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Induction of TNF Receptor I-Mediated Apoptosis via Two Sequential Signaling Complexes
Open accessAbstract
Apoptosis induced by TNF-receptor I (TNFR1) is thought to proceed via recruitment of the adaptor FADD and caspase-8 to the receptor complex. TNFR1 signaling is also known to activate the transcription factor NF-kappa B and promote survival. The mechanism by which this decision between cell death and survival is arbitrated is not clear. We report that TNFR1-induced apoptosis involves two sequential signaling complexes. The initial plasma membrane bound complex (complex I) consists of TNFR1, the adaptor TRADD, the kinase RIP1, and TRAF2 and rapidly signals activation of NF-kappa B. In a second step, TRADD and RIP1 associate with FADD and caspase-8, forming a cytoplasmic complex (complex II). When NF-kappa B is activated by complex I, complex II harbors the caspase-8 inhibitor FLIP(L) and the cell survives. Thus, TNFR1-mediated-signal transduction includes a checkpoint, resulting in cell death (via complex II) in instances where the initial signal (via complex I, NF-kappa B) fails to be activated.
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“The outcome of TNFα exposure on cell fate depends on the activities of two separate TNFR complexes, one of which mediates survival through activation of nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) 55.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [55]
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Cites
Death Receptors: Signaling and Modulation
Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866
Wang, C.-Y., Mayo, M., Korneluk, R., Goeddel, D., & Baldwin, A. (1998) · Science · doi:10.1126/science.281.5383.1680 · Cited by 2,950
NF-κB at the crossroads of life and death
Karin, M., & Lin, A. (2002) · Nature Immunology · doi:10.1038/ni0302-221 · Cited by 2,709
Inhibition of death receptor signals by cellular FLIP
Irmler, M., Thome, M., Hahne, M., Schneider, P., Hofmann, K., Steiner, V., Bodmer, J.-L., Schröter, M., Burns, K., Mattmann, C., et al. (1997) · Nature · doi:10.1038/40657 · Cited by 2,548
Self-citationHsu, H., Shu, H., Pan, M., & Goeddel, D. V. (1996) · Cell · doi:10.1016/s0092-8674(00)80984-8 · Cited by 1,998
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
Self-citationTNF-R1 Signaling: A Beautiful Pathway
Chen, G., & Goeddel, D. V. (2002) · Science · doi:10.1126/science.1071924 · Cited by 1,930
Signal transduction by tumor necrosis factor and its relatives.
Baud, V., & Karin, M. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02064-5 · Cited by 1,741
CD95's deadly mission in the immune system
Krammer, P. H. (2000) · Nature · doi:10.1038/35037728 · Cited by 1,710
Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors
Thome, M., Schneider, P., Hofmann, K., Fickenscher, H., Meinl, E., Neipel, F., Mattmann, C., Burns, K., Bodmer, J.-L., Schröter, M., et al. (1997) · Nature · doi:10.1038/386517a0 · Cited by 1,316
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Modulation of apoptosis as a target for liver disease
Eichhorst, S. T. (2005) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.9.1.83 · Cited by 54
Stang, M. T., Armstrong, M. J., Watson, G. A., Sung, K. Y., Liu, Y., Ren, B., & Yim, J. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210470 · Cited by 55
Increased Soluble TNF Receptor 2 in Antidepressant-Free Patients with Late-Life Depression
Diniz, B. S., Teixeira, A. L., Talib, L. L., Mendonça, V. A., Gattaz, W. F., & Forlenza, O. V. (2010) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2010.02.008 · Cited by 54
