RIPK3, MLKL, and TNFR1 (mainly via NF-κB)—impinge on the control of the so-called “inflammasome”, a supramolecular platform for the activation of CASP1 and consequent secretion of mature interleukin 1 beta (IL1B; best known as IL-1β) and IL18 [524–529].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [527]
Cites
Schroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475 · see citing works
Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
Degterev, A., Huang, Z., Boyce, M., Li, Y., Jagtap, P., Mizushima, N., Cuny, G. D., Mitchison, T. J., Moskowitz, M. A., & Yuan, J. (2005) · Nature Chemical Biology · doi:10.1038/nchembio711 · Cited by 3,068 · see citing works
Muzio, M., Chinnaiyan, A. M., Kischkel, F. C., O'Rourke, K., Shevchenko, A., Ni, J., Scaffidi, C., Bretz, J. D., Zhang, M., Gentz, R., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81266-0 · Cited by 3,046 · see citing works
Mixed Lineage Kinase Domain-like Protein Mediates Necrosis Signaling Downstream of RIP3 Kinase
Sun, L., Wang, H., Wang, Z., He, S., Chen, S., Liao, D., Wang, L., Yan, J., Liu, W., Lei, X., et al. (2012) · Cell · doi:10.1016/j.cell.2011.11.031 · Cited by 2,698 · see citing works
Cho, Y., Challa, S., Moquin, D., Genga, R., Ray, T. D., Guildford, M., & Chan, F. K.-M. (2009) · Cell · doi:10.1016/j.cell.2009.05.037 · Cited by 2,435 · see citing works
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382 · see citing works
Boldin, M. P., Goncharov, T. M., Goltseve, Y. V., & Wallach, D. (1996) · Cell · doi:10.1016/s0092-8674(00)81265-9 · Cited by 2,292 · see citing works
Self-citationReceptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-α
He, S., Wang, L., Miao, L., Wang, T., Du, F., Zhao, L., & Wang, X. (2009) · Cell · doi:10.1016/j.cell.2009.05.021 · Cited by 2,214 · see citing works
Conditional gene targeting in macrophages and granulocytes using LysMcre mice
Clausen, B. E., Burkhardt, C., Reith, W., Renkawitz, R., & Förster, I. (1999) · Transgenic Research · doi:10.1023/a:1008942828960 · Cited by 2,143 · see citing works
Identification of RIP1 kinase as a specific cellular target of necrostatins
Degterev, A., Hitomi, J., Germscheid, M., Ch'en, I. L., Korkina, O., Teng, X., Abbott, D., Cuny, G. D., Yuan, C., Wagner, G., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.83 · Cited by 2,059 · see citing works
Holler, N., Zaru, R., Micheau, O., Thome, M., Attinger, A., Valitutti, S., Bodmer, J.-L., Schneider, P., Seed, B., & Tschopp, J. (2000) · Nature Immunology · doi:10.1038/82732 · Cited by 1,932 · see citing works
RIP3, an Energy Metabolism Regulator That Switches TNF-Induced Cell Death from Apoptosis to Necrosis
Zhang, D.-W., Shao, J., Lin, J., Zhang, N., Lu, B.-J., Lin, S.-C., Dong, M.-Q., & Han, J. (2009) · Science · doi:10.1126/science.1172308 · Cited by 1,931 · see citing works
Molecular mechanisms of caspase regulation during apoptosis
Riedl, S. J., & Shi, Y. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1496 · Cited by 1,893 · see citing works
Varfolomeev, E., Schuchmann, M., Luria, V., Chiannilkulchai, N., Beckmann, J., Mett, I., Rebrikov, D., Brodianski, V. M., Kemper, O., Kollet, O., et al. (1998) · Immunity · doi:10.1016/s1074-7613(00)80609-3 · Cited by 1,332 · see citing works
Self-citationCatalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosis
Oberst, A., Dillon, C. P., Weinlich, R., McCormick, L. L., Fitzgerald, P., Pop, C., Hakem, R., Salvesen, G. S., & Green, D. R. (2011) · Nature · doi:10.1038/nature09852 · Cited by 1,278 · see citing works
RIP3 mediates the embryonic lethality of caspase-8-deficient mice
Kaiser, W. J., Upton, J. W., Long, A. B., Livingston-Rosanoff, D., Daley-Bauer, L. P., Hakem, R., Caspary, T., & Mocarski, E. S. (2011) · Nature · doi:10.1038/nature09857 · Cited by 1,057 · see citing works
Sensing and reacting to microbes through the inflammasomes
Franchi, L., Muñoz-Planillo, R., & Núñez, G. (2012) · Nature Immunology · doi:10.1038/ni.2231 · Cited by 1,013 · see citing works
Hitomi, J., Christofferson, D. E., Ng, A., Yao, J., Degterev, A., Xavier, R. J., & Yuan, J. (2008) · Cell · doi:10.1016/j.cell.2008.10.044 · Cited by 989 · see citing works
Wang, Z., Jiang, H., Chen, S., Du, F., & Wang, X. (2012) · Cell · doi:10.1016/j.cell.2011.11.030 · Cited by 949 · see citing works
The Inflammatory Response to Cell Death
Rock, K. L., & Kono, H. (2007) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.3.121806.151456 · Cited by 945 · see citing works
Galactosamine-induced sensitization to the lethal effects of endotoxin.
