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RIP3 mediates the embryonic lethality of caspase-8-deficient mice
Open accessAbstract
Apoptosis and necroptosis are complementary pathways controlled by common signalling adaptors, kinases and proteases; among these, caspase-8 (Casp8) is critical for death receptor-induced apoptosis. This caspase has also been implicated in non-apoptotic pathways that regulate Fas-associated via death domain (FADD)-dependent signalling and other less defined biological processes as diverse as innate immune signalling and myeloid or lymphoid differentiation patterns. Casp8 suppresses RIP3-RIP1 (also known as RIPK3-RIPK1) kinase complex-dependent necroptosis that follows death receptor activation as well as a RIP3-dependent, RIP1-independent necrotic pathway that has emerged as a host defence mechanism against murine cytomegalovirus. Disruption of Casp8 expression leads to embryonic lethality in mice between embryonic days 10.5 and 11.5 (ref. 7). Thus, Casp8 may naturally hold alternative RIP3-dependent death pathways in check in addition to promoting apoptosis. We find that RIP3 is responsible for the mid-gestational death of Casp8-deficient embryos. Remarkably, Casp8(-/-)Rip3(-/-) double mutant mice are viable and mature into fertile adults with a full immune complement of myeloid and lymphoid cell types. These mice seem immunocompetent but develop lymphadenopathy by four months of age marked by accumulation of abnormal T cells in the periphery, a phenotype reminiscent of mice with Fas-deficiency (lpr/lpr; also known as Fas). Thus, Casp8 contributes to homeostatic control in the adult immune system; however, RIP3 and Casp8 are together completely dispensable for mammalian development.
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“In addition, the assembly of the necrosome upon TNFR1 stimulation impinges on two conditions: (1) pharmacological or genetic CASP8 inactivation [478, 479], and (2) RIPK1 deubiquitination-dependent phosphorylation (at least in some settings), which can be favored by exogenously provided SMAC mimetics, ensuring the release of RIPK1 from complex I (see above) [334, 335, 480, 481].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [478]
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Cites
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216
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
Receptor 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
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 1,987
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
Restoration of p53 function leads to tumour regression in vivo
Ventura, A., Kirsch, D. G., McLaughlin, M. E., Tuveson, D. A., Grimm, J., Lintault, L., Newman, J., Reczek, E. E., Weissleder, R., & Jacks, T. (2007) · Nature · doi:10.1038/nature05541 · Cited by 1,820
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
Regulation of an ATG7 - beclin 1 Program of Autophagic Cell Death by Caspase-8
Yu, L., Alva, A. S., Su, H. C., Dutt, P., Freundt, E. C., Welsh, S. J., Baehrecke, E. H., & Lenardo, M. J. (2004) · Science · doi:10.1126/science.1096645 · Cited by 1,249
Identification of Lps2 as a key transducer of MyD88-independent TIR signalling
Hoebe, K. H. N., Du, X., Georgel, P., Janssen, E. M., Tabeta, K., Kim, S. O., Goode, J., Lin, P., Mann, N., Mudd, S., et al. (2003) · Nature · doi:10.1038/nature01889 · Cited by 1,232
The many roles of FAS receptor signaling in the immune system
Strasser, A., Jost, P. J., & Nagata, S. (2009) · Immunity · doi:10.1016/j.immuni.2009.01.001 · Cited by 968
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Duprez, L., Bertrand, M. J. M., Berghe, T. V., Dondelinger, Y., Festjens, N., & Vandenabeele, P. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.288670 · Cited by 46
