DAI/ZBP1/DLM-1 Complexes with RIP3 to Mediate Virus-Induced Programmed Necrosis that Is Targeted by Murine Cytomegalovirus vIRA
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Programmed necrosis, like apoptosis, eliminates pathogen-infected cells as a component of host defense. Receptor-interacting protein kinase (RIP) 3 (also called RIPK3) mediates RIP homotypic interaction motif (RHIM)-dependent programmed necrosis induced by murine cytomegalovirus (MCMV) infection or death receptor activation and suppressed by the MCMV-encoded viral inhibitor of RIP activation (vIRA). We find that interferon-independent expression of DNA-dependent activator of interferon regulatory factors (DAI, also known as ZBP1 or DLM-1) sensitizes cells to virus-induced necrosis and that DAI knockdown or knockout cells are resistant to this death pathway. Importantly, as with RIP3(-/-) mice, vIRA mutant MCMV pathogenesis is restored in DAI(-/-) mice, consistent with a DAI-RIP3 complex being the natural target of vIRA. Thus, DAI interacts with RIP3 to mediate virus-induced necrosis analogous to the RIP1-RIP3 complex controlling death receptor-induced necroptosis. These studies unveil a role for DAI as the RIP3 partner mediating virus-induced necrosis.
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Necroptosis is a regulated form of necrosis triggered by intra- and extracellular signals and is initiated by chemokine receptors such as FAS, by pathogen recognition receptors such as TLR3, TLR4, and ZBP1, and by TNFR1.
“Necroptosis is a regulated form of necrosis triggered by intra- and extracellular signals and is initiated by chemokine receptors such as FAS [292], by pathogen recognition receptors such as Toll-like receptor (TLR)3, TLR4, and Z-DNA binding protein (ZBP)1 [293, 294], and by the TNF receptor (TNFR)1 [295].”
From Oligodendrocyte death and myelin loss in the cuprizone model: an updated overview of the intrinsic and extrinsic causes of cuprizone demyelination (2022) · cites this paper as [293]
The Results section states that TLR3 can induce necroptosis, and the Discussion identifies DAI/ZBP1 as a pattern-recognition receptor involved in virus-induced programmed necrosis. The citation is attached to the group of pathogen-recognition receptors, but our copy does not establish TLR4 as an initiator of necroptosis. (LLM, conf=0.84)
Experimental — accuracy not yet measuredNecroptosis is a form of RCD initiated by perturbations of extracellular or intracellular microenvironment detected by specific death receptors including FAS and TNFR1, or PRRs including TLR3, TLR4, ZBP1.
“Necroptosis is a form of RCD initiated by perturbations of the extracellular or intracellular microenvironment detected by specific death receptors, including (but not limited to) FAS and TNFR1 [423–427], or pathogen recognition receptors (PRRs), including TLR3, TLR4, and Z-DNA binding protein 1 (ZBP1; also known as DAI) [428–430].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [429]
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Cites
Hengartner, M. O. (2000) · Nature · doi:10.1038/35037710 · Cited by 7,295 · 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
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 · 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
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
DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response
Takaoka, A., Wang, Z., Choi, M. K., Yanai, H., Negishi, H., Ban, T., Lu, Y., Miyagishi, M., Kodama, T., Honda, K., et al. (2007) · Nature · doi:10.1038/nature06013 · Cited by 1,704 · see citing works
Strasser, A., O’Connor, L., & Dixit, V. M. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.217 · Cited by 1,369 · 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 · cited 4× · see citing works
“Likewise, the RIP3-dependent necroptosis resulting in lethality of Casp8−/− mice (Kaiser et al., 2011; Oberst et al., 2011) was not rescued loss of DAI (Figure S3D), and Casp8−/−DAI−/− embryos were phenotypically indistinguishable from Casp8−/− littermate embryos (data not shown).”
