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Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity
Open accessAbstract
Caspase-8 (casp8) is required for extrinsic apoptosis, and mice deficient in casp8 fail to develop and die in utero while ultimately failing to maintain the proliferation of T cells, B cells, and a host of other cell types. Paradoxically, these failures are not caused by a defect in apoptosis, but by a presumed proliferative function of this protease. Indeed, following mitogenic stimulation, T cells lacking casp8 or its adaptor protein FADD (Fas-associated death domain protein) develop a hyperautophagic morphology, and die a programmed necrosis-like death process termed necroptosis. Recent studies have demonstrated that receptor-interacting protein kinases (RIPKs) RIPK1 and RIPK3 together facilitate TNF-induced necroptosis, but the precise role of RIPKs in the demise of T cells lacking FADD or casp8 activity is unknown. Here we demonstrate that RIPK3 and FADD have opposing and complementary roles in promoting T-cell clonal expansion and homeostasis. We show that the defective proliferation of T cells bearing an interfering form of FADD (FADDdd) is rescued by crossing with RIPK3 −/− mice, although such rescue ultimately leads to lymphadenopathy. Enhanced recovery of these double-mutant T cells following stimulation demonstrates that FADD, casp8, and RIPK3 are all essential for clonal expansion, contraction, and antiviral responses. Finally, we demonstrate that caspase-mediated cleavage of RIPK1-containing necrosis inducing complexes (necrosomes) is sufficient to prevent necroptosis in the face of death receptor signaling. These studies highlight the “two-faced” nature of casp8 activity, promoting clonal expansion in some situations and apoptotic demise in others.
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“Moreover, the proliferative defects of Casp8−/− or Fadd−/− T cells can be rescued by the administration of the RIPK1 inhibitor Nec-1 or the concomitant ablation of Ripk3 [489].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [489]
Citations
Cites
Death Receptors: Signaling and Modulation
Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866
T cell receptor antagonist peptides induce positive selection.
Hogquist, K., Jameson, S., Heath, W., Howard, J. L., Bevan, M., & Carbone, F. (1994) · Cell · doi:10.1016/0092-8674(94)90169-4 · Cited by 3,252
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
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
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
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
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
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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
Necroptosis and its role in inflammation
Pasparakis, M., & Vandenabeele, P. (2015) · Nature · doi:10.1038/nature14191 · Cited by 2,148
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
Cell Death SignalingPreprint
Green, D. R., & Llambi, F. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a006080 · Cited by 1,178
Programmed cell death as a defence against infection
Jørgensen, I., Rayamajhi, M., & Miao, E. A. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2016.147 · Cited by 1,057
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
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 740
Koo, G.-B., Morgan, M. J., Lee, D., Kim, W.-J., Yoon, J.-H., Koo, J. S., Kim, S. H., Kim, S., Son, M. K., Hong, S. S., et al. (2015) · Cell Research · doi:10.1038/cr.2015.56 · Cited by 500
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
Newton, K., & Manning, G. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014830 · Cited by 410
Programmed necrosis: backup to and competitor with apoptosis in the immune system
Han, J., Zhong, C., & Zhang, D. (2011) · Nature Immunology · doi:10.1038/ni.2159 · Cited by 375