Galanos, C., Freudenberg, M. A., & Reutter, W. G. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.11.5939 · Cited by 938 · see citing works
Zhao, J., Jitkaew, S., Cai, Z., Choksi, S., Li, Q., Luo, J., & Liu, Z.-G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200012109 · Cited by 901 · see citing works
Notch–RBP-J signaling controls the homeostasis of CD8− dendritic cells in the spleen
Caton, M. L., Smith-Raska, M., & Reizis, B. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20062648 · Cited by 864 · see citing works
Feoktistova, M., Geserick, P., Kellert, B., Panayotova‐Dimitrova, D., Langlais, C., Hupe, M., Cain, K., MacFarlane, M., Häcker, G. A., & Leverkus, M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.011 · Cited by 855 · see citing works
Cleavage of the death domain kinase RIP by Caspase-8 prompts TNF-induced apoptosisPreprint
Lin, Y., Devin, A., Rodriguez, Y., & Liu, Z.-G. (1999) · Genes & Development · doi:10.1101/gad.13.19.2514 · Cited by 835 · see citing works
He, S., Liang, Y., Shao, F., & Wang, X. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116302108 · Cited by 725 · see citing works
Gringhuis, S. I., Kaptein, T. M., Wevers, B. A., Theelen, B., van der Vlist, M., Boekhout, T., & Geijtenbeek, T. B. H. (2012) · Nature Immunology · doi:10.1038/ni.2222 · Cited by 612 · see citing works
RIP Kinase-Dependent Necrosis Drives Lethal Systemic Inflammatory Response Syndrome
Duprez, L., Takahashi, N., Hauwermeiren, F. V., Vandendriessche, B., Goossens, V., Berghe, T. V., Declercq, W., Libert, C., Cauwels, A., & Vandenabeele, P. (2011) · Immunity · doi:10.1016/j.immuni.2011.09.020 · Cited by 591 · see citing works
Inhibition of Fas death signals by FLIPs
Tschopp, J., Irmler, M., & Thome, M. (1998) · Current Opinion in Immunology · doi:10.1016/s0952-7915(98)80223-9 · Cited by 527 · see citing works
Inhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation
Vince, J. E., Wong, W. W.-L., Gentle, I., Lawlor, K. E., Allam, R., O'Reilly, L., Mason, K., Gross, O., Ma, S., Guarda, G., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.012 · Cited by 491 · see citing works
Phagocyte receptors for apoptotic cells: recognition, uptake, and consequences
Fadok, V. A., Bratton, D. L., & Henson, P. M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci14122 · Cited by 474 · see citing works
Piccini, A., Carta, S., Tassi, S., Lasigliè, D., Fossati, G., & Rubartelli, A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709684105 · Cited by 460 · see citing works
Developmental kinetics and lifespan of dendritic cells in mouse lymphoid organs
Kamath, A. T., Henri, S., Battye, F. L., Tough, D. F., & Shortman, K. (2002) · Blood · doi:10.1182/blood.v100.5.1734.h81702001734_1734_1741 · Cited by 454 · see citing works
Caspase-8 Serves Both Apoptotic and Nonapoptotic Roles1
Kang, T., Ben-Moshe, T., Varfolomeev, E., Pewzner‐Jung, Y., Yogev, N., Jurewicz, A., Waisman, A., Brenner, O., Haffner, R., Gustafsson, E., et al. (2004) · Journal of Immunology · doi:10.4049/jimmunol.173.5.2976 · Cited by 425 · see citing works
Self-citationPore dilation of neuronal P2X receptor channels
Virginio, C., MacKenzie, A., Rassendren, F. A., North, R. A., & Surprenant, A. (1999) · Nature Neuroscience · doi:10.1038/7225 · Cited by 414 · see citing works
Phagocyte receptors for apoptotic cells: recognition, uptake, and consequences
Fadok, V. A., Bratton, D. L., & Henson, P. M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200114122 · Cited by 409 · see citing works
Vanlangenakker, N., Vanden Berghe, T., Bogaert, P., Laukens, B., Zobel, K., Deshayes, K., Vucic, D., Fulda, S., Vandenabeele, P., & Bertrand, M. J. M. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.138 · Cited by 339 · see citing works
Basal Release of ATP: An Autocrine-Paracrine Mechanism for Cell Regulation
Corriden, R., & Insel, P. A. (2010) · Science Signaling · doi:10.1126/scisignal.3104re1 · Cited by 338 · see citing works
Necrostatin: A Potentially Novel Cardioprotective Agent?
