RIPK1 maintains epithelial homeostasis by inhibiting apoptosis and necroptosis
Open accessAbstract
Necroptosis has emerged as an important pathway of programmed cell death in embryonic development, tissue homeostasis, immunity and inflammation. RIPK1 is implicated in inflammatory and cell death signalling and its kinase activity is believed to drive RIPK3-mediated necroptosis. Here we show that kinase-independent scaffolding RIPK1 functions regulate homeostasis and prevent inflammation in barrier tissues by inhibiting epithelial cell apoptosis and necroptosis. Intestinal epithelial cell (IEC)-specific RIPK1 knockout caused IEC apoptosis, villus atrophy, loss of goblet and Paneth cells and premature death in mice. This pathology developed independently of the microbiota and of MyD88 signalling but was partly rescued by TNFR1 (also known as TNFRSF1A) deficiency. Epithelial FADD ablation inhibited IEC apoptosis and prevented the premature death of mice with IEC-specific RIPK1 knockout. However, mice lacking both RIPK1 and FADD in IECs displayed RIPK3-dependent IEC necroptosis, Paneth cell loss and focal erosive inflammatory lesions in the colon. Moreover, a RIPK1 kinase inactive knock-in delayed but did not prevent inflammation caused by FADD deficiency in IECs or keratinocytes, showing that RIPK3-dependent necroptosis of FADD-deficient epithelial cells only partly requires RIPK1 kinase activity. Epidermis-specific RIPK1 knockout triggered keratinocyte apoptosis and necroptosis and caused severe skin inflammation that was prevented by RIPK3 but not FADD deficiency. These findings revealed that RIPK1 inhibits RIPK3-mediated necroptosis in keratinocytes in vivo and identified necroptosis as a more potent trigger of inflammation compared with apoptosis. Therefore, RIPK1 is a master regulator of epithelial cell survival, homeostasis and inflammation in the intestine and the skin.
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Absence of Ripk1 from keratinocytes promotes spontaneous necroptosis and consequent cutaneous inflammation, which can be prevented by co-deletion of Ripk3, Mlkl, or Zbp1 but not Fadd.
“Likewise, the absence of Ripk1 from keratinocytes promotes spontaneous necroptosis and consequent cutaneous inflammation, which can be prevented by the co-deletion of Ripk3, Mlkl, or Zbp1 but not Fadd [440, 502].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [502]
Conditional knockout mouse models demonstrate key role of RIPK1 for preservation of intestinal and cutaneous homeostasis and survival.
“Conditional knockout mouse models demonstrate the key role of RIPK1 for the preservation of intestinal and cutaneous homeostasis and survival [502, 503].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [502]
Mice lacking Ripk1 in intestinal epithelial cells display increased rates of spontaneous CASP8-driven apoptosis and develop severe inflammatory lesions leading to premature death, a phenotype that can be prevented by co-deleting Fadd or (to lesser degree) Tnfrsf1a.
“In particular, mice lacking Ripk1 in intestinal epithelial cells display increased rates of spontaneous CASP8-driven apoptosis and develop severe inflammatory lesions leading to premature death, a detrimental phenotype that can be prevented by co-deleting Fadd or (to a lesser degree) Tnfrsf1a [502].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [502]
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Single Lgr5 stem cells build crypt-villus structures in vitro without a mesenchymal niche
Sato, T., Vries, R. G., Snippert, H. J., van de Wetering, M., Barker, N., Stange, D. E., van Es, J. H., Abo, A., Kujala, P., Peters, P. J., et al. (2009) · Nature · doi:10.1038/nature07935 · Cited by 7,204 · see citing works
IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
Kawai, T., Takahashi, K., Sato, S., Coban, C., Kumar, H., Kato, H., Ishii, K. J., Takeuchi, O., & Akira, S. (2005) · Nature Immunology · doi:10.1038/ni1243 · Cited by 2,562 · see citing works
IKKβ Links Inflammation and Tumorigenesis in a Mouse Model of Colitis-Associated Cancer
Greten, F. R., Eckmann, L., Greten, T. F., Park, J. M., Li, Z.-W., Egan, L. J., Kagnoff, M. F., & Karin, M. (2004) · Cell · doi:10.1016/j.cell.2004.07.013 · Cited by 2,433 · see citing works
Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-mediated function.
