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Fas triggers an alternative, caspase-8–independent cell death pathway using the kinase RIP as effector molecule
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TNF-Dependent Recruitment of the Protein Kinase RIP to the TNF Receptor-1 Signaling Complex
Hsu, H., Huang, J., Shu, H.-B., Baichwal, V., & Goeddel, D. V. (1996) · Immunity · doi:10.1016/s1074-7613(00)80252-6 · Cited by 1,182
Dual Signaling of the Fas Receptor: Initiation of Both Apoptotic and Necrotic Cell Death Pathways
Vercammen, D., Brouckaert, G., Denecker, G., Van de Craen, M., Declercq, W., Fiers, W., & Vandenabeele, P. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.5.919 · Cited by 556
Cited by
Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009
Kroemer, G., Galluzzi, L., Vandenabeele, P., Abrams, J., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., El-Deiry, W. S., Golstein, P., Green, D. R., et al. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2008.150 · Cited by 3,399
Self-citationChemical 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
Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
Micheau, O., & Tschopp, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00521-x · Cited by 2,738
Self-citationCho, 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
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382
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
Necroptosis and its role in inflammation
Pasparakis, M., & Vandenabeele, P. (2015) · Nature · doi:10.1038/nature14191 · Cited by 2,148
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
Crosstalk in NF-κB Signaling Pathways
Oeckinghaus, A., Hayden, M. S., & Ghosh, S. (2011) · Nature Immunology · doi:10.1038/ni.2065 · Cited by 1,942
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 Science of Stroke: Mechanisms in Search of Treatments
Moskowitz, M. A., Lo, E. H., & Iadecola, C. (2010) · Neuron · doi:10.1016/j.neuron.2010.07.002 · Cited by 1,930
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
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
Crosstalk between apoptosis.; necrosis and autophagy
Nikoletopoulou, V., Markaki, M., Palikaras, K., & Tavernarakis, N. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.001 · Cited by 1,366
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
“Cleaved caspase-8 was observed in whole lysates from these cells upon FLIP knockdown and TNF treatment, indicating that active caspase-8 was present in these cells, but was unable to prevent formation of the RIPK1-RIPK3 complex in the absence of FLIP (fig.”
InfluentialLinkermann, A., & Green, D. R. (2014) · New England Journal of Medicine · doi:10.1056/nejmra1310050 · Cited by 1,103
Pyroptosis versus necroptosis: similarities, differences, and crosstalk
Frank, D., & Vince, J. E. (2019) · Cell Death & Differentiation · doi:10.1038/s41418-018-0212-6 · Cited by 1,062
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
The development of the concept of ferroptosis
Hirschhorn, T., & Stockwell, B. R. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.043 · Cited by 1,052
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
Cell death by necrosis: towards a molecular definition
Golstein, P., & Kroemer, G. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.001 · Cited by 1,044
Autophagy and apoptosis dysfunction in neurodegenerative disorders
Ghavami, S., Shojaei, S., Yeganeh, B., Ande, S. R., Jangamreddy, J. R., Mehrpour, M., Christoffersson, J., Chaabane, W., Moghadam, A. R., Kashani, H. H., et al. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.10.004 · Cited by 1,039
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
Regulation of tumour necrosis factor signalling: live or let die
Brenner, D., Blaser, H., & Mak, T. W. (2015) · Nature Reviews Immunology · doi:10.1038/nri3834 · Cited by 998
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
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
The Fas Signaling Pathway: More Than a Paradigm
Wajant, H. (2002) · Science · doi:10.1126/science.1071553 · Cited by 957
Wang, Z., Jiang, H., Chen, S., Du, F., & Wang, X. (2012) · Cell · doi:10.1016/j.cell.2011.11.030 · Cited by 949
Toll-like Receptor 4 Is a Sensor for Autophagy Associated with Innate Immunity
Xu, Y., Jagannath, C., Liu, X.-D., Sharafkhaneh, A., Kolodziejska, K. E., & Eissa, N. T. (2007) · Immunity · doi:10.1016/j.immuni.2007.05.022 · Cited by 880
Tumor necrosis factor and cancer, buddies or foes?