InfluentialRIP3 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
Self-citationFeoktistova, 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
Tenev, T., Bianchi, K., Darding, M., Broemer, M., Langlais, C., Wållberg, F., Zachariou, A., Lopez, J. S., MacFarlane, M., Cain, K., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.006 · Cited by 818 · 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
TANK-binding kinase-1 delineates innate and adaptive immune responses to DNA vaccines
Ishii, K. J., Kawagoe, T., Koyama, S., Matsui, K., Kumar, H., Kawai, T., Uematsu, S., Takeuchi, O., Takeshita, F., Coban, C., et al. (2008) · Nature · doi:10.1038/nature06537 · Cited by 628 · 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
Self-citationBurke, J. R., Pattoli, M. A., Gregor, K. R., Brassil, P. J., MacMaster, J. F., McIntyre, K. W., Yang, X., Iotzova, V. S., Clarke, W., Strnad, J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209677200 · Cited by 550 · 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
Manipulation of Host Cell Death Pathways during Microbial Infections
Lamkanfi, M., & Dixit, V. M. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.06.007 · Cited by 450 · see citing works
A cytomegalovirus-encoded inhibitor of apoptosis that suppresses caspase-8 activation
Skaletskaya, A., Bartle, L. M., Chittenden, T. D., McCormick, A. L., Mocarski, E. S., & Goldmacher, V. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.141108798 · Cited by 418 · see citing works
Self-citationDAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF‐κB
Rebsamen, M., Heinz, L. X., Meylan, E., Michallet, M., Schroder, K., Hofmann, K., Vázquez, J., Benedict, C. A., & Tschopp, J. (2009) · EMBO Reports · doi:10.1038/embor.2009.109 · Cited by 365 · see citing works
Regulation of innate immune responses by DAI (DLM-1/ZBP1) and other DNA-sensing molecules
Wang, Z., Choi, M. K., Ban, T., Yanai, H., Negishi, H., Lu, Y., Tamura, T., Takaoka, A., Nishikura, K., & Taniguchi, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801295105 · Cited by 337 · 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
Self-citationKaiser, W. J., Upton, J. W., & Mocarski, E. S. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.9.6427 · Cited by 277 · see citing works
Self-citationCytoplasmic DNA innate immune pathways
Barber, G. N. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01051.x · Cited by 247 · see citing works
A Ribonucleotide Reductase Homolog of Cytomegalovirus and Endothelial Cell Tropism
Brune, W., Ménard, C., Heesemann, J., & Koszinowski, U. H. (2001) · Science · doi:10.1126/science.291.5502.303 · Cited by 208 · see citing works
Human Cytomegalovirus Induces the Interferon Response via the DNA Sensor ZBP1
DeFilippis, V. R., Alvarado, D. M., Sali, T. M., Rothenburg, S., & Früh, K. (2009) · Journal of Virology · doi:10.1128/jvi.01748-09 · Cited by 204 · see citing works
Upton, J. W., Kaiser, W. J., & Mocarski, E. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c800051200 · Cited by 202 · see citing works
Self-citationRole of Murine Cytomegalovirus US22 Gene Family Members in Replication in Macrophages
Ménard, C., Wagner, M., Ruzsics, Z., Holak, K., Brune, W., Campbell, A. E., & Koszinowski, U. H. (2003) · Journal of Virology · doi:10.1128/jvi.77.10.5557-5570.2003 · Cited by 173 · see citing works
Viral Subversion of Apoptotic Enzymes: Escape from Death Row
Best, S. M. (2008) · Annual Review of Microbiology · doi:10.1146/annurev.micro.62.081307.163009 · Cited by 168 · see citing works
Fu, Y., Comella, N., Tognazzi, K., Brown, L. F., Dvorak, H. F., & Kocher, O. N. (1999) · Gene · doi:10.1016/s0378-1119(99)00419-9 · Cited by 162 · see citing works
Li, M. O., & Beg, A. A. (2000) · Journal of Virology · doi:10.1128/jvi.74.16.7470-7477.2000 · Cited by 144 · see citing works
Mack, C., Sickmann, A., Lembo, D., & Brune, W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800168105 · Cited by 141 · see citing works
McCormick, A. L., Skaletskaya, A., Barry, P. A., Mocarski, E. S., & Goldmacher, V. S. (2003) · Virology · doi:10.1016/j.virol.2003.07.003 · Cited by 140 · see citing works
Self-citationNecrosis is associated with IL-6 production but apoptosis is not
Berghe, T. V., Kalai, M., Denecker, G., Meeus, A., Saelens, X., & Vandenabeele, P. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.05.003 · Cited by 105 · see citing works
Lembo, D., Donalisio, M., Hofer, A., Cornaglia, M., Brune, W., Koszinowski, U. H., Thelander, L., & Landolfo, S. (2004) · Journal of Virology · doi:10.1128/jvi.78.8.4278-4288.2004 · Cited by 91 · see citing works