Phosphoproteome profiling uncovers a key role for CDKs in TNF signaling
Tanzer, M. C., Bludau, I., Stafford, C. A., Hornung, V., & Mann, M. (2021) · Nature Communications · doi:10.1038/s41467-021-26289-6 · Cited by 53
Transmembrane TNF–TNFR2 Impairs Th17 Differentiation by Promoting Il2 Expression
Miller, P. G., Bonn, M. B., & McKarns, S. C. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500286 · Cited by 53
Membrane Trafficking of Death Receptors: Implications on Signalling
Schneider‐Brachert, W., Heigl, U., & Ehrenschwender, M. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140714475 · Cited by 54
Du, Q., Jiang, L., Wang, X., Wang, M., She, F., & Chen, Y. (2014) · Cancer Science · doi:10.1111/cas.12504 · Cited by 54
Ma, E., Wang, X., Li, Y., Sun, X., Tai, W., Li, T., & Guo, T. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.06.008 · Cited by 55
RIP Kinase-Mediated Necrosis as an Alternative Mechanism of Photoreceptor Death
Murakami, Y., Miller, J. W., & Vavvas, D. G. (2011) · Oncotarget · doi:10.18632/oncotarget.286 · Cited by 56
Kurada, B. R. V. V. S. N., Li, L. C., Mulherkar, N., Subramanian, M., Prasad, K. V. S., & Prabhakar, B. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808554200 · Cited by 54
Necroptosis: A novel manner of cell death, associated with stroke (Review)
Liu, C., Zhang, K., Shen, H., Yao, X., Sun, Q., & Chen, G. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3279 · Cited by 53
TNFα sensitizes hepatocytes to FasL-induced apoptosis by NFκB-mediated Fas upregulation
Faletti, L. E., Peintner, L., Neumann, S., Sandler, S., Grabinger, T., Nelly, S. M., Merfort, I., Huang, C., Tschaharganeh, D. F., Kang, T.-W., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0935-9 · Cited by 55
SMAC mimetics and RIPK inhibitors as therapeutics for chronic inflammatory diseases
Jensen, S., Seidelin, J. B., LaCasse, E. C., & Nielsen, O. H. (2020) · Science Signaling · doi:10.1126/scisignal.aax8295 · Cited by 55
Bata, N., & Cosford, N. D. P. (2021) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.1c00130 · Cited by 60
Endothelial Cell Dysfunction, Injury and Death
Pober, J. S., & Min, W. (2006) · Springer eBooks · doi:10.1007/3-540-36028-x_5 · Cited by 54
The Role of Death Receptor Ligands in Shaping Tumor Microenvironment
Whiteside, T. L. (2006) · Immunological Investigations · doi:10.1080/08820130600991893 · Cited by 54
Wachter, T., Sprick, M. R., Hausmann, D., Kerstan, A., McPherson, K., Stassi, G., Bröcker, E., Walczak, H., & Leverkus, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409554200 · Cited by 55
AMPK and its Activator Berberine in the Treatment of Neurodegenerative Diseases
Qin, S., Tang, H., Li, W., Gong, Y., Li, S., Huang, J., Fang, Y., Yuan, W., Liu, Y., Wang, S., et al. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200523172334 · Cited by 53
Tang, L., Liu, S., Li, S., Chen, Y., Xie, B., & Zhou, J. F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210127 · Cited by 57
High-fat diet and neuroinflammation: The role of mitochondria
Song, M., Bai, Y., & Song, F. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107615 · Cited by 60
Maurya, A. K., & Vinayak, M. (2015) · Tumor Biology · doi:10.1007/s13277-015-3634-5 · Cited by 53
Yang, D., Yaguchi, T., Yamamoto, H., & Nishizaki, T. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.01.020 · Cited by 53
TNFα-induced macrophage death via caspase-dependent and independent pathways
Tran, T. M., Temkin, V., Shi, B., Pagliari, L. J., Daniel, S., Ferran, C. J., & Pope, R. M. (2009) · APOPTOSIS · doi:10.1007/s10495-009-0311-4 · Cited by 56
