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TNF-α Induces Two Distinct Caspase-8 Activation Pathways
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Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
Nuclear factor-κB in cancer development and progression
Karin, M. (2006) · Nature · doi:10.1038/nature04870 · Cited by 3,519
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
IAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis
Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218
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
Chang, L., Kamata, H., Solinas, G., Luo, J.-L., Maeda, S., Venuprasad, K., Liu, Y.-C., & Karin, M. (2006) · Cell · doi:10.1016/j.cell.2006.01.021 · Cited by 706
Ubiquitination of RIP Is Required for Tumor Necrosis Factor α-induced NF-κB Activation
Li, H., Kobayashi, M., Blonska, M., You, Y., & Lin, X. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600620200 · Cited by 277
Research works printed but not linked: 35
- Bignell, 2000, Identification of the familial cylindromatosis tumour-suppressor gene, Nat. Genet., 25, 160, 10.1038/76006 · DOI · Paper page
- Chai, 2000, Structural and biochemical basis of apoptotic activation by Smac/DIABLO, Nature, 406, 855, 10.1038/35022514 · DOI · Paper page
- Chen, 2002, TNF-R1 signaling: a beautiful pathway, Science, 296, 1634, 10.1126/science.1071924 · DOI · Paper page
- Chu, 1997, Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control, Proc. Natl. Acad. Sci. USA, 94, 10057, 10.1073/pnas.94.19.10057 · DOI · Paper page
- Conze, 2005, Posttranscriptional downregulation of c-IAP2 by the ubiquitin protein ligase c-IAP1 in vivo, Mol. Cell. Biol., 25, 3348, 10.1128/MCB.25.8.3348-3356.2005 · DOI
- Deng, 2003, A JNK-dependent pathway is required for TNFalpha-induced apoptosis, Cell, 115, 61, 10.1016/S0092-8674(03)00757-8 · DOI · Paper page
- Du, 2000, Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition, Cell, 102, 33, 10.1016/S0092-8674(00)00008-8 · DOI · Paper page
- Ea, 2006, Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO, Mol. Cell, 22, 245, 10.1016/j.molcel.2006.03.026 · DOI · Paper page
- Feldmann, 2003, Lasker Clinical Medical Research Award. TNF defined as a therapeutic target for rheumatoid arthritis and other autoimmune diseases, Nat. Med., 9, 1245, 10.1038/nm939 · DOI · Paper page
- Holler, 2000, Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule, Nat. Immunol., 1, 489, 10.1038/82732 · DOI · Paper page
- Irmler, 1997, Inhibition of death receptor signals by cellular FLIP, Nature, 388, 190, 10.1038/40657 · DOI · Paper page
- Jin, 2006, Distinct signaling pathways in TRAIL- versus tumor necrosis factor-induced apoptosis, Mol. Cell. Biol., 26, 8136, 10.1128/MCB.00257-06 · DOI
- Kelliher, 1998, The death domain kinase RIP mediates the TNF-induced NF-kappaB signal, Immunity, 8, 297, 10.1016/S1074-7613(00)80535-X · DOI · Paper page
- Kreuz, 2001, NF-kappaB inducers upregulate cFLIP, a cycloheximide-sensitive inhibitor of death receptor signaling, Mol. Cell. Biol., 21, 3964, 10.1128/MCB.21.12.3964-3973.2001 · DOI · Paper page
- Li, 2004, A small molecule Smac mimic potentiates TRAIL- and TNFalpha-mediated cell death, Science, 305, 1471, 10.1126/science.1098231 · DOI · Paper page
- Liu, 2000, Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain, Nature, 408, 1004, 10.1038/35050006 · DOI · Paper page
- Micheau, 2001, NF-kappaB signals induce the expression of c-FLIP, Mol. Cell. Biol., 21, 5299, 10.1128/MCB.21.16.5299-5305.2001 · DOI · Paper page
- Muppidi, 2004, Life and death decisions: secondary complexes and lipid rafts in TNF receptor family signal transduction, Immunity, 21, 461, 10.1016/j.immuni.2004.10.001 · DOI · Paper page
- O'Donnell, 2007, Ubiquitination of RIP1 regulates an NF-kappaB-independent cell-death switch in TNF signaling, Curr. Biol., 17, 418, 10.1016/j.cub.2007.01.027 · DOI · Paper page
- Panka, 2001, Phosphatidylinositol 3-kinase/Akt activity regulates c-FLIP expression in tumor cells, J. Biol. Chem., 276, 6893, 10.1074/jbc.C000569200 · DOI · Paper page
- Petersen, 2007, Autocrine TNFalpha Signaling Renders Human Cancer Cells Susceptible to Smac-Mimetic-Induced Apoptosis, Cancer Cell, 12, 445, 10.1016/j.ccr.2007.08.029 · DOI · Paper page
- Stanger, 1995, RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death, Cell, 81, 513, 10.1016/0092-8674(95)90072-1 · DOI · Paper page
- Tinel, 2004, The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress, Science, 304, 843, 10.1126/science.1095432 · DOI · Paper page
- Ting, 1996, RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis, EMBO J., 15, 6189, 10.1002/j.1460-2075.1996.tb01007.x · DOI · Paper page
- Varfolomeev, 2004, Tumor necrosis factor: an apoptosis JuNKie?, Cell, 116, 491, 10.1016/S0092-8674(04)00166-7 · DOI · Paper