Greve, A., Skals, M., Fagerberg, S. K., Tonnus, W., Ellermann‐Eriksen, S., Evans, R. J., Linkermann, A., & Prætorius, H. A. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00113 · Cited by 46
The web of death: the expanding complexity of necroptotic signaling
Horne, C. R., Samson, A. L., & Murphy, J. M. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.05.008 · Cited by 47
Innate and adaptive immune abnormalities underlying autoimmune diseases: the genetic connections
Chi, X., Huang, M., Tu, H., Zhang, B., Lin, X., Xu, H., Dong, C., & Hu, X. (2023) · Science China Life Sciences · doi:10.1007/s11427-021-2187-3 · Cited by 47
Iron promotes both ferroptosis and necroptosis in the early stage of reperfusion in ischemic stroke
Du, B., Deng, Z., Chen, K., Yang, Z., Wei, J., Zhou, L., Meng, J., Cheng, Y., Tian, X., Tuo, Q., et al. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101262 · Cited by 46
ARC is a novel therapeutic approach against acetaminophen-induced hepatocellular necrosis
An, J., Mehrhof, F. B., Harms, C., Lättig-Tünnemann, G., Lee, S. L. L., Endres, M., Li, M., Sellge, G., Mandić, A. D., Trautwein, C., et al. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.10.002 · Cited by 45
Viral RNA at Two Stages of Reovirus Infection Is Required for the Induction of Necroptosis
Berger, A. K., Hiller, B. E., Thete, D., Snyder, A. J., Perez, E., Upton, J. W., & Danthi, P. (2017) · Journal of Virology · doi:10.1128/jvi.02404-16 · Cited by 47
Self-citationSilke, J., & Vince, J. E. (2016) · Current topics in microbiology and immunology · doi:10.1007/82_2016_507 · Cited by 46
Targeting MicroRNA Function in Acute Pancreatitis
Xiang, H., Tao, X., Xia, S., Qu, J., Song, H., Liu, J., & Shang, D. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00726 · Cited by 45
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Lafont, É., Hartwig, T., & Walczak, H. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.11.002 · Cited by 45
Weir, A. L., & Vince, J. E. (2022) · Biochemical Journal · doi:10.1042/bcj20210711 · Cited by 45
Caspase mechanisms in the regulation of inflammation
Bibo‐Verdugo, B., & Salvesen, G. S. (2022) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2022.101085 · Cited by 46
Role of caspase-8 in thymus function
Pozzesi, N., Fierabracci, A., Liberati, A. M., Martelli, M. P., Ayroldi, E., Riccardi, C., & Delfino, D. V. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.166 · Cited by 45
CNOT3 suppression promotes necroptosis by stabilizing mRNAs for cell death-inducing proteins
Suzuki, T., Kikuguchi, C., Sharma, S., Sasaki, T., Tokumasu, M., Adachi, S., Natsume, T., Kanegae, Y., & Yamamoto, T. S. (2015) · Scientific Reports · doi:10.1038/srep14779 · Cited by 45
Endoplasmic reticulum stress-mediated cell death in cardiovascular disease
An, Y., Wang, X., Guan, X., Yuan, P., Liu, Y., Wei, L., Wang, F., & Qi, X. (2024) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2023.12.003 · Cited by 46
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Matsuzawa, Y., Oshima, S., Nibe, Y., Kobayashi, M., Maeyashiki, C., Nemoto, Y., Nagaishi, T., Okamoto, R., Tsuchiya, K., Nakamura, T., et al. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.11.075 · Cited by 44
Yang, X., Lin, Z., Zhao, N., Zhou, L., Liu, F., Cichacz, Z. A., Zhang, L., Zhan, Q., & Zhao, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100127 · Cited by 43
Ebermann, L., Ruzsics, Z., Guzmán, C. A., van Rooijen, N., Casalegno‐Garduño, R., Koszinowski, U. H., & Čičin‐Šain, L. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1003062 · Cited by 43
Cylindromatosis mediates neuronal cell death in vitro and in vivo
Ganjam, G. K., Terpolilli, N. A., Diemert, S., Eisenbach, I., Hoffmann, L., Reuther, C., Herden, C., Roth, J., Plesnila, N., & Culmsee, C. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-017-0046-7 · Cited by 46