A Death Receptor-associated Anti-apoptotic Protein, BRE, Inhibits Mitochondrial Apoptotic Pathway
Li, Q., Ching, A. K.-K., Chan, B. C.-L., Chow, S. K.-Y., Lim, P., Ho, T. C.-Y., Ip, W., Wong, C. K., Lam, C. W.-K., Lee, K. K., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408678200 · Cited by 53
Assays for Necroptosis and Activity of RIP Kinases
Degterev, A., Zhou, W., Maki, J. L., & Yuan, J. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801430-1.00001-9 · Cited by 53
FADD regulates NF-κB activation and promotes ubiquitination of cFLIPL to induce apoptosis
Ranjan, K., & Pathak, C. (2016) · Scientific Reports · doi:10.1038/srep22787 · Cited by 53
Autocrine Tnf signaling favors malignant cells in myelofibrosis in a Tnfr2-dependent fashion
Heaton, W. L., Senina, A. V., Pomicter, A. D., Salama, M. E., Clair, P. M., Yan, D., Bell, R. N., Gililland, J. M., Prchal, J. T., O’Hare, T., et al. (2018) · Leukemia · doi:10.1038/s41375-018-0131-z · Cited by 56
Advances in RIPK1 kinase inhibitors
Chen, L., Zhang, X., Ou, Y., Liu, M., Yu, D., Song, Z., Niu, L., Zhang, L., & Shi, J. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.976435 · Cited by 56
Mitochondrial DNA in cell death and inflammation
Heilig, R., Lee, J., & Tait, S. W. G. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221525 · Cited by 56
Yang, T., Qu, X., Zhao, J., Wang, X., Wang, Q., Dai, J., Zhu, C., Li, J., & Jiang, L. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01175-4 · Cited by 54
Davidovich, P. B., Higgins, C. A., Najda, Z., Longley, D. B., & Martin, S. J. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113476 · Cited by 57
Mitochondrial Quality Control in Health and Disease
Ye, L., Fu, X., & Li, Q. (2025) · MedComm · doi:10.1002/mco2.70319 · Cited by 60
Ramaswamy, M., Clel, S. Y., Cruz, A. C., & Siegel, R. M. (2009) · Results and problems in cell differentiation · doi:10.1007/400_2008_24 · Cited by 52
Kang, H. W., Kim, J. M., Cha, M. Y., Jung, H. C., Song, I. S., & Kim, J. S. (2012) · Digestive Diseases and Sciences · doi:10.1007/s10620-012-2237-x · Cited by 52
The TL1A/DR3/DcR3 pathway in autoimmune rheumatic diseases
Siakavellas, S. I., Sfikakis, P. P., & Bamias, G. (2015) · Seminars in Arthritis and Rheumatism · doi:10.1016/j.semarthrit.2015.02.007 · Cited by 52
Verbert, L., Lee, B., Kocks, S. L., Assefa, Z., Parys, J. B., Missiaen, L., Callewaert, G., Fissore, R. A., SMEDT, H. D., & Bultynck, G. (2007) · Biology of the Cell · doi:10.1042/bc20070086 · Cited by 52
Juric, V., Chen, C.-C., & Lau, L. F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031303 · Cited by 52
Human C1q Induces Apoptosis in an Ovarian Cancer Cell Line via Tumor Necrosis Factor Pathway
Kaur, A., Sultan, S. H. A., Murugaiah, V., Pathan, A. A., Alhamlan, F. S., Karteris, E., & Kishore, U. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00599 · Cited by 53
Armaka, M., Ospelt, C., Pasparakis, M., & Kollias, G. A. (2018) · Nature Communications · doi:10.1038/s41467-018-02935-4 · Cited by 52
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Kang, K., Ok, M., & Lee, S. (2020) · Journal of Obesity & Metabolic Syndrome · doi:10.7570/jomes20120 · Cited by 53
Low temperature protects mammalian cells from apoptosis initiated by various stimuli in vitro
Sakurai, T., Itoh, K., Liu, Y., Higashitsuji, H., Sumitomo, Y., Sakamaki, K., & Fujita, J. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.06.002 · Cited by 52
Caruso, J. A., Mathieu, P., Joiakim, A., Zhang, H., & Reiners, J. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508383200 · Cited by 53