Wang, X., & Lin, Y. (2008) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2008.00889.x · Cited by 730
Festjens, N., Vanden Berghe, T., & Vandenabeele, P. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.06.014 · Cited by 710
Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features
Berghe, T. V., Vanlangenakker, N., Parthoens, E., Deckers, W., Devos, M., Festjens, N., Guerin, C. J., Brunk, U. T., Declercq, W., & Vandenabeele, P. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.184 · Cited by 639
Roca, F. J., & Ramakrishnan, L. (2013) · Cell · doi:10.1016/j.cell.2013.03.022 · Cited by 592
TNF receptor subtype signalling: Differences and cellular consequences
MacEwan, D. J. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00262-5 · Cited by 610
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
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
Apoptosis and necroptosis in the liver: a matter of life and death
Schwabe, R. F., & Luedde, T. (2018) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-018-0065-y · Cited by 582
Necroptosis: A Specialized Pathway of Programmed Necrosis
Galluzzi, L., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2008.12.004 · Cited by 561
Exploring the TRAILs less travelled: TRAIL in cancer biology and therapy
von Karstedt, S., Montinaro, A., & Walczak, H. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2017.28 · Cited by 556
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
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
Wang, Y., & Kanneganti, T.-D. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.07.038 · Cited by 545
Activation of Necroptosis in Multiple Sclerosis
Ofengeim, D., Ito, Y., Najafov, A., Zhang, Y., Shan, B., DeWitt, J. P., Ye, J., Zhang, X., Chang, A., Vakifahmetoglu-Norberg, H., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.02.051 · Cited by 526
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
Sakon, S., Xue, X., Takekawa, M., Sasazuki, T., Okazaki, T., Kojima, Y., Piao, J., Yagita, H., Okumura, K., Doi, T., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg379 · Cited by 497
Caspase 8 inhibits programmed necrosis by processing CYLD
O’Donnell, M. A., Perez-Jimenez, E., Oberst, A., Ng, A., Massoumi, R., Xavier, R., Green, D. R., & Ting, A. T. (2011) · Nature Cell Biology · doi:10.1038/ncb2362 · Cited by 494
The Long Form of FLIP Is an Activator of Caspase-8 at the Fas Death-inducing Signaling Complex
Micheau, O., Thome, M., Schneider, P., Holler, N., Tschopp, J., Nicholson, D. W., Briand, C., & Grütter, M. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206882200 · Cited by 482
Self-citationThe Role of the Kinases RIP1 and RIP3 in TNF-Induced Necrosis
Vandenabeele, P., Declercq, W., Van Herreweghe, F., & Vanden Berghe, T. (2010) · Science Signaling · doi:10.1126/scisignal.3115re4 · Cited by 482
Apoptosis, necrosis and necroptosis: cell death regulation in the intestinal epithelium
Günther, C., Neumann, H., Neurath, M. F., & Becker, C. (2013) · Gut · doi:10.1136/gutjnl-2011-301364 · Cited by 462
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
Torti, S. V., Manz, D. H., Paul, B. T., Blanchette-Farra, N., & Torti, F. M. (2018) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-082117-051732 · Cited by 426
Caspase-8 Blocks Kinase RIPK3-Mediated Activation of the NLRP3 Inflammasome
Kang, T.-B., Yang, S.-H., Toth, B., Kovalenko, A., & Wallach, D. (2013) · Immunity · doi:10.1016/j.immuni.2012.09.015 · Cited by 419
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
Bubici, C., Papa, S., Dean, K., & Franzoso, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209936 · Cited by 399
Autophagy in acute kidney injury
Kaushal, G. P., & Shah, S. V. (2016) · Kidney International · doi:10.1016/j.kint.2015.11.021 · Cited by 389
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
Yoon, S., Kovalenko, A., Bogdanov, K., & Wallach, D. (2017) · Immunity · doi:10.1016/j.immuni.2017.06.001 · Cited by 368
Regulated necrosis in kidney ischemia-reperfusion injury
Pefanis, A., Ierino, F. L., Murphy, J. M., & Cowan, P. J. (2019) · Kidney International · doi:10.1016/j.kint.2019.02.009 · Cited by 361
TRAIL induces necroptosis involving RIPK1/RIPK3-dependent PARP-1 activation
Jouan-Lanhouet, S., Arshad, M. I., Piquet-Pellorce, C., Martin-Chouly, C., Le Moigne-Muller, G., Van Herreweghe, F., Takahashi, N., Sergent, O., Lagadic-Gossmann, D., Vandenabeele, P., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2012.90 · Cited by 357
Vanlangenakker, N., Vanden Berghe, T., Bogaert, P., Laukens, B., Zobel, K., Deshayes, K., Vucic, D., Fulda, S., Vandenabeele, P., & Bertrand, M. J. M. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.138 · Cited by 339
The AIM 2 inflammasome: Sensor of pathogens and cellular perturbations
Lugrin, J., & Martinon, F. (2018) · Immunological Reviews · doi:10.1111/imr.12618 · Cited by 333
Stat3 controls lysosomal-mediated cell death in vivo
Kreuzaler, P. A., Staniszewska, A. D., Li, W., Omidvar, N., Kedjouar, B., Turkson, J., Poli, V., Flavell, R. A., Clarkson, R. W. E., & Watson, C. J. (2011) · Nature Cell Biology · doi:10.1038/ncb2171 · Cited by 312
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
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
Fas ligand/Fas system in the brain: regulator of immune and apoptotic responses
Choi, C., & Benveniste, E. N. (2004) · Brain Research Reviews · doi:10.1016/j.brainresrev.2003.08.007 · Cited by 270