Adachi, O., Kawai, T., Takeda, K., Matsumoto, M., Tsutsui, H., Sakagami, M., Nakanishi, K., & Akira, S. (1998) · Immunity · doi:10.1016/s1074-7613(00)80596-8 · Cited by 2,358 · see citing works
Improving CRISPR-Cas nuclease specificity using truncated guide RNAs
Fu, Y., Sander, J. D., Reyon, D., Cascio, V. M., & Joung, J. K. (2014) · Nature Biotechnology · doi:10.1038/nbt.2808 · Cited by 1,993 · see citing works
Kaser, A., Zeissig, S., & Blumberg, R. S. (2010) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101225 · Cited by 1,806 · see citing works
Regulated 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
Pfeffer, K., Matsuyama, T., Kündig, T. M., Wakeham, A., Kishihara, K., Shahinian, A., Wiegmann, K., Ohashi, P. S., Krönke, M., & Mak, T. W. (1993) · Cell · doi:10.1016/0092-8674(93)90134-c · Cited by 1,677 · see citing works
Schwenk, F., Baron, U., & Rajewsky, K. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.24.5080 · Cited by 1,289 · see citing works
Catalytic 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
IAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis
Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218 · see citing works
High-efficiency deleter mice show that FLPe is an alternative to Cre-loxP
Rodríguez, C. I., Buchholz, F., Galloway, J. L., Sequerra, R., Kasper, J. S., Ayala, R., Stewart, A. F., & Dymecki, S. M. (2000) · Nature Genetics · doi:10.1038/75973 · Cited by 1,162 · see citing works
The Death Domain Kinase RIP Mediates the TNF-Induced NF-κB Signal
Kelliher, M. A., Grimm, S., Ishida, Y., Kuo, F., Stanger, B. Z., & Leder, P. (1998) · Immunity · doi:10.1016/s1074-7613(00)80535-x · Cited by 1,102 · see citing works
Self-citationEpithelial NEMO links innate immunity to chronic intestinal inflammation
Nenci, A., Becker, C., Wullaert, A., Gareus, R., Loo, G., Danese, S., Huth, M., Nikolaev, A., Neufert, C. F., Madison, B., et al. (2007) · Nature · doi:10.1038/nature05698 · Cited by 1,077 · see citing works
Self-citationIAP Antagonists Target cIAP1 to Induce TNFα-Dependent Apoptosis
Vince, J. E., Wong, W. W.-L., Khan, N. R., Feltham, R., Chau, D., Ahmed, A. U., Benetatos, C. A., Chunduru, S. K., Condon, S. M., McKinlay, M. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.037 · Cited by 1,061 · 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
Tissue‐specific and inducible Cre‐mediated recombination in the gut epithelium
Marjou, F. E., Janssen, K., Chang, B. H., Li, M., Hindie, V., Chan, L., Louvard, D., Chambon, P., METZGER, D., & Robine, S. (2004) · genesis · doi:10.1002/gene.20042 · Cited by 1,044 · see citing works
RIP1 is an essential mediator of Toll-like receptor 3–induced NF-κB activation
Meylan, E., Burns, K., Hofmann, K., Blancheteau, V., Martinon, F., Kelliher, M. A., & Tschopp, J. (2004) · Nature Immunology · doi:10.1038/ni1061 · Cited by 848 · see citing works
Self-citationMadison, B., Dunbar, L., Qiao, X. T., Braunstein, K., Braunstein, E. M., & Gumucio, D. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204935200 · Cited by 748 · see citing works
Paneth cells as a site of origin for intestinal inflammation
Adolph, T. E., Tomczak, M. F., Niederreiter, L., Ko, H.-J., Böck, J., Martinez-Naves, E., Glickman, J. N., Tschurtschenthaler, M., Hartwig, J., Hosomi, S., et al. (2013) · Nature · doi:10.1038/nature12599 · Cited by 732 · see citing works
A T-bet gradient controls the fate and function of CCR6−RORγt+ innate lymphoid cells
Klose, C. S. N., Kiss, E. A., Schwierzeck, V., Ebert, K., Hoyler, T., d’Hargues, Y., Göppert, N., Croxford, A. L., Waisman, A., Tanriver, Y., et al. (2013) · Nature · doi:10.1038/nature11813 · Cited by 722 · see citing works
FADD prevents RIP3-mediated epithelial cell necrosis and chronic intestinal inflammation
Welz, P.-S., Wullaert, A., Vlantis, K., Kondylis, V., Fernández-Majada, V., Ermolaeva, M., Kirsch, P., Sterner-Kock, A., van Loo, G., & Pasparakis, M. (2011) · Nature · doi:10.1038/nature10273 · Cited by 594 · see citing works
Self-citationRIP 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
Intestinal Bacteria and the Regulation of Immune Cell Homeostasis
Hill, D. A., & Artis, D. (2010) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101330 · Cited by 586 · see citing works
Virus Inhibition of RIP3-Dependent Necrosis
Upton, J. W., Kaiser, W. J., & Mocarski, E. S. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.03.006 · Cited by 559 · see citing works
Newton, K., Sun, X., & Dixit, V. M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.4.1464-1469.2004 · Cited by 544 · see citing works
Probiotic Escherichia coli Nissle 1917 inhibits leaky gut by enhancing mucosal integrity