Palmer, S. N., Chappidi, S., Pinkham, C., & Hancks, D. C. (2021) · Molecular Biology and Evolution · doi:10.1093/molbev/msab256 · Cited by 43
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Hoste, E., Denecker, G., Gilbert, B., Nieuwerburgh, F. V., van der Fits, L., Asselbergh, B., Rycke, R. M. D., Hachem, J. P., Deforce, D. L. D., Prens, E. P., et al. (2012) · Journal of Investigative Dermatology · doi:10.1038/jid.2012.350 · Cited by 45
Koenig, A., Buskiewicz, I. A., Fortner, K. A., Russell, J. Q., Asaoka, T., He, Y.-W., Hakem, R., Eriksson, J. E., & Budd, R. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.506428 · Cited by 42
Self-citationRIP1 kinase activity-dependent roles in embryonic development of Fadd-deficient mice
Liu, Y., Fan, C., Zhang, Y., Yu, X., Wu, X., Zhang, X., Zhao, Q., Zhang, H., Xie, Q., Li, M., et al. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.78 · Cited by 42
Wang, Y., Karki, R., Zheng, M., Kancharana, B., Lee, S., Kesavardhana, S., Hansen, B. S., Pruett‐Miller, S. M., & Kanneganti, T. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2100757 · Cited by 42
Kikuchi, M., Kuroki, S., Kayama, M., Sakaguchi, S., Lee, K.-K., & Yonehara, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.419747 · Cited by 42
Mechanisms of RIPK3‐induced inflammation
Shlomovitz, I., Zargrian, S., & Gerlic, M. (2016) · Immunology and Cell Biology · doi:10.1038/icb.2016.124 · Cited by 43
Tonnus, W., Gembardt, F., Latk, M., Parmentier, S. P., Hugo, C., Bornstein, S. R., & Linkermann, A. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0193-5 · Cited by 44
Preyat, N., Rossi, M., Kers, J., Chen, L., Bertin, J., Gough, P. J., Moine, A. L., Rongvaux, A., Gool, F. V., & Léo, O. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.60 · Cited by 42
Coupienne, I., Fettweis, G., & Piette, J. (2011) · Lasers in Surgery and Medicine · doi:10.1002/lsm.21088 · Cited by 41
Kumar, S., Budhathoki, S., Oliveira, C. B., Kahle, A. D., Calhan, O. Y., Lukens, J. R., & Deppmann, C. D. (2023) · JCI Insight · doi:10.1172/jci.insight.157433 · Cited by 41
Zhao, W., Fan, C.-L., Hu, X., Ban, X.-X., Wan, H., He, Y., Zhāng, Q., & Xiong, K. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01373-1 · Cited by 44
Park, E., Kim, Y., Noh, H., Lee, H., Yoo, S., & Park, S. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.121 · Cited by 41
Xu, Q., Jitkaew, S., Choksi, S., Kadigamuwa, C., Qu, J., Choe, M., Jang, J., Liu, C., & Liu, Z.-G. (2017) · Nature Communications · doi:10.1038/s41467-017-00496-6 · Cited by 42
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Hoste, E., Lecomte, K., Annusver, K., Vandamme, N., Roels, J., Maschalidi, S., Verboom, L., Vikkula, H., Sze, M., Hove, L. V., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25944-2 · Cited by 41
Kupka, S., Reichert, M., Dráber, P., & Walczak, H. (2016) · FEBS Journal · doi:10.1111/febs.13644 · Cited by 41
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Solon, M., Ge, N., Hambro, S., Haller, S., Jiang, J. W., Baca, M., Preston, J., Maltzman, A., Wickliffe, K. E., Liang, Y., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01286-6 · Cited by 41
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Venero, J. L., Burguillos, M. Á., & Joseph, B. (2013) · Developmental Neuroscience · doi:10.1159/000346155 · Cited by 42
Wang, Y., Karki, R., Mall, R., Sharma, B. R., Kalathur, R., Lee, S., Kancharana, B., So, M., Combs, K. L., & Kanneganti, T. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111434 · Cited by 40
Liu, X., Miao, M., Sun, J., Wu, J., & Qin, X. (2023) · APOPTOSIS · doi:10.1007/s10495-023-01904-7 · Cited by 40
Kang, T., Jeong, J.-S., Yang, S., Kovalenko, A., & Wallach, D. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0104-9 · Cited by 39
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Xiao, Y., Li, H., Zhang, J., Volk, A. G., Zhang, S., Wei, W., Zhang, S., Breslin, P., & Zhang, J. (2011) · Blood · doi:10.1182/blood-2011-06-359448 · Cited by 39