PKC-mediated phosphorylation regulates c-FLIP ubiquitylation and stability
Kaunisto, A., Kochin, V., Asaoka, T., Mikhailov, A., Poukkula, M., Meinander, A., & Eriksson, J. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.35 · Cited by 51
Gururaja, T. L., Yung, S. L., Ding, R., Huang, J., Zhou, X., McLaughlin, J. R., Daniel-Issakani, S., Singh, R., COOPER, R. D. G., Payan, D. G., et al. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.08.012 · Cited by 51
Espino, J., Rodríguez, A. B., & Pariente, J. A. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12042 · Cited by 51
Moriwaki, K., Shinzaki, S., & Miyoshi, E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.262741 · Cited by 51
Death by Committee: Organellar Trafficking and Communication in Apoptosis
Aslan, J. E., & Thomas, G. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00951.x · Cited by 51
Reyes‐Zurita, F. J., Rufino‐Palomares, E. E., Garcı́a-Salguero, L., Peragón, J., Medina, P. P., Parra, A., Cascante, M., & Lupiáñez, J. A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0146178 · Cited by 51
T Cells and Regulated Cell Death
Spetz, J. K. E., Presser, A. G., & Sarosiek, K. A. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.07.004 · Cited by 55
Linear ubiquitination of cFLIP induced by LUBAC contributes to TNFα-induced apoptosis
Tang, Y., Joo, D., Liu, G., Tu, H., You, J., Jin, J., Zhao, X., Hung, M., & Lin, X. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005449 · Cited by 50
Palmitoylation is required for TNF-R1 signaling
Zingler, P., Särchen, V., Glatter, T., Caning, L., Saggau, C., Kathayat, R. S., Dickinson, B. C., Adam, D., Schneider‐Brachert, W., Schütze, S., et al. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0405-8 · Cited by 51
Surface Calreticulin Mediates Muramyl Dipeptide-induced Apoptosis in RK13 Cells
Chen, D., Texada, D. E., Duggan, C., Liang, C., Reden, T. B., Kooragayala, L. M., & Langford, M. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413380200 · Cited by 51
RSK2 mediates NF‐κB activity through the phosphorylation of IκBα in the TNF‐R1 pathway
Peng, C., Cho, Y., Zhu, F., Xu, Y., Wen, W., Ma, W., Bode, A. M., & Dong, Z. (2010) · The FASEB Journal · doi:10.1096/fj.09-151290 · Cited by 51
TRADD interacts with STAT1-α and influences interferon-γ signaling
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Dailah, H. G. (2022) · Molecules · doi:10.3390/molecules27217207 · Cited by 51
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Wu, X., Sun, L., & Xu, F. (2023) · Pharmaceuticals · doi:10.3390/ph16060783 · Cited by 51
Schattenberg, J. M., & Schuchmann, M. (2009) · APOPTOSIS · doi:10.1007/s10495-009-0366-2 · Cited by 49
Palmitoylation of TNF alpha is involved in the regulation of TNF receptor 1 signalling
Poggi, M., Kara, I., Brunel, J. M., Landrier, J., Govers, R., Bonardo, B., Fluhrer, R., Haass, C., Alessi, M., & Peiretti, F. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.11.009 · Cited by 50
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Sun, M., Pang, J. S., Chen, S., Kuo, P., Chen, K., Kao, L.-Y., Wu, J.-Y., Lin, K., & Tsao, Y. (2007) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.07-0340 · Cited by 50
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Carafa, V., Nebbioso, A., Cuomo, F., Rotili, D., Cobellis, G., Bontempo, P., Baldi, A., Spugnini, E. P., Citro, G., Chambery, A., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-3081 · Cited by 51
Evidence of tumor necrosis factor receptor 1 signaling in human temporal lobe epilepsy.