Ukena, S. N., Singh, A., Dringenberg, U., Engelhardt, R., Seidler, U., Hansen, W., Bleich, A., Bruder, D., Franzke, A., Rogler, G., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0001308 · Cited by 482 · see citing works
Self-citationNEMO/IKKγ-Deficient Mice Model Incontinentia Pigmenti
Schmidt‐Supprian, M., Bloch, W., Courtois, G., Addicks, K., Israël, A., Rajewsky, K., & Pasparakis, M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80263-4 · Cited by 437 · see citing works
Self-citationFunctional complementation between FADD and RIP1 in embryos and lymphocytes
Zhang, H., Zhou, X., McQuade, T. J., Li, J., Chan, F. K.-M., & Zhang, J. (2011) · Nature · doi:10.1038/nature09878 · Cited by 422 · see citing works
Hermance, N. M., Khurana, S., Lee, T. H.-Y., Fitzgerald, K. A., & Kelliher, M. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506831200 · Cited by 345 · see citing works
Self-citationSurvival Function of the FADD-CASPASE-8-cFLIPL Complex
Dillon, C. P., Oberst, A., Weinlich, R., Janke, L. J., Kang, T.-B., Ben-Moshe, T., Mak, T. W., Wallach, D., & Green, D. R. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.03.010 · Cited by 331 · see citing works
Polykratis, A., Hermance, N. M., Zelic, M., Roderick, J. E., KIM, C. S., Van, T.-M., Lee, T. H., Chan, F. K.-M., Pasparakis, M., & Kelliher, M. A. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400590 · Cited by 328 · see citing works
Self-citationSasaki, Y., Derudder, E., Hobeika, E., Pelanda, R., Reth, M. G., Rajewsky, K., & Schmidt‐Supprian, M. (2006) · Immunity · doi:10.1016/j.immuni.2006.04.005 · Cited by 322 · see citing works
Bonnet, M. C., Preukschat, D., Welz, P.-S., van Loo, G., Ermolaeva, M. A., Bloch, W., Haase, I., & Pasparakis, M. (2011) · Immunity · doi:10.1016/j.immuni.2011.08.014 · Cited by 295 · see citing works
Self-citationLee, T. H.-Y., Shank, J., Cusson, N., & Kelliher, M. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404206200 · Cited by 255 · 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
Control of Life-or-Death Decisions by RIP1 Kinase
Christofferson, D. E., Li, Y., & Yuan, J. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021113-170259 · Cited by 200 · see citing works
Steinbrecher, K. A., Harmel-Laws, E., Sitcheran, R., & Baldwin, A. S. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.4.2588 · Cited by 174 · see citing works
Kumari, S., Bonnet, M., Ulvmar, M. H., Wolk, K., Karagianni, N., Witte, E., Uthoff‐Hachenberg, C., Renauld, J., Kollias, G. A., Toftgård, R., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.10.009 · Cited by 170 · see citing works
Self-citationKeratin 14 Cre transgenic mice authenticate keratin 14 as an oocyte‐expressed protein
Hafner, M., Wenk, J., Nenci, A., Pasparakis, M., Scharffetter‐Kochanek, K., Smyth, N. R., Peters, T., Keß, D., Holtkötter, O., Shephard, P., et al. (2004) · genesis · doi:10.1002/gene.20016 · Cited by 167 · see citing works
Self-citationImpaired epidermal wound healing in vivo upon inhibition or deletion of Rac1
Tscharntke, M., Pofahl, R., Chrostek‐Grashoff, A., Smyth, N. R., Niessen, C. M., Niemann, C., Hartwig, B., Herzog, V., Klein, H. W., Krieg, T. M., et al. (2007) · Journal of Cell Science · doi:10.1242/jcs.03426 · Cited by 110 · see citing works
Constitutive IKK2 activation in intestinal epithelial cells induces intestinal tumors in mice
Vlantis, K., Wullaert, A., Sasaki, Y., Schmidt‐Supprian, M., Rajewsky, K., Roskams, T., & Pasparakis, M. (2011) · Journal of Clinical Investigation · doi:10.1172/jci45349 · Cited by 100 · see citing works
Self-citationGentle, I. E., Wong, W. W.-L., Evans, J. M., Bankovacki, A., Cook, W. D., Khan, N. R., Nachbur, U., Rickard, J., Anderton, H., Moulin, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.216226 · Cited by 96 · see citing works
Oligodendrocyte-Specific FADD Deletion Protects Mice from Autoimmune-Mediated Demyelination
McGuire, C., Volckaert, T., Wolke, U., Sze, M., Rycke, R. D., Waisman, A., Prinz, M., Beyaert, R., Pasparakis, M., & van Loo, G. (2010) · Journal of Immunology · doi:10.4049/jimmunol.1000930 · Cited by 64 · see citing works
Self-citationTNFα-induced noncanonical NF-κB activation is attenuated by RIP1 through stabilization of TRAF2
Kim, J., Morgan, M., Kim, D., Lee, J., Bai, L., Lin, Y., Liu, Z.-G., & Kim, Y. (2011) · Journal of Cell Science · doi:10.1242/jcs.075770 · Cited by 58 · see citing works
Snippert, H. J. G., Schepers, A. G., Delconte, G., Siersema, P. D., & Clevers, H. C. (2011) · Nature Protocols · doi:10.1038/nprot.2011.365 · Cited by 47 · see citing works