Qi, X., Gurung, P., Malireddi, R. K. S., Karmaus, P. W. F., Sharma, D., Vogel, P., Chi, H., Green, D. R., & Kanneganti, T. (2016) · Mucosal Immunology · doi:10.1038/mi.2016.25 · Cited by 40
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Gan, I., Jiang, J., Lian, D., Huang, X., Fuhrmann, B., Liu, W., Haig, A. R., Jevnikar, A. M., & Zhang, Z. (2018) · American Journal of Transplantation · doi:10.1111/ajt.15112 · Cited by 38
Brentnall, M., Weir, D. B., Rongvaux, A., Marcus, A. I., & Boise, L. (2014) · Journal of Cell Science · doi:10.1242/jcs.135137 · Cited by 38
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Dong, X., Liu, H., Zhang, M., Zhao, P., Liu, S., Yan, H., & Wang, Y. (2019) · Europe PMC (PubMed Central) · Cited by 37
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Fan, Q., Huang, Z. M., Boucher, M., Shang, X., Zuo, L., Brinks, H., Lau, W. B., Zhang, J., Chuprun, J. K., & Gao, E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073537 · Cited by 37
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Chan, F. K.-M. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008805 · Cited by 37
Liccardi, G., & Annibaldi, A. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01061-5 · Cited by 37
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Liao, Y., Yang, Y., Wang, X., Wei, M., Guo, Q., & Zhao, L. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.112917 · Cited by 36
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Xia, Y., Wang, Y., Chen, K., Zhang, M., Jiang, Q., & Xu, T. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.156551 · Cited by 35
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Freimuth, J., Bangen, J., Lambertz, D., Hu, W., Nevzorova, Y. A., Sonntag, R., Gaßler, N., Riethmacher, D., Trautwein, C., & Liedtke, C. (2013) · Hepatology · doi:10.1002/hep.26538 · Cited by 34
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Lee, S., Lee, E., Kang, D. H., Lee, J., Hong, S. H., Jeong, W., & Kang, S. W. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00642-7 · Cited by 34
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Self-citationLi, D., Ai, Y., Guo, J., Dong, B., Lin, L., Cai, G., Chen, S., Xu, D., Wang, F., & Wang, X. (2020) · eLife · doi:10.7554/elife.61564 · Cited by 33
Yang, Y., Wang, L., Zhang, H., & Luo, L. (2021) · Journal of Molecular Medicine · doi:10.1007/s00109-021-02126-7 · Cited by 33
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Ke, J., Zhao, F., Luo, Y., Deng, F., & Wu, X. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.58163 · Cited by 32
Eltom, S. M., Belvisi, M. G., Yew‐Booth, L., Dekkak, B., Maher, S. A., Dubuis, E. D., Jones, V. M., Fitzgerald, K. A., & Birrell, M. A. (2014) · Respiratory Research · doi:10.1186/s12931-014-0087-0 · Cited by 34
Croker, B. A., Silke, J., & Gerlic, M. (2015) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000148 · Cited by 33
Nikseresht, S., Khodagholi, F., Nategh, M., & Dargahi, L. (2015) · Journal of Molecular Neuroscience · doi:10.1007/s12031-015-0609-3 · Cited by 32
Sharma, D., Sharma, B. R., Vogel, P., & Kanneganti, T. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.10.015 · Cited by 31
Stolzer, I., Kaden-Volynets, V., Ruder, B., Letizia, M., Bittel, M., Rausch, P., Basic, M., Bleich, A., Baines, J. F., Neurath, M. F., et al. (2019) · Inflammatory Bowel Diseases · doi:10.1093/ibd/izz142 · Cited by 31
A Two-Cell Model for IL-1β Release Mediated by Death-Receptor Signaling
Donado, C. A., Cao, A., Simmons, D. P., Croker, B. A., Brennan, P. J., & Brenner, M. B. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.03.030 · Cited by 31
Ghazavi, F., Huysentruyt, J., Coninck, J. D., Kourula, S., Martens, S., Hassannia, B., Wartewig, T., Divert, T., Roelandt, R., Popper, B., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024508119 · Cited by 31