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 377
Interferon-induced RIP1/RIP3-mediated necrosis requires PKR and is licensed by FADD and caspases
Thapa, R. J., Nogusa, S., Chen, P., Maki, J. L., Lerro, A., Andrake, M., Rall, G. F., Degterev, A., & Balachandran, S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301218110 · Cited by 355
RIP3: a molecular switch for necrosis and inflammationPreprint
Moriwaki, K., & Chan, F. K.-M. (2013) · Genes & Development · doi:10.1101/gad.223321.113 · Cited by 364
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 359
Cancer therapy in the necroptosis era
Su, Z., Yang, Z., Xie, L., DeWitt, J. P., & Chen, Y. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.8 · Cited by 343
Distinct roles of RIP1–RIP3 hetero- and RIP3–RIP3 homo-interaction in mediating necroptosis
Wu, X.-N., Yang, Z.-H., Wang, X.-K., Zhang, Y., Wan, H., Song, Y., Chen, X., Shao, J., & Han, J. (2014) · Cell Death & Differentiation · doi:10.1038/cdd.2014.77 · Cited by 299
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 309
Chaabane, W., User, S. D., El-Gazzah, M., Jaksik, R., Sajjadi, E., Rzeszowska‐Wolny, J., & Łoś, M. (2012) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-012-0205-y · Cited by 290
Regulated Cell Death: Signaling and Mechanisms
Ashkenazi, A., & Salvesen, G. S. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013226 · Cited by 289
Self-citationWang, J., Zhang, X.-J., Li, Q., Wang, K., Wang, Y., Jiao, J.-Q., Feng, C., Sun, T., Zhou, L., Gong, Y., et al. (2015) · Circulation Research · doi:10.1161/circresaha.117.305781 · Cited by 265
Crosstalk between Long Noncoding RNAs and MicroRNAs in Health and Disease
Bayoumi, A., Sayed, A., Brosková, Z., Teoh, J., Wilson, J., Su, H., Tang, Y., & Kim, I. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17030356 · Cited by 223
The ‘complexities’ of life and death: Death receptor signalling platforms
Dickens, L. S., Powley, I. R., Hughes, M. A., & MacFarlane, M. (2012) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.04.005 · Cited by 208
Programmed Cell Death, from a Cancer Perspective: An Overview
Mishra, A. P., Salehi, B., Sharifi‐Rad, M., Pezzani, R., Kobarfard, F., Sharifi‐Rad, J., & Nigam, M. (2018) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-018-0329-9 · Cited by 200
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 197
The molecular relationships between apoptosis, autophagy and necroptosis
Lalaoui, N., Lindqvist, L., Sandow, J. J., & Ekert, P. G. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.02.003 · Cited by 181
It cuts both ways: reconciling the dual roles of caspase 8 in cell death and survival
Oberst, A., & Green, D. R. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3214 · Cited by 160
RIP1/RIP3-regulated necroptosis as a target for multifaceted disease therapy (Review)
Liu, Y., Liu, T., Lei, T., Zhang, D., Du, S., Girani, L., Qi, D., Chen, L., Tong, R., & Wang, Y. (2019) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2019.4244 · Cited by 157
Viral modulation of programmed necrosis
Kaiser, W. J., Upton, J. W., & Mocarski, E. S. (2013) · Current Opinion in Virology · doi:10.1016/j.coviro.2013.05.019 · Cited by 151
Caspase blockade induces RIP3-mediated programmed necrosis in Toll-like receptor-activated microglia
Kim, S. J., & Li, J. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.238 · Cited by 149
The roles of FADD in extrinsic apoptosis and necroptosis
Lee, E., Seo, J.-H., Jeong, M.-H., Lee, S.-S., & Song, J.-W. (2012) · BMB Reports · doi:10.5483/bmbrep.2012.45.9.186 · Cited by 137
Functions of caspase 8: The identified and the mysterious
Salvesen, G. S., & Walsh, C. M. (2014) · Seminars in Immunology · doi:10.1016/j.smim.2014.03.005 · Cited by 141
Self-citationLee, E., Kim, J.-H., Ahn, Y.-H., Seo, J., Ko, A., Jeong, M., Kim, S.-J., Ro, J. Y., Park, K.-M., Lee, H., et al. (2012) · Nature Communications · doi:10.1038/ncomms1981 · Cited by 130
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 134