Piao, J., Hasegawa, M., Heissig, B., Hattori, K., Takeda, K., Iwakura, Y., Okumura, K., Inohara, N., & Nakano, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.221853 · Cited by 36 · see citing works
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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
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D'Arcy, M. (2019) · Cell Biology International · doi:10.1002/cbin.11137 · Cited by 2,328 · see citing works
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Self-citationThe microbiome and innate immunity
Thaiss, C. A., Zmora, N., Levy, M., & Elinav, E. (2016) · Nature · doi:10.1038/nature18847 · Cited by 2,012 · see citing works
TNF biology, pathogenic mechanisms and emerging therapeutic strategies
Kalliolias, G. D., & Ivashkiv, L. B. (2015) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2015.169 · Cited by 1,390 · see citing works
Old, new and emerging functions of caspases
Shalini, S., Dorstyn, L., Dawar, S., & Kumar, S. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.216 · Cited by 1,267 · see citing works
Monocyte-derived alveolar macrophages drive lung fibrosis and persist in the lung over the life span
Misharin, A. V., Morales-Nebreda, L., Reyfman, P. A., Cuda, C. M., Walter, J. M., McQuattie-Pimentel, A. C., Chen, C.-I., Anekalla, K. R., Joshi, N., Williams, K. J. N., et al. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20162152 · Cited by 1,133 · see citing works
Caspase-8 is the molecular switch for apoptosis, necroptosis and pyroptosis
Fritsch, M., Günther, S. D., Schwarzer, R., Albert, M., Schorn, F., Werthenbach, J. P., Schiffmann, L. M., Stair, N., Stocks, H., Seeger, J. M., et al. (2019) · Nature · doi:10.1038/s41586-019-1770-6 · Cited by 1,122 · see citing works
Self-citationNecroptosis 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
Newton, K., Strasser, A., Kayagaki, N., & Dixit, V. M. (2024) · Cell · doi:10.1016/j.cell.2023.11.044 · Cited by 1,029 · see citing works
Necroptosis and RIPK1-mediated neuroinflammation in CNS diseases
Yuan, J., Amin, P., & Ofengeim, D. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-018-0093-1 · Cited by 967 · see citing works
Fundamental Mechanisms of Regulated Cell Death and Implications for Heart Disease
Re, D. P. D., Amgalan, D., Linkermann, A., Liu, Q., & Kitsis, R. N. (2019) · Physiological Reviews · doi:10.1152/physrev.00022.2018 · Cited by 979 · see citing works
Death by TNF: a road to inflammation
Loo, G., & Bertrand, M. J. M. (2022) · Nature reviews. Immunology · doi:10.1038/s41577-022-00792-3 · Cited by 977 · see citing works
Caspases in Cell Death, Inflammation, and Pyroptosis
Kesavardhana, S., Malireddi, R. K. S., & Kanneganti, T. (2020) · Annual Review of Immunology · doi:10.1146/annurev-immunol-073119-095439 · Cited by 927 · see citing works
Renal tubule injury: a driving force toward chronic kidney disease
Liu, B., Tang, T., Lv, L., & Lan, H.-Y. (2018) · Kidney International · doi:10.1016/j.kint.2017.09.033 · Cited by 922 · see citing works
Regulated cell death (RCD) in cancer: key pathways and targeted therapies
Peng, F., Liao, M., Qin, R., Zhu, S., Peng, C. Y., Fu, L., Chen, Y., & Han, B. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01110-y · Cited by 850 · see citing works
Caspase‐8: regulating life and death
Tummers, B., & Green, D. R. (2017) · Immunological Reviews · doi:10.1111/imr.12541 · Cited by 754 · see citing works
Necroptosis: Mechanisms and Relevance to Disease
Galluzzi, L., Kepp, O., Chan, F. K.-M., & Kroemer, G. (2016) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-052016-100247 · Cited by 721 · 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
Samir, P., Malireddi, R. K. S., & Kanneganti, T.-D. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00238 · Cited by 557 · see citing works
The diverse role of RIP kinases in necroptosis and inflammation
Silke, J., Rickard, J. A., & Gerlic, M. (2015) · Nature Immunology · doi:10.1038/ni.3206 · Cited by 522 · 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
Tsurusaki, S., Tsuchiya, Y., Koumura, T., Nakasone, M., Sakamoto, T., Matsuoka, M., Imai, H., Yuet-Yin Kok, C., Okochi, H., Nakano, H., et al. (2019) · Cell Death & Disease · doi:10.1038/s41419-019-1678-y · Cited by 529 · see citing works
Harris, P. A., Berger, S. B., Jeong, J. U., Nagilla, R., Bandyopadhyay, D., Campobasso, N., Capriotti, C. A., Cox, J. A., Dare, L. C., Dong, X., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01751 · Cited by 502 · see citing works
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Dostert, C., Grusdat, M., Letellier, E., & Brenner, D. (2018) · Physiological Reviews · doi:10.1152/physrev.00045.2017 · Cited by 502 · see citing works