Lippmann, J., Rothenburg, S., Deigendesch, N., Eitel, J., Meixenberger, K., van Laak, V., Slevogt, H., N’Guessan, P. D., Hippenstiel, S., Chakraborty, T., et al. (2008) · Cellular Microbiology · doi:10.1111/j.1462-5822.2008.01232.x · Cited by 89 · see citing works
McCormick, A. L., Meiering, C. D., Smith, G. B., & Mocarski, E. S. (2005) · Journal of Virology · doi:10.1128/jvi.79.19.12205-12217.2005 · Cited by 78 · see citing works
Self-citationFurr, S. R., Chauhan, V. S., Moerdyk-Schauwecker, M. J., & Marriott, I. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-99 · Cited by 74 · see citing works
Benedict, C. A., Angulo, A., Patterson, G., et al. (2003) · Journal of Virology · doi:10.1128/jvi.78.2.741-750.2004 · Cited by 67 · see citing works
Cytomegaloviruses inhibit Bak- and Bax-mediated apoptosis with two separate viral proteins
Cam, M., Handke, W., Picard‐Maureau, M., et al. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.147 · Cited by 64 · see citing works
Multiple death pathways in TNF-treated fibroblasts: RIP3- and RIP1-dependent and independent routes
Zhang, D., Zheng, M., Zhao, J., Li, Y.-Y., Huang, Z., Li, Z., & Han, J. (2011) · Cell Research · doi:10.1038/cr.2011.3 · Cited by 60 · see citing works
DeFilippis, V. R., Sali, T. M., Alvarado, D. M., White, L., Bresnahan, W. A., & Früh, K. (2010) · Journal of Virology · doi:10.1128/jvi.00169-10 · Cited by 39 · see citing works
Karayel, E., Bürckstümmer, T., Bilban, M., Dürnberger, G., Weitzer, S., Martinez, J., & Superti‐Furga, G. (2009) · European Journal of Immunology · doi:10.1002/eji.200939344 · Cited by 33 · see citing works
Diverse TNFα-induced death pathways are enhanced by inhibition of NF-κB
Katdare, M., Efimova, E. V., Labay, E., Khodarev, N. N., Darga, T. E., Garofalo, M. C., Nakamura, S., Kufe, D. W., Posner, M. C., & Weichselbaum, R. R. (2007) · International Journal of Oncology · doi:10.3892/ijo.31.6.1519 · Cited by 8 · see citing works
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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-citationNLRP3 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
DNA damage and the balance between survival and death in cancer biology
Roos, W. P., Thomas, A. D., & Kaina, B. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2015.2 · Cited by 1,189 · see citing works
Li, J., McQuade, T., Siemer, A. B., Napetschnig, J., Moriwaki, K., Hsiao, Y.-S., Damko, E., Moquin, D., Walz, T., McDermott, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.019 · Cited by 1,222 · 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
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
Essential versus accessory aspects of cell death: recommendations of the NCCD 2015
Galluzzi, L., Bravo-San Pedro, J. M., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Alnemri, E. S., Altucci, L., Andrews, D., Annicchiarico-Petruzzelli, M., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.137 · Cited by 1,002 · see citing works
Toll-like Receptor 3-mediated Necrosis via TRIF, RIP3, and MLKL
Kaiser, W. J., Sridharan, H., Huang, C., Mandal, P., Upton, J. W., Gough, P. J., Sehon, C. A., Marquis, R. W., Bertin, J., & Mocarski, E. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.462341 · Cited by 959 · see citing works
Self-citationKuriakose, T., Man, S. M., Subbarao Malireddi, R. K., Karki, R., Kesavardhana, S., Place, D. E., Neale, G., Vogel, P., & Kanneganti, T.-D. (2016) · Science Immunology · doi:10.1126/sciimmunol.aag2045 · Cited by 818 · 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
Initiation and execution mechanisms of necroptosis: an overview
Grootjans, S., Vanden Berghe, T., & Vandenabeele, P. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.65 · Cited by 566 · 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
STING and the innate immune response to nucleic acids in the cytosol
Burdette, D. L., & Vance, R. E. (2013) · Nature Immunology · doi:10.1038/ni.2491 · Cited by 501 · see citing works
Dying cells actively regulate adaptive immune responses
Yatim, N., Cullen, S., & Albert, M. L. (2017) · Nature Reviews Immunology · doi:10.1038/nri.2017.9 · Cited by 442 · see citing works
RIPK1 counteracts ZBP1-mediated necroptosis to inhibit inflammation
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
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
Phototherapy in cancer treatment: strategies and challenges
Cai, Y., Chai, T., Nguyen, W., Liu, J., Xiao, E., Ran, X., Ran, Y., Du, D., Chen, W., & Chen, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02140-y · Cited by 453 · see citing works
RIPK1 inhibits ZBP1-driven necroptosis during development
Newton, K., Wickliffe, K. E., Maltzman, A., Dugger, D. L., Strasser, A., Pham, V. C., Lill, J. R., Roose-Girma, M., Warming, S., Solon, M., et al. (2016) · Nature · doi:10.1038/nature20559 · Cited by 390 · 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