RIPK1 can mediate apoptosis in addition to necroptosis during embryonic development
Zhang, X., Dowling, J. P., & Zhang, J. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1490-8 · Cited by 115
Necroptosis: The Trojan horse in cell autonomous antiviral host defense
Mocarski, E. S., Guo, H., & Kaiser, W. J. (2015) · Virology · doi:10.1016/j.virol.2015.03.016 · Cited by 108
Current translational potential and underlying molecular mechanisms of necroptosis
Molnár, T., Mázló, A., Tslaf, V., Szöllősi, A. G., Emri, G., & Koncz, G. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2094-z · Cited by 110
SETDB1-Mediated Cell Fate Transition between 2C-Like and Pluripotent States
Wu, K., Liu, H., Wang, Y., He, J., Xu, S., Chen, Y., Kuang, J., Liu, J., Guo, L., Li, D., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.010 · Cited by 104
The Inflammatory Signal Adaptor RIPK3: Functions Beyond Necroptosis
Moriwaki, K., & Chan, F. K.-M. (2016) · International review of cytology · doi:10.1016/bs.ircmb.2016.08.007 · Cited by 107
Ammonia regulates chicken tracheal cell necroptosis via the LncRNA-107053293/MiR-148a-3p/FAF1 axis
Wang, W. J., Shi, Q., Wang, S., Zhang, H., & Xu, S. (2019) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2019.121626 · Cited by 102
Necroptotic Cell Death Signaling and Execution Pathway: Lessons from Knockout Mice
Belizário, J. E., Cordeiro, L., & Enns, S. C. (2015) · Mediators of Inflammation · doi:10.1155/2015/128076 · Cited by 106
Necroptosis-independent signaling by the RIP kinases in inflammation
Moriwaki, K., & Chan, F. K.-M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2203-4 · Cited by 99
Khan, N. R., Lawlor, K. E., Murphy, J. M., & Vince, J. E. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2013.10.017 · Cited by 93
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
Self-citationNecroptosis in tumorigenesis, activation of anti-tumor immunity, and cancer therapy
Meng, M.-B., Wang, H.-H., Cui, Y.-L., Wu, Z.-Q., Shi, Y., Zaorsky, N. G., Deng, L., Yuan, Z., Lü, Y., & Wang, P. (2016) · Oncotarget · doi:10.18632/oncotarget.10548 · Cited by 91
The role of caspase-8 in inflammatory signalling and pyroptotic cell death
Pang, J., & Vince, J. E. (2023) · Seminars in Immunology · doi:10.1016/j.smim.2023.101832 · Cited by 90
Programmed necrosis and autophagy in immune function
Lu, J. V., & Walsh, C. M. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01147.x · Cited by 82
Self-citationNecroptosis in Intestinal Inflammation and Cancer: New Concepts and Therapeutic Perspectives
Negroni, A., Colantoni, E., Cucchiara, S., & Stronati, L. (2020) · Biomolecules · doi:10.3390/biom10101431 · Cited by 81
True Grit: Programmed Necrosis in Antiviral Host Defense, Inflammation, and Immunogenicity
Mocarski, E. S., Kaiser, W. J., Livingston‐Rosanoff, D., Upton, J. W., & Daley‐Bauer, L. P. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302426 · Cited by 75
TNF-α sensitizes chemotherapy and radiotherapy against breast cancer cells
Wu, X., Wu, M., Jiang, M., Zhi, Q., Bian, X., Xu, M., Gong, F.-R., Hou, J., Tao, M., Shou, L., et al. (2017) · Cancer Cell International · doi:10.1186/s12935-017-0382-1 · Cited by 73
A Non-canonical PDK1-RSK Signal Diminishes Pro-caspase-8-Mediated Necroptosis Blockade
Yang, Z., Wu, X., He, P., Wang, X., Wu, J., Ai, T., Zhong, C., Wu, X., Yu, C., Zhu, R., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.09.004 · Cited by 70
Necroptotic signaling in adaptive and innate immunity
Lu, J. V., Chen, H. C., & Walsh, C. M. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.07.003 · Cited by 71
Self-citationRIPK3 interacts with MAVS to regulate type I IFN-mediated immunity to Influenza A virus infection
Downey, J., Pernet, E., Coulombe, F., Allard, B., Meunier, I., Jaworska, J., Qureshi, S. T., Vinh, D. C., Martin, J. G., Joubert, P., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006326 · Cited by 68