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Mifflin, L., Ofengeim, D., & Yuan, J. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0071-y · Cited by 493 · see citing works
Z-nucleic-acid sensing triggers ZBP1-dependent necroptosis and inflammation
Jiao, H., Wachsmuth, L., Kumari, S., Schwarzer, R., Lin, J., Eren, R. O., Fisher, A. D., Lane, R. K., Young, G. R., Kassiotis, G., et al. (2020) · Nature · doi:10.1038/s41586-020-2129-8 · Cited by 493 · see citing works
Self-citationNewton, K., Dugger, D. L., Maltzman, A., Greve, J. M., Hedehus, M., Martin-McNulty, B., Carano, R. A. D., Cao, T. C., van Bruggen, N., Bernstein, L., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.46 · Cited by 442 · see citing works
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Lin, J., Kumari, S., Kim, C., Van, T.-M., Wachsmuth, L., Polykratis, A., & Pasparakis, M. (2016) · Nature · doi:10.1038/nature20558 · Cited by 421 · see citing works
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Patankar, J. V., & Becker, C. (2020) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-020-0326-4 · Cited by 421 · see citing works
Newton, K., & Manning, G. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014830 · Cited by 401 · see citing works
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A Review on Caspases: Key Regulators of Biological Activities and Apoptosis
Sahoo, G., Samal, D., Khandayataray, P., & Murthy, M. K. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03433-5 · Cited by 406 · see citing works
Immunogenic cell death in cancer: targeting necroptosis to induce antitumour immunity
Meier, P., Legrand, A. J., Adam, D., & Silke, J. (2024) · Nature reviews. Cancer · doi:10.1038/s41568-024-00674-x · Cited by 405 · see citing works
RIPK1 and RIPK3: critical regulators of inflammation and cell death
Newton, K. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.01.001 · Cited by 367 · see citing works
Programmed Necrosis in the Cross Talk of Cell Death and Inflammation
Chan, F. K.-M., Luz, N. F., & Moriwaki, K. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112248 · Cited by 350 · see citing works
Cell Death in the Lung: The Apoptosis–Necroptosis Axis
Sauler, M., Bazan, I. S., & Lee, P. J. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114320 · Cited by 325 · see citing works
The Autophagy Machinery Controls Cell Death Switching between Apoptosis and Necroptosis
Goodall, M. L., Fitzwalter, B. E., Zahedi, S., Wu, M., Rodriguez, D., Mulcahy-Levy, J. M., Green, D. R., Morgan, M., Cramer, S. D., & Thorburn, A. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.04.018 · Cited by 314 · see citing works
Programmed Cell Death Tunes Tumor Immunity
Liu, J., Hong, M., Li, Y., Chen, D., Wu, Y., & Hu, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.847345 · Cited by 320 · see citing works
RIPK1 ensures intestinal homeostasis by protecting the epithelium against apoptosis
Takahashi, N., Vereecke, L., Bertrand, M. J. M., Duprez, L., Berger, S. B., Divert, T., Gonçalves, A., Sze, M., Gilbert, B., Kourula, S., et al. (2014) · Nature · doi:10.1038/nature13706 · Cited by 318 · see citing works
Regulation of alveolar macrophage death in acute lung inflammation
Fan, E., & Fan, J. (2018) · Respiratory Research · doi:10.1186/s12931-018-0756-5 · Cited by 315 · see citing works
ZBP1: Innate Sensor Regulating Cell Death and Inflammation
Kuriakose, T., & Kanneganti, T. (2017) · Trends in Immunology · doi:10.1016/j.it.2017.11.002 · Cited by 300 · see citing works
Checkpoints in TNF-Induced Cell Death: Implications in Inflammation and Cancer
Annibaldi, A., & Meier, P. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.11.002 · Cited by 287 · see citing works
RIPK1 and RIPK3 Kinases Promote Cell-Death-Independent Inflammation by Toll-like Receptor 4
Najjar, M., Saleh, D., Zelic, M., Nogusa, S., Shah, S., Tai, A., Finger, J. N., Polykratis, A., Gough, P. J., Bertin, J., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.06.007 · Cited by 285 · see citing works
Self-citationDying cells fan the flames of inflammation
Newton, K., Dixit, V. M., & Kayagaki, N. (2021) · Science · doi:10.1126/science.abi5934 · Cited by 278 · see citing works
Schwarzer, R., Jiao, H., Wachsmuth, L., Tresch, A., & Pasparakis, M. (2020) · Immunity · doi:10.1016/j.immuni.2020.04.002 · Cited by 277 · see citing works
Self-citationFerroptosis and Necroptosis in the Kidney
Belavgeni, A., Meyer, C., Stumpf, J., Hugo, C., & Linkermann, A. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.03.016 · Cited by 279 · see citing works