Smith, C., Davidson, S. M., Lim, S. Y., Simpkin, J. C., Hothersall, J. S., & Yellon, D. M. (2007) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-007-6035-1 · Cited by 327 · see citing works
Non‐specific effects of methyl ketone peptide inhibitors of caspases
Schotte, P., Declercq, W., Huffel, S. V., Vandenabeele, P., & Beyaert, R. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01640-8 · Cited by 302 · see citing works
Viral infection and the evolution of caspase 8-regulated apoptotic and necrotic death pathways
Mocarski, E. S., Upton, J. W., & Kaiser, W. J. (2011) · Nature reviews. Immunology · doi:10.1038/nri3131 · Cited by 300 · see citing works
Caspase-8 deficiency in epidermal keratinocytes triggers an inflammatory skin disease
Kovalenko, A., Kim, J., Kang, T., Rajput, A., Bogdanov, K., Dittrich‐Breiholz, O., Kracht, M., Brenner, O. J., & Wallach, D. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20090616 · Cited by 212 · see citing works
Self-citationRajput, A., Kovalenko, A., Bogdanov, K., Yang, S., Kang, T., Kim, J., Du, J., & Wallach, D. (2011) · Immunity · doi:10.1016/j.immuni.2010.12.018 · Cited by 203 · see citing works
Self-citationRIPK-Dependent Necrosis and Its Regulation by Caspases: A Mystery in Five Acts
Green, D. R., Oberst, A., Dillon, C. P., Weinlich, R., & Salvesen, G. S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.003 · Cited by 169 · see citing works
Reprieval from execution: the molecular basis of caspase inhibition
Stennicke, H. R., Ryan, C., & Salvesen, G. S. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)02045-x · Cited by 162 · see citing works
Kang, T., Oh, G., Scandella, E., Bolinger, B., Ludewig, B., Kovalenko, A., & Wallach, D. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.4.2522 · Cited by 138 · see citing works
Self-citationCD95 (Fas)-induced caspase-mediated proteolysis of NF-kappaB.
Ravi, R. K., Bedi, A., Fuchs, E. J., & Bedi, A. (1998) · PubMed · Cited by 120 · see citing works
Proliferative versus apoptotic functions of caspase-8
van Raam, B. J., & Salvesen, G. S. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.06.005 · Cited by 90 · see citing works
Role of caspase‐8 in hepatocyte response to infection and injury in mice†
Moshe, T. B., Barash, H., Kang, T., Kim, J., Kovalenko, A., Gross, E., Schuchmann, M., Abramovitch, R., Galun, E., & Wallach, D. (2007) · Hepatology · doi:10.1002/hep.21495 · Cited by 83 · see citing works
Self-citationNihei, O. K., de Carvalho, A. C. C., Savino, W., & Alves, L. A. (2000) · Blood · doi:10.1182/blood.v96.3.996 · Cited by 67 · see citing works
Inhibition of programmed cell death by cytomegaloviruses
Brune, W. (2010) · Virus Research · doi:10.1016/j.virusres.2010.10.012 · Cited by 58 · see citing works
Mankan, A. K., Kubarenko, A. V., & Hornung, V. (2011) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2011.04534.x · Cited by 55 · see citing works
‘Necrosome’-induced inflammation: must cells die for it?