Huang, D., Chen, P., Huang, G., Sun, H., Luo, X., Chen, F., Chen, F., Wang, Y., Zeng, C., Su, L., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04633-y · Cited by 31
Caspase-8 inactivation drives autophagy-dependent inflammasome activation in myeloid cells
Wu, Y., Mo, S.-T., Chen, I., Hsieh, F., Hsieh, S.-L. E., Zhang, J., & Lai, M. (2022) · Science Advances · doi:10.1126/sciadv.abn9912 · Cited by 32
NFκB and ubiquitination: partners in disarming RIPK1-mediated cell death
O’Donnell, M. A., & Ting, A. T. (2012) · Immunologic Research · doi:10.1007/s12026-012-8321-7 · Cited by 31
Davaro, F., Forde, S., Garfield, M. K., Jiang, Z., Halmen, K. A., Tamburro, N. D., Kurt‐Jones, E. A., Fitzgerald, K. A., Golenbock, D. T., & Wang, D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.571505 · Cited by 31
Altered mitochondrial calcium handling and cell death by necroptosis: An emerging paradigm
Faizan, M. I., & Ahmad, T. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.12.004 · Cited by 31
Leng, J., Zhao, W., Guo, J., Yu, G., Zhu, G., Ge, J., He, D., Xu, Y., Chen, X., Zhou, Y., et al. (2022) · Kidney International · doi:10.1016/j.kint.2022.08.019 · Cited by 30
Beyond canonical inflammasomes: emerging pathways in IL-1-mediated autoinflammatory disease
Lukens, J. R., & Kanneganti, T. (2014) · Seminars in Immunopathology · doi:10.1007/s00281-014-0434-8 · Cited by 30
Proteasome inhibition blocks necroptosis by attenuating death complex aggregation
Ali, M., & Mocarski, E. S. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0371-x · Cited by 31
Self-citationLi, K., Zhang, D., Zhai, S., Wu, H., & Liu, H. (2023) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-023-00737-y · Cited by 30
Yu, X., Gong, H., Zhou, Y., Zhang, H., Cao, J., & Zhou, J. (2015) · Parasites & Vectors · doi:10.1186/s13071-015-1213-7 · Cited by 30
Kavanagh, E. T., Burguillos, M. Á., Carrillo-Jiménez, A., Oliva-Martín, M. J., Santiago, M., Rodhe, J., Joseph, B., & Venero, J. L. (2015) · Aging · doi:10.18632/aging.100805 · Cited by 30
TRADD regulates perinatal development and adulthood survival in mice lacking RIPK1 and RIPK3
Dowling, J. P., Alsabbagh, M. Y., Casale, C. D., Liu, Z.-G., & Zhang, J. (2019) · Nature Communications · doi:10.1038/s41467-019-08584-5 · Cited by 30
Metadata
- Authors
- Kaiser, W. J., Upton, J. W., Long, A. B., Livingston-Rosanoff, D., Daley-Bauer, L. P., Hakem, R., Caspary, T., & Mocarski, E. S.
- Affiliations
- Emory University (US)
- University Health Network (CA)
- Corresponding author
- Kaiser, William J.
- ORCID
- Venue
- Nature
- Published
- 2011-03
- Volume
- 471
- Issue
- 7338
- Pages
- 368-372
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3060292
- OpenAlex
- W2042577315
- Cited by
- 1,057
- References
- 31
- Citations by year
- 2026: 37 · 2025: 60 · 2024: 56 · 2023: 51 · 2022: 66 · 2021: 61 · 2020: 70 · 2019: 55 · 2018: 68 · 2017: 59 · 2016: 88 · 2015: 75 · 2014: 120 · 2013: 69 · 2012: 71
- FWCI
- 40.08
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Georgia Cancer Coalition
- National Institutes of Health (DP5OD012198)
- National Institute of General Medical Sciences (T32GM008169)
- National Institute of Allergy and Infectious Diseases (R01AI030363, R01AI20211, R01AI020211, R56AI030363, R21AI030363, AI30363)
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Keywords
- caspase-8, necroptosis, embryonic lethality, death receptor signaling, FADD, Fas, RIPK1, apoptosis, lymphoid development, innate immunity, programmed cell death
- MeSH terms
- Animals, Cell Line, Embryo, Mammalian, Female, Immunocompetence, Lymphatic Diseases, Male, Mice, Inbred C57BL, Necrosis, Apoptosis, Gene Deletion, Mice, Knockout, GTPase-Activating Proteins, Embryo Loss, Mice, Caspase 8, Receptor-Interacting Protein Serine-Threonine Kinases, Caspase Inhibitors
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