He, J., Liu, D., Zhao, L., Zhou, D., Rong, J., Zhang, L., & Xia, Z. (2022) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2022.11357 · Cited by 277 · see citing works
TNFR1-dependent cell death drives inflammation in Sharpin-deficient mice
Rickard, J. A., Anderton, H., Etemadi, N., Nachbur, U., Darding, M., Peltzer, N., Lalaoui, N., Lawlor, K. E., Vanyai, H. K., Hall, C. M., et al. (2014) · eLife · doi:10.7554/elife.03464 · Cited by 261 · see citing works
Oxidative stress-mediated HMGB1 biology
Yan, Y. Q., Tang, D., & Kang, R. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00093 · Cited by 262 · see citing works
More to Life than NF-κB in TNFR1 Signaling
Ting, A. T., & Bertrand, M. J. M. (2016) · Trends in Immunology · doi:10.1016/j.it.2016.06.002 · Cited by 254 · see citing works
Glutathione peroxidase 4 prevents necroptosis in mouse erythroid precursors
Canli, Ö., Alankuş, Y. B., Grootjans, S., Vegi, N., Hültner, L., Hoppe, P. S., Schroeder, T., Vandenabeele, P., Bornkamm, G. W., & Greten, F. R. (2016) · Blood · doi:10.1182/blood-2015-06-654194 · Cited by 247 · see citing works
RIP kinases as modulators of inflammation and immunity
He, S., & Wang, X. (2018) · Nature Immunology · doi:10.1038/s41590-018-0188-x · Cited by 246 · see citing works
Cuchet, D., Eletto, D., Wu, C., Plagnol, V., Papapietro, O., Curtis, J. W., Ceron‐Gutierrez, L., Bacon, C. M., Hackett, S. J., Alsaleem, B., et al. (2018) · Science · doi:10.1126/science.aar2641 · Cited by 244 · see citing works
Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation
Laurien, L., Nagata, M., Schünke, H., Delanghe, T., Wiederstein, J. L., Kumari, S., Schwarzer, R., Corona, T., Krüger, M., Bertrand, M. J. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15466-8 · Cited by 240 · see citing works
Self-citationMenon, M. B., Gropengießer, J., Fischer, J., Novikova, L., Deuretzbacher, A., Lafera, J., Schimmeck, H., Czymmeck, N., Ronkina, N., Kotlyarov, A., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3614 · Cited by 238 · see citing works
Necroinflammation in Kidney Disease
Mulay, S. R., Linkermann, A., & Anders, H. (2015) · Journal of the American Society of Nephrology · doi:10.1681/asn.2015040405 · Cited by 231 · see citing works
Kondylis, V., Kumari, S., Vlantis, K., & Pasparakis, M. (2017) · Immunological Reviews · doi:10.1111/imr.12550 · Cited by 226 · see citing works
Self-citationNajafov, A., Chen, H., & Yuan, J. (2017) · Trends in cancer · doi:10.1016/j.trecan.2017.03.002 · Cited by 225 · see citing works
RIPK1 Distinctly Regulates <i>Yersinia</i>-Induced Inflammatory Cell Death, PANoptosis
Malireddi, R. K. S., Kesavardhana, S., Karki, R., Kancharana, B., Burton, A. R., & Kanneganti, T.-D. (2020) · ImmunoHorizons · doi:10.4049/immunohorizons.2000097 · Cited by 224 · see citing works
Karunakaran, D., Nguyen, M.-A., Geoffrion, M., Vreeken, D., Lister, Z., Cheng, H. S., Otte, N., Essebier, P., Wyatt, H., Kandiah, J. W., et al. (2020) · Circulation · doi:10.1161/circulationaha.118.038379 · Cited by 219 · see citing works
Molecular crosstalk between apoptosis, necroptosis, and survival signaling
Berghe, T. V., Kaiser, W. J., Bertrand, M. J. M., & Vandenabeele, P. (2015) · Molecular & Cellular Oncology · doi:10.4161/23723556.2014.975093 · Cited by 203 · see citing works
Gut epithelial TSC1/mTOR controls RIPK3-dependent necroptosis in intestinal inflammation and cancer
Xie, Y., Zhao, Y., Shi, L., Li, W., Chen, K., Li, M., Chen, X., Zhang, H., Li, T., Matsuzawa, Y., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci133264 · Cited by 198 · 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
Self-citationHuman RIPK1 deficiency causes combined immunodeficiency and inflammatory bowel diseases
Li, Y., Führer, M., Bahrami, E., Socha, P., Klaudel‐Dreszler, M., Bouzidi, A., Liu, Y., Lehle, A. S., Magg, T., Hollizeck, S., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1813582116 · Cited by 196 · see citing works
ZBP1 mediates interferon-induced necroptosis
Yang, D., Liang, Y., Zhao, S., Ding, Y. P., Zhuang, Q., Shi, Q., Ai, T., Wu, S., & Han, J. (2019) · Cellular and Molecular Immunology · doi:10.1038/s41423-019-0237-x · Cited by 195 · see citing works
Woznicki, J. A., Saini, N., Flood, P. F., Rajaram, S., Lee, C. M., Stamou, P., Skowyra, A., Bustamante-Garrido, M., Regazzoni, K., Crawford, N., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04151-3 · Cited by 191 · see citing works
Complex Pathologic Roles of RIPK1 and RIPK3: Moving Beyond Necroptosis
Wegner, K. W., Saleh, D., & Degterev, A. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.12.005 · Cited by 190 · see citing works