Wallach, D., Kovalenko, A., & Kang, T. (2011) · Trends in Immunology · doi:10.1016/j.it.2011.07.004 · Cited by 48 · see citing works
Self-citationCell-autonomous and non-cell-autonomous functions of caspase-8
Moshe, T. B., Kang, T., Kovalenko, A., et al. (2008) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2008.04.012 · Cited by 11 · see citing works
Self-citationAnti‐inflammatory functions of the “apoptotic” caspases
Wallach, D., Kang, T., Rajput, A., Kim, J., Bogdanov, K., Yang, S., & Kovalenko, A. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05742.x · Cited by 9 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works
Self-citationRegulated necrosis: the expanding network of non-apoptotic cell death pathways
Berghe, T. V., Linkermann, A., Jouan-Lanhouet, S., Walczak, H., & Vandenabeele, P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3737 · Cited by 1,735 · see citing works
NLRP3 inflammasome activation and cell death
Huang, Y., Xu, W., & Zhou, R. (2021) · Cellular & Molecular Immunology · doi:10.1038/s41423-021-00740-6 · Cited by 1,527 · see citing works
Necroptosis: The Release of Damage-Associated Molecular Patterns and Its Physiological Relevance
Kaczmarek, A., Vandenabeele, P., & Krysko, D. V. (2013) · Immunity · doi:10.1016/j.immuni.2013.02.003 · Cited by 1,411 · see citing works
Linkermann, A., & Green, D. R. (2014) · New England Journal of Medicine · doi:10.1056/nejmra1310050 · Cited by 1,103 · see citing works
Pyroptosis versus necroptosis: similarities, differences, and crosstalk
Frank, D., & Vince, J. E. (2019) · Cell Death & Differentiation · doi:10.1038/s41418-018-0212-6 · Cited by 1,062 · see citing works
Necroptosis in development, inflammation and disease
Weinlich, R., Oberst, A., Beere, H. M., & Green, D. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.149 · Cited by 1,016 · see citing works
ESCRT-III Acts Downstream of MLKL to Regulate Necroptotic Cell Death and Its Consequences
Gong, Y.-N., Guy, C., Olauson, H., Becker, J. U., Yang, M., Fitzgerald, P., Linkermann, A., & Green, D. R. (2017) · Cell · doi:10.1016/j.cell.2017.03.020 · Cited by 689 · see citing works
Regulated necrosis: disease relevance and therapeutic opportunities
Conrad, M., Angeli, J. P. F., Vandenabeele, P., & Stockwell, B. R. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.6 · Cited by 630 · see citing works
Apoptosis and necroptosis in the liver: a matter of life and death
Schwabe, R. F., & Luedde, T. (2018) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-018-0065-y · Cited by 582 · see citing works
RIPK1 Blocks Early Postnatal Lethality Mediated by Caspase-8 and RIPK3
Dillon, C. P., Weinlich, R., Rodriguez, D. A., Cripps, J. G., Quarato, G., Gurung, P., Verbist, K. C., Brewer, T. L., Llambi, F., Gong, Y.-N., et al. (2014) · Cell · doi:10.1016/j.cell.2014.04.018 · Cited by 562 · see citing works
Regulated cell death and inflammation: an auto-amplification loop causes organ failure
Linkermann, A., Stockwell, B. R., Krautwald, S., & Anders, H.-J. (2014) · Nature Reviews Immunology · doi:10.1038/nri3743 · Cited by 522 · see citing works
Eckhart, L., Lippens, S., Tschachler, E., & Declercq, W. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.010 · Cited by 515 · see citing works
Mechanisms of inflammasome activation: recent advances and novel insights
Vanaja, S. K., Rathinam, V. A. K., & Fitzgerald, K. A. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.12.009 · Cited by 499 · see citing works
Necroptosis in health and diseases
Zhou, W., & Yuan, J. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.07.013 · Cited by 414 · see citing works
Immunological impact of cell death signaling driven by radiation on the tumor microenvironment
Rodriguez-Ruiz, M. E., Vitale, I., Harrington, K. J., Melero, I., & Galluzzi, L. (2020) · Nature Immunology · doi:10.1038/s41590-019-0561-4 · Cited by 385 · see citing works
Die another way – non-apoptotic mechanisms of cell death
Tait, S. W. G., Ichim, G., & Green, D. R. (2014) · Journal of Cell Science · doi:10.1242/jcs.093575 · Cited by 366 · see citing works