Yamamoto, A., Schindler, C., Murphy, B., Bellver-Estellés, C., So, N., Taki, W., Meller, R., Simon, R., & Henshall, D. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.07.003 · Cited by 47
Machuy, N., Thiede, B., Rajalingam, K., Dimmler, C., Thieck, O., Meyer, T. F., & Rudel, T. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400089-mcp200 · Cited by 51
Zhang, S., Wu, L., Shi, W., Qin, J., Feng, W. J., Chen, Y., & Zhang, R. (2023) · Advanced Functional Materials · doi:10.1002/adfm.202302360 · Cited by 49
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RIP1 comes back to life as a cell death regulator in TNFR1 signaling
O’Donnell, M. A., & Ting, A. T. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08016.x · Cited by 47
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Endothelial cell myosin light chain kinase (MLCK) regulates TNF?-induced NF?B activity
Wadgaonkar, R., Linz-McGillem, L. A., Zaiman, A., & Garcia, J. G. N. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20250 · Cited by 49
Subcellular compartmentalization of TNF receptor-1 and CD95 signaling pathways
Tchikov, V., Bertsch, U., Fritsch, J. H., Edelmann, B., & Schütze, S. (2010) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.11.002 · Cited by 49
Siggers, R. H., & Hackam, D. J. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0821-4 · Cited by 51
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Liao, Y., Wang, H.-X., Mao, X., Wang, H., Wang, H., Li, Y., Sun, Y., Song, C., Tan, L., Ding, C., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.17970 · Cited by 49
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Seo, J., Kim, M. W., Bae, K., Lee, S. C., Song, J., & Lee, E. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.11.012 · Cited by 48
Necroptosis in inflammatory bowel disease and other intestinal diseases
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TNF receptor signalling in autoinflammatory diseases
Jarosz-Griffiths, H., Holbrook, J. A., Reyna, S. J. L., & McDermott, M. (2019) · International Immunology · doi:10.1093/intimm/dxz024 · Cited by 46
Mauro, C., Zazzeroni, F., Papa, S., Bubici, C., & Franzoso, G. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-530-9_10 · Cited by 49
Regulation of the release of damage-associated molecular patterns from necroptotic cells
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Zhang, L., Ding, Y., Yuan, Z., Liu, J., Sun, J., Lei, F., Wu, S., Li, S., & Zhang, D. (2015) · Oncotarget · doi:10.18632/oncotarget.2800 · Cited by 48
Parra, A., Martin-Fonseca, S., Rivas, F., Reyes‐Zurita, F. J., Medina‐O’Donnell, M., Martı́nez, A., García‐Granados, A., Lupiáñez, J. A., & Alberício, F. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.12.049 · Cited by 48
Inhibitor of Apoptosis Proteins: Fascinating Biology Leads to Attractive Tumor Therapeutic Targets
Varfolomeev, E. E., & Vucic, D. (2011) · Future Oncology · doi:10.2217/fon.11.40 · Cited by 49
Yang, J., McEachern, D., Li, W., Davis, M. A., Li, H., Morgan, M. A., Bai, L., Sebolt, J. T., Sun, H., Lawrence, T. S., et al. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-10-0643 · Cited by 48
Dong, Y., Dekens, D. W., Deyn, P. P. D., Naudé, P. J. W., & Eisel, U. L. M. (2015) · Antibodies · doi:10.3390/antib4040369 · Cited by 50
Chhibber‐Goel, J., Coleman-Vaughan, C., Agrawal, V., Sawhney, N., Hickey, E., Powell, J. C., & McCarthy, J. V. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.679076 · Cited by 47
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Metadata
- Authors
- Micheau, O., & Tschopp, J.
- Affiliations
- University of Lausanne (CH)
- Corresponding author
- Tschopp, Jürg
- ORCID
- Micheau, Olivier
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2003-07
- Volume
- 114
- Issue
- 2
- Pages
- 181-190
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2114727688
- Cited by
- 2,738
- References
- 40
- Citations by year
- 2026: 91 · 2025: 103 · 2024: 113 · 2023: 132 · 2022: 152 · 2021: 129 · 2020: 132 · 2019: 107 · 2018: 112 · 2017: 123 · 2016: 132 · 2015: 123 · 2014: 139 · 2013: 125 · 2012: 144
- FWCI
- 33.67
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3669 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 (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- IRIS (submittedVersion)
- SERVAL (Université de Lausanne) (submittedVersion)
- 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
- TNF receptor 1, apoptosis, TRADD, RIPK1, TRAF2, FADD, caspase-8, FLIP(L), NF-κB activation, cell survival, receptor signaling complex
- MeSH terms
- Carrier Proteins, Cell Membrane, Cell Survival, Cytoplasm, Humans, Models, Biological, Proteins, Tumor Cells, Cultured, Tumor Necrosis Factor-alpha, Signal Transduction, Transcriptional Activation, NF-kappa B, RNA-Binding Proteins, Apoptosis, Receptors, Tumor Necrosis Factor, fas Receptor, Jurkat Cells, Caspases, Nuclear Pore Complex Proteins, Intracellular Signaling Peptides and Proteins, TNF Receptor-Associated Factor 1, Adaptor Proteins, Signal Transducing, Caspase 8, Fas-Associated Death Domain Protein, CASP8 and FADD-Like Apoptosis Regulating Protein, Caspase 9, Caspase Inhibitors
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