Roles of RIPK3 in necroptosis, cell signaling, and disease
Morgan, M. J., & Kim, Y. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00868-z · Cited by 189 · see citing works
CHIP controls necroptosis through ubiquitylation- and lysosome-dependent degradation of RIPK3
Seo, J., Lee, E.-W., Sung, H., Seong, D., Dondelinger, Y., Shin, J., Jeong, M., Lee, H.-K., Kim, J.-H., Han, S. Y., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3314 · Cited by 182 · see citing works
Holding RIPK1 on the Ubiquitin Leash in TNFR1 Signaling
Peltzer, N., Darding, M., & Walczak, H. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.01.006 · Cited by 184 · see citing works
Inhibitors Targeting RIPK1/RIPK3: Old and New Drugs
Martens, S., Hofmans, S., Declercq, W., Augustyns, K., & Vandenabeele, P. (2020) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.01.002 · Cited by 185 · see citing works
Necroptosis: an alternative cell death program defending against cancer
Chen, D., Yu, J., & Zhang, L. (2016) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2016.03.003 · Cited by 182 · see citing works
Necroptosis Promotes Staphylococcus aureus Clearance by Inhibiting Excessive Inflammatory Signaling
Kitur, K., Wachtel, S., Brown, A. O., Wickersham, M., Paulino, F. E., Peñaloza, H. F., Soong, G., Bueno, S. M., Parker, D., & Prince, A. S. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.039 · Cited by 180 · see citing works
ATG16L1 orchestrates interleukin-22 signaling in the intestinal epithelium via cGAS–STING
Aden, K., Tran, F., Ito, G., Sheibani-Tezerji, R., Lipinski, S., Kuiper, J. W., Tschurtschenthaler, M., Saveljeva, S., Bhattacharyya, J., Häsler, R., et al. (2018) · Journal of Experimental Medicine · doi:10.1084/jem.20171029 · Cited by 167 · see citing works
Self-citationDara, L., Johnson, H. S., Suda, J., Win, S., Gaarde, W. A., Han, D., & Kaplowitz, N. (2015) · Hepatology · doi:10.1002/hep.27939 · Cited by 177 · see citing works
Liu, T., Kern, J. T., Jain, U., Sonnek, N. M., Xiong, S., Simpson, K. F., VanDussen, K. L., Winkler, E. S., Haritunians, T., Malique, A., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.04.004 · Cited by 173 · see citing works
Emerging insights into human health and NK cell biology from the study of NK cell deficiencies
Mace, E. M., & Orange, J. S. (2018) · Immunological Reviews · doi:10.1111/imr.12725 · Cited by 171 · see citing works
RIPK1 Suppresses a TRAF2-Dependent Pathway to Liver Cancer
Schneider, A. T., Gautheron, J., Feoktistova, M., Roderburg, C., Loosen, S. H., Roy, S., Benz, F., Schemmer, P., Büchler, M. W., Nachbur, U., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2016.11.009 · Cited by 155 · see citing works
Apoptosis, Necrosis, and Necroptosis in the Gut and IntestinalHomeostasis
Negroni, A., Cucchiara, S., & Stronati, L. (2015) · Mediators of Inflammation · doi:10.1155/2015/250762 · Cited by 163 · see citing works
Schwarzer, R., Laurien, L., & Pasparakis, M. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.02.004 · Cited by 161 · see citing works
Self-citationThe pathological features of regulated necrosis
Tonnus, W., Meyer, C., Paliege, A., Belavgeni, A., von Mäßenhausen, A., Bornstein, S. R., Hugo, C., Becker, J. U., & Linkermann, A. (2019) · The Journal of Pathology · doi:10.1002/path.5248 · Cited by 160 · see citing works
Structure Guided Design of Potent and Selective Ponatinib-Based Hybrid Inhibitors for RIPK1
Najjar, M., Suebsuwong, C., Ray, S. S., Thapa, R. J., Maki, J. L., Nogusa, S., Shah, S., Saleh, D., Gough, P. J., Bertin, J., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.02.052 · Cited by 153 · see citing works
Intrinsic Defense Mechanisms of the Intestinal Epithelium
Ramanan, D., & Cadwell, K. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.03.003 · Cited by 153 · see citing works
Programmed necrosis and necroptosis signalling
Feoktistova, M., & Leverkus, M. (2014) · FEBS Journal · doi:10.1111/febs.13120 · Cited by 153 · see citing works
Characterization of GSK′963: a structurally distinct, potent and selective inhibitor of RIP1 kinase
Berger, S., Harris, P. A., Nagilla, R., Kasparcova, V., Hoffman, S., Swift, B., Dare, L. C., Schaeffer, M. C., Capriotti, C. A., Ouellette, M. T., et al. (2015) · Cell Death Discovery · doi:10.1038/cddiscovery.2015.9 · Cited by 151 · see citing works
TWEAK and RIPK1 mediate a second wave of cell death during AKI
Martín‐Sánchez, D., Fontecha‐Barriuso, M., Carrasco, S., Sánchez-Niño, M. D., von Mäßenhausen, A., Linkermann, A., Cannata‐Ortiz, P., Ruiz‐Ortega, M., Egido, J., Ortíz, A., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716578115 · Cited by 149 · see citing works