Programmed Necrosis: A Prominent Mechanism of Cell Death following Neonatal Brain Injury
Chavez‐Valdez, R., Martin, L. J., & Northington, F. J. (2012) · Neurology Research International · doi:10.1155/2012/257563 · Cited by 64
DeLaney, A. A., Berry, C. T., Christian, D. A., Hart, A. P., Bjånes, E., Wynosky-Dolfi, M. A., Li, X., Tummers, B., Udalova, I. A., Chen, Y. H., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1820529116 · Cited by 58
DED or alive: assembly and regulation of the death effector domain complexes
Riley, J. S., Malik, A., Holohan, C., & Longley, D. B. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.213 · Cited by 60
Intrinsic cleavage of receptor-interacting protein kinase-1 by caspase-6
van Raam, B. J., Ehrnhoefer, D. E., Hayden, M. R., & Salvesen, G. S. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.98 · Cited by 54
Self-citationKim, L. A., Amarnani, D., Gnanaguru, G., Tseng, W. A., Vavvas, D. G., & D'Amore, P. A. (2014) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.13-13662 · Cited by 47
The role of necroptosis in the treatment of diseases
Cho, Y. S. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.5.074 · Cited by 48
Barati, M., Javidi, M. A., Darvishi, B., Shariatpanahi, S. P., Moosavi, Z. S. M., Ghadirian, R., Khani, T., Sanati, H., Simaee, H., Barough, M. S., et al. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.04.002 · Cited by 47
Mechanisms and pathogenesis underlying environmental chemical-induced necroptosis
Sepand, M. R., Aliomrani, M., Nourian, Y. H., Khalhori, M.-R., Farzaei, M. H., & Sanadgol, N. (2020) · Environmental Science and Pollution Research · doi:10.1007/s11356-020-09360-5 · Cited by 45
Grand challenges in cell death and survival: apoptosis vs. necroptosis
Walsh, C. M. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00003 · Cited by 43
Self-citationHIV-1 protease cleaves the serine-threonine kinases RIPK1 and RIPK2
Wagner, R. N., Reed, J. C., & Chanda, S. K. (2015) · Retrovirology · doi:10.1186/s12977-015-0200-6 · Cited by 41
Cellular Dynamics of Fas-Associated Death Domain in the Regulation of Cancer and Inflammation
Ranjan, K., & Pathak, C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063228 · Cited by 36
Fueling the Flames: Mammalian Programmed Necrosis in Inflammatory DiseasesPreprint
Chan, F. K.-M. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008805 · Cited by 37
The serine threonine kinase RIP3: lost and found
Morgan, M. J., & Kim, Y. (2015) · BMB Reports · doi:10.5483/bmbrep.2015.48.6.068 · Cited by 38
Yu, X., Mao, M., Liu, X., Shen, T., Li, T., Yu, H., Zhang, J., Chen, X., Zhao, X., & Zhu, D. (2020) · Journal of Molecular Medicine · doi:10.1007/s00109-020-01886-y · Cited by 35
Montero, M. L., Liu, J., Orozco, J. L., Casiano, C. A., & León, M. A. D. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15038 · Cited by 35
Arshad, M. I., Piquet‐Pellorce, C., Filliol, A. A., L’Helgoualc’h, A., Lucas‐Clerc, C., Jouan-Lanhouet, S., Dimanche‐Boitrel, M., & Samson, M. (2015) · Journal of Molecular Medicine · doi:10.1007/s00109-015-1270-6 · Cited by 34
Mechanisms of Dysregulated Humoral and Cellular Immunity by SARS-CoV-2
Taefehshokr, N., Taefehshokr, S., & Heit, B. (2020) · Pathogens · doi:10.3390/pathogens9121027 · Cited by 35
Inflammatory cell death induced by cytotoxic lymphocytes: a dangerous but necessary liaison
de Miguel, D., Ramírez-Labrada, A., Uranga-Murillo, I., Hidalgo, S., Santiago, L., Gálvez, E. M., Arias, M. A., & Pardo, J. (2021) · FEBS Journal · doi:10.1111/febs.16093 · Cited by 33
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
Cloaked in ubiquitin, a killer hides in plain sight: the molecular regulation of RIPK 1
Justus, S. J., & Ting, A. T. (2015) · Immunological Reviews · doi:10.1111/imr.12304 · Cited by 27
Guo, R., Lin, B., Pan, J., Liong, E. C., Xu, A. M., Youdim, M. B. H., Fung, M., So, K., & Tipoe, G. L. (2016) · Scientific Reports · doi:10.1038/srep32447 · Cited by 26