Cytosolic DNA Sensing in Organismal Tumor Control
Vanpouille-Box, C., Demaria, S., Formenti, S. C., & Galluzzi, L. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.05.013 · Cited by 250 · 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
Sensing of viral and endogenous RNA by ZBP1/DAI induces necroptosis
Maelfait, J., Liverpool, L., Bridgeman, A., Ragan, K. B., Upton, J. W., & Rehwinkel, J. (2017) · The EMBO Journal · doi:10.15252/embj.201796476 · Cited by 237 · see citing works
Self-citationBanoth, B., Tuladhar, S., Karki, R., Sharma, B. R., Briard, B., Kesavardhana, S., Burton, A., & Kanneganti, T.-D. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015924 · Cited by 237 · see citing works
Zirngibl, M., Assinck, P., Sizov, A., Caprariello, A. V., & Plemel, J. R. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00538-8 · Cited by 233 · see citing works
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Ruder, B., Atreya, R., & Becker, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081887 · Cited by 228 · see citing works
Lytic cell death in metabolic liver disease
Gautheron, J., Gores, G. J., & Rodrigues, C. M. P. (2020) · Journal of Hepatology · doi:10.1016/j.jhep.2020.04.001 · Cited by 225 · see citing works
Xia, B., Fang, S., Chen, X., Hu, H., Chen, P., Wang, H., & Gao, Z. (2016) · Cell Research · doi:10.1038/cr.2016.26 · Cited by 202 · see citing works
Poly-ubiquitination in TNFR1-mediated necroptosis
Dondelinger, Y., Darding, M., Bertrand, M. J. M., & Walczak, H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2191-4 · Cited by 173 · see citing works
Horiguchi, H., Loftus, T. J., Hawkins, R. B., Raymond, S. L., Stortz, J. A., Hollen, M. K., Weiss, B. P., Miller, E. S., Bihorac, A., Larson, S. D., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00595 · Cited by 164 · see citing works
Jacobsen, A. V., Lowes, K. N., Tanzer, M. C., Lucet, I. S., Hildebrand, J. M., Petrie, E. J., van Delft, M. F., Liu, Z., Conos, S. A., Zhang, J.-G., et al. (2016) · Cell Death & Disease · doi:10.1038/cddis.2015.386 · Cited by 160 · see citing works
Location, location, location: A compartmentalized view of TNF-induced necroptotic signaling.
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Molecular mechanisms of necroptosis and relevance for neurodegenerative diseases.
(2020) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2019.12.006 · Cited by 51 · see citing works
The interplay of autophagy and non-apoptotic cell death pathways
(2020) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2019.12.004 · Cited by 50 · 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
Wang, Z., Feng, J., Yu, J., & Chen, G. (2019) · Journal of Cell Science · doi:10.1242/jcs.227777 · Cited by 35 · see citing works
Bencze, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010362 · Cited by 20 · see citing works
- Authors
- Upton, J. W., Kaiser, W. J., & Mocarski, E. S.
- Affiliations
- Emory University (US)
- Corresponding author
- Mocarski, Edward S.
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 11
- Issue
- 3
- Pages
- 290-297
- ISSN
- 1931-3128 (ISSN-L)
- PMC
- PMC3531981
- OpenAlex
- W2084414744
- Cited by
- 758
- References
- 44
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- FWCI
- 18.74
- Type
- journal article
- Language
- en
- Update notices
- addendum (2019-10-09)
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- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 503 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell Host & Microbe (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Biomedical Innovation
- National Institutes of Health (1f32ai080175-01a1)
- National Institute of Allergy and Infectious Diseases (R01AI030363, R01AI20211, R01AI020211, F32 AI080175, R56AI030363, R21AI030363, AI30363, F32 AI080175-01A1)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Epidemiology › Cytomegalovirus and herpesvirus research
- Keywords
- necroptosis, RIPK3, DAI, ZBP1, murine cytomegalovirus, VirA, virus-induced cell death, host defense against viruses, protein complex formation
- MeSH terms
- Animals, Glycoproteins, Herpesviridae Infections, Inflammation, Mice, Inbred C57BL, Necrosis, Viral Proteins, Signal Transduction, NF-kappa B, RNA-Binding Proteins, Interferon-beta, Apoptosis, Muromegalovirus, Mice, Knockout, Viral Load, NIH 3T3 Cells, Multiprotein Complexes, Mice, Receptor-Interacting Protein Serine-Threonine Kinases, Host-Pathogen Interactions
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 ›
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