Gut mucosal DAMPs in IBD: from mechanisms to therapeutic implications
Boyapati, R. K., Rossi, A. G., Satsangi, J., & Ho, G. (2016) · Mucosal Immunology · doi:10.1038/mi.2016.14 · Cited by 148 · see citing works
Cell death in chronic inflammation: breaking the cycle to treat rheumatic disease
Anderton, H., Wicks, I. P., & Silke, J. (2020) · Nature Reviews Rheumatology · doi:10.1038/s41584-020-0455-8 · Cited by 145 · see citing works
Linear ubiquitination in immunity
Shimizu, Y., Taraborrelli, L., & Walczak, H. (2015) · Immunological Reviews · doi:10.1111/imr.12309 · Cited by 135 · see citing works
Role of necroptosis in the pathogenesis of solid organ injury
Zhao, H., Jaffer, T., Eguchi, S., Wang, Z., Linkermann, A., & Ma, D. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.316 · Cited by 141 · see citing works
A20 and cell death-driven inflammation
Priem, D., van Loo, G., & Bertrand, M. J. M. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.03.001 · Cited by 139 · see citing works
Mechanisms of Pediatric Inflammatory Bowel Disease
Peloquin, J. M., Goel, G., Villablanca, E. J., & Xavier, R. J. (2016) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112151 · Cited by 138 · see citing works
Kondylis, V., Polykratis, A., Ehlken, H., Ochoa-Callejero, L., Straub, B. K., Krishna-Subramanian, S., Van, T.-M., Curth, H.-M., Heise, N., Weih, F., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.10.001 · Cited by 131 · see citing works
Self-citationThe intestinal epithelium as guardian of gut barrier integrity
Zhang, K., Hornef, M. W., & Dupont, A. (2015) · Cellular Microbiology · doi:10.1111/cmi.12501 · Cited by 138 · see citing works
The Two Faces of Receptor Interacting Protein Kinase-1
Weinlich, R., & Green, D. R. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.11.001 · Cited by 127 · see citing works
The MLKL Channel in Necroptosis Is an Octamer Formed by Tetramers in a Dyadic Process
Huang, D., Zheng, X., Wang, Z.-A., Chen, X., He, W., Zhang, Y., Xu, J.-G., Zhao, H., Shi, W., Wang, X., et al. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00497-16 · Cited by 132 · see citing works
An outline of necrosome triggers
Berghe, T. V., Hassannia, B., & Vandenabeele, P. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2189-y · Cited by 130 · see citing works
Damaging heterozygous mutations in NFKB1 lead to diverse immunologic phenotypes
Kaustio, M., Haapaniemi, E. M., Göös, H., Hautala, T., Park, G., Syrjänen, J., Einarsdóttir, E., Sahu, B., Kilpinen, S., Rounioja, S., et al. (2017) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2016.10.054 · Cited by 133 · see citing works
Interferons and the immunogenic effects of cancer therapy
Minn, A. J. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.09.007 · Cited by 130 · see citing works
- Authors
- Dannappel, M., Vlantis, K., Kumari, S., Polykratis, A., Kim, C., Wachsmuth, L., Eftychi, C., Lin, J., Corona, T., Hermance, N., Zelic, M., Kirsch, P., Basic, M., Bleich, A., Kelliher, M., & Pasparakis, M.
- Affiliations
- University of Cologne (DE)
- University of Massachusetts Chan Medical School (US)
- Universität Ulm (DE)
- Medizinische Hochschule Hannover (DE)
- Corresponding author
- Pasparakis, Manolis
- ORCID
- Venue
- Nature
- Published
- 2014-08-17
- Volume
- 513
- Issue
- 7516
- Pages
- 90-94
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC4206266
- OpenAlex
- W1985231277
- Cited by
- 534
- References
- 47
- Citations by year
- 2026: 21 · 2025: 33 · 2024: 46 · 2023: 36 · 2022: 56 · 2021: 47 · 2020: 47 · 2019: 49 · 2018: 44 · 2017: 33 · 2016: 59 · 2015: 49 · 2014: 14
- FWCI
- 21.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Kölner Universitäts PublikationsServer (Universität zu Köln) (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI075118, T32AI095213)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- RIPK1, necroptosis, apoptosis, epithelial homeostasis, FADD, caspase-8, RIPK3, intestinal epithelium, skin inflammation, keratinocytes, TNFR1, barrier tissues, inflammation, programmed cell death, Paneth cells, goblet cells, villous atrophy, intestinal inflammation
- MeSH terms
- Animals, Cell Survival, Epithelial Cells, Female, Homeostasis, Inflammation, Intestinal Mucosa, Intestines, Male, Necrosis, Skin, Keratinocytes, Apoptosis, Mice, Knockout, Paneth Cells, Receptors, Tumor Necrosis Factor, Type I, Mice, Caspase 8, Fas-Associated Death Domain Protein, Receptor-Interacting Protein Serine-Threonine Kinases, Myeloid Differentiation Factor 88
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