Caspases Connect Cell-Death Signaling to Organismal Homeostasis
Galluzzi, L., López-Soto, A., Kumar, S., & Kroemer, G. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.020 · Cited by 350 · see citing works
XIAP Restricts TNF- and RIP3-Dependent Cell Death and Inflammasome Activation
Yabal, M., Müller, N., Adler, H., Knies, N., Groß, C. J., Damgaard, R. B., Kanegane, H., Ringelhan, M., Kaufmann, T., Heikenwälder, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.008 · Cited by 255 · see citing works
Molecular mechanisms of regulated necrosis
Galluzzi, L., Kepp, O., Krautwald, S., Kroemer, G., & Linkermann, A. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.02.006 · Cited by 258 · see citing works
Alvarez-Diaz, S., Dillon, C. P., Lalaoui, N., Tanzer, M. C., Rodriguez, D. A., Lin, A., Lebois, M., Hakem, R., Josefsson, E. C., O’Reilly, L. A., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.07.016 · Cited by 242 · see citing works
Vlantis, K., Wullaert, A., Polykratis, A., Kondylis, V., Dannappel, M., Schwarzer, R., Welz, P., Corona, T., Walczak, H., Weih, F., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.02.020 · Cited by 189 · see citing works
Protective Roles for Caspase-8 and cFLIP in Adult Homeostasis
Weinlich, R., Oberst, A., Dillon, C. P., Janke, L. J., Milasta, S., Lukens, J. R., Rodriguez, D. A., Gurung, P., Savage, C., Kanneganti, T. D., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.045 · Cited by 157 · see citing works
The NLRP3 inflammasome renders cell death pro-inflammatory
Gaidt, M. M., & Hornung, V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.11.013 · Cited by 124 · see citing works
Moriwaki, K., Farias Luz, N., Balaji, S., De Rosa, M. J., O’Donnell, C. L., Gough, P. J., Bertin, J., Welsh, R. M., & Chan, F. K.-M. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501662 · Cited by 116 · see citing works
Zhang, X., Fan, C., Zhang, H., Zhao, Q., Liu, Y., Xu, C., Xie, Q., Wu, X., Yu, X., Zhang, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.06.103 · Cited by 93 · see citing works
The Tumor Suppressor Hace1 Is a Critical Regulator of TNFR1-Mediated Cell Fate
Tortola, L., Nitsch, R., Bertrand, M. J. M., Kogler, M., Redouane, Y., Kozieradzki, I., Uribesalgo, I., Fennell, L. M., Daugaard, M., Klug, H., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.032 · Cited by 64 · see citing works
Zhao, Q., Yu, X., Zhang, H., Liu, Y., Zhang, X., Wu, X., Xie, Q., Li, M., Ying, H., & Zhang, H. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.04.011 · Cited by 49 · see citing works
Macrophage Nogo-B Drives Liver Fibrosis
Zhang, L., Ni, M., Si, J., Cheng, F., Zhang, L., Liang, Y., Liu, M., Li, W., Li, J., Chi, Y., et al. (2026) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2025.101622 · Cited by 1 · see citing works
- Authors
- Kang, T.-B., Yang, S.-H., Toth, B., Kovalenko, A., & Wallach, D.
- Affiliations
- Konkuk University (KR)
- Weizmann Institute of Science (IL)
- Corresponding author
- Wallach, David
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2013-01
- Volume
- 38
- Issue
- 1
- Pages
- 27-40
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W2078252006
- Cited by
- 419
- References
- 55
- Citations by year
- 2026: 8 · 2025: 20 · 2024: 21 · 2023: 16 · 2022: 32 · 2021: 24 · 2020: 33 · 2019: 28 · 2018: 36 · 2017: 30 · 2016: 38 · 2015: 40 · 2014: 58 · 2013: 35
- FWCI
- 17.11
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Immunity (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- caspase-8, NLRP3 inflammasome, RIPK3, RIPK1, MLKL, PGAM5, dendritic cells, lipopolysaccharide, inflammasome assembly, necrosis, chronic inflammation
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Carrier Proteins, Cells, Cultured, Dendritic Cells, Lipopolysaccharides, Signal Transduction, Transcriptional Activation, Gene Deletion, Mice, Caspase 8, Receptor-Interacting Protein Serine-Threonine Kinases, Interleukin-1beta, Inflammasomes
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