A unique death pathway keeps RIPK1 D325A mutant mice in check at embryonic day 10.5
Zhang, Y., Huang, K., Zhang, Y., Tao, H., Li, L., Ruan, C., Sun, Y.-H., Shi, W., Han, W., Wu, S., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001304 · Cited by 26
Caspase-8 restricts antiviral CD8 T cell hyperaccumulation
Feng, Y., Daley‐Bauer, L. P., Roback, L., Guo, H., Koehler, H. S., Potempa, M., Lanier, L. L., & Mocarski, E. S. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904319116 · Cited by 26
Habib, P., Stamm, A.-S., Zeyen, T., Noristani, R., Slowik, A., Beyer, C., Wilhelm, T., Huber, M., Komnig, D., Schulz, J., et al. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.112978 · Cited by 22
Just, S., Nishanth, G., Buchbinder, J. H., Wang, X., Naumann, M., Lavrik, I. N., & Schlüter, D. (2016) · Scientific Reports · doi:10.1038/srep39796 · Cited by 24
Dowling, J. P., Nair, A., & Zhang, J. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00012 · Cited by 24
Li, Z., Wang, H., Wang, Z., & Geng, Y. (2022) · Molecules · doi:10.3390/molecules27227682 · Cited by 22
Dong, Z., Li, H., Wang, Y., Lin, S., Guo, F., Zhao, J., Yao, R., Li, Z., Wang, W., Buttino, I., et al. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.165785 · Cited by 23
IAP antagonists sensitize murine osteosarcoma cells to killing by TNFα
Shekhar, T. M., Miles, M. A., Gupte, A., Taylor, S., Tascone, B., Walkley, C. R., & Hawkins, C. J. (2016) · Oncotarget · doi:10.18632/oncotarget.8980 · Cited by 22
Use of a glycerin-based gel sheeting in scar management.
Baum, T. M., & Busuito, M. J. (1998) · PubMed · Cited by 21
RIPK3 in necroptosis and cancer
Morgan, M. J., & Kim, Y. (2025) · Molecules and Cells · doi:10.1016/j.mocell.2025.100199 · Cited by 21
Peng, L. (2024) · Clinical Immunology · doi:10.1016/j.clim.2024.110313 · Cited by 20
c-FLIP Protects T Lymphocytes from Apoptosis in the Intrinsic Pathway
He, M., & He, Y.-W. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1400469 · Cited by 18
He, L., Zhan, F., Lu, L., Zhang, X., & Wu, J. (2023) · BMC Pregnancy and Childbirth · doi:10.1186/s12884-023-05821-0 · Cited by 16
Ran, R., Zhang, S.-B., Shi, Y., Song, W., Song, W., Dong, Y.-B., Zhou, K., & Zhang, H. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112616 · Cited by 15
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Metadata
- Authors
- Lu, J. V., Weist, B. M., van Raam, B. J., Marro, B. S., Nguyen, L. V., Srinivas, P., Bell, B. D., Luhrs, K. A., Lane, T. E., Salvesen, G. S., & Walsh, C. M.
- Affiliations
- University of California, Irvine (US)
- Sanford–Burnham Medical Research Institute, La Jolla, CA 92037
- Sanford Burnham Prebys Medical Discovery Institute (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2011-08-29
- Volume
- 108
- Issue
- 37
- Pages
- 15312-15317
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3174674
- OpenAlex
- W2089868528
- Cited by
- 122
- References
- 40
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 6 · 2023: 4 · 2022: 4 · 2021: 4 · 2020: 10 · 2019: 10 · 2018: 6 · 2017: 5 · 2016: 13 · 2015: 17 · 2014: 14 · 2013: 10 · 2012: 11
- FWCI
- 5.07
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA 69381, P01CA069381, P30CA062203, T32CA009054)
- National Institute of Allergy and Infectious Diseases (R01AI063419, AI50506, R01AI050506, AI63419)
- National Institute of Neurological Disorders and Stroke (NS41249, R01NS041249)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- FADD, RIPK3, caspase-8, T cell homeostasis, T cell clonal expansion, necroptosis, necrosome, RIPK1, antiviral immunity, death receptor signaling, apoptosis, lymphadenopathy, T cell proliferation
- MeSH terms
- Animals, Cell Survival, Crosses, Genetic, Female, Murine hepatitis virus, Hepatitis, Viral, Animal, Homeostasis, Immunity, Male, CD8-Positive T-Lymphocytes, Cell Proliferation, Mice, Fas-Associated Death Domain Protein, Receptor-Interacting Protein Serine-Threonine Kinases
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