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
Heme induces programmed necrosis on macrophages through autocrine TNF and ROS production
Fortes, G. B., Alves, L. S., de Oliveira, R., Dutra, F. F., Rodrigues, D., Fernandez, P. L., Souto-Padron, T., De Rosa, M. J., Kelliher, M., Golenbock, D., et al. (2012) · Blood · doi:10.1182/blood-2011-08-375303 · Cited by 246
Alvarez-Diaz, S., Dillon, C. P., Lalaoui, N., Tanzer, M. C., Rodriguez, D. A., Lin, A., Lebois, M., Hakem, R., Josefsson, E. C., O’Reilly, L. A., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.07.016 · Cited by 242
Tumour Necrosis Factor Alpha in Intestinal Homeostasis and Gut Related Diseases
Ruder, B., Atreya, R., & Becker, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081887 · Cited by 228
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
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
Lee, E., Song, C.-H., Bae, S.-J., Ha, K.-T., & Karki, R. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01069-y · Cited by 164
Ppm1b negatively regulates necroptosis through dephosphorylating Rip3
Chen, W., Wu, J., Li, L., Zhang, Z., Ren, J., Liang, Y., Chen, F., Yang, C., Zhou, Z., Sean Su, S., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3120 · Cited by 161
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
An evolutionary perspective on the necroptotic pathway
Dondelinger, Y., Hulpiau, P., Saeys, Y., Bertrand, M. J. M., & Vandenabeele, P. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.06.004 · Cited by 159
Surviving apoptosis: life–death signaling in single cells
Flusberg, D. A., & Sorger, P. K. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.03.003 · Cited by 149
Strategies Used by Bacteria to Grow in Macrophages
Mitchell*, G., Chen*, C., & Portnoy, D. A. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.mchd-0012-2015 · Cited by 137
Hsp90 modulates the stability of MLKL and is required for TNF-induced necroptosis
Zhao, X. M., Chen, Z., Zhao, J. B., Zhang, P. P., Pu, Y. F., Jiang, S. H., Hou, J. J., Cui, Y. M., Jia, X. L., & Zhang, S. Q. (2016) · Cell Death & Disease · doi:10.1038/cddis.2015.390 · Cited by 135
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., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102779108 · Cited by 122
Control of neuronal branching by the death receptor CD95 (Fas/Apo-1)
Zuliani, C., Kleber, S., Klussmann, S., Wenger, T., Kenzelmann, M., Schreglmann, N., Martinez, A., del Rio, J. A., Soriano, E., Vodrazka, P., et al. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401720 · Cited by 117
The linear ubiquitin chain assembly complex regulates TRAIL‐induced gene activation and cell death
Lafont, E., Kantari‐Mimoun, C., Draber, P., De Miguel, D., Hartwig, T., Reichert, M., Kupka, S., Shimizu, Y., Taraborrelli, L., Spit, M., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201695699 · Cited by 114
Activation of cell-surface proteases promotes necroptosis, inflammation and cell migration
Cai, Z., Zhang, A., Choksi, S., Li, W., Li, T., Zhang, X.-M., & Liu, Z.-G. (2016) · Cell Research · doi:10.1038/cr.2016.87 · Cited by 103
Zou, J., Kawai, T., Tsuchida, T., Kozaki, T., Tanaka, H., Shin, K.-S., Kumar, H., & Akira, S. (2013) · Immunity · doi:10.1016/j.immuni.2012.12.007 · Cited by 103
Protein-based therapeutic approaches targeting death receptors
French, L. E., & Tschopp, J. (2003) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401185 · Cited by 102
Self-citation5-ALA-PDT induces RIP3-dependent necrosis in glioblastoma
Coupienne, I., Fettweis, G., Rubio, N., Agostinis, P., & Piette, J. (2011) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05213f · Cited by 91
Location, location, location: A compartmentalized view of TNF-induced necroptotic signaling.
Samson, A. L., Garnish, S. E., Hildebrand, J. M., & Murphy, J. M. (2021) · Science Signaling · doi:10.1126/scisignal.abc6178 · Cited by 82
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Yang, Z., Jiang, B., Wang, Y., Ni, H., Zhang, J., Xia, J., Shi, M., Hung, L.-M., Ruan, J., Mak, T. W., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.012 · Cited by 78
Badr, C. E., Wurdinger, T., Nilsson, J., Niers, J. M., Whalen, M., Degterev, A., & Tannous, B. A. (2011) · Neuro-Oncology · doi:10.1093/neuonc/nor067 · Cited by 62
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
Chen, Y., Huang, Y., Yang, S., Yen, H., Tsai, H., Hsieh, M., & Hsiao, Y. (2021) · Environmental Toxicology · doi:10.1002/tox.23146 · Cited by 26
Kamiya, M., Kimura, N., Umezawa, N., Hasegawa, H., & Yasuda, S. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1191815 · Cited by 21
Wang, Y., Liu, S., Chen, Y., Zhu, B., & Xing, Q. (2022) · World Journal of Oncology · doi:10.14740/wjon1446 · Cited by 17
Metadata
- Authors
- Holler, N., Zaru, R., Micheau, O., Thome, M., Attinger, A., Valitutti, S., Bodmer, J.-L., Schneider, P., Seed, B., & Tschopp, J.
- Venue
- Nature Immunology
- Published
- 2000-12
- Volume
- 1
- Issue
- 6
- Pages
- 489-495
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- OpenAlex
- W1523845694
- Cited by
- 1,938
- References
- 2
- FWCI
- 16.33
- Type
- journal article
- Language
- en
- Open access
- closed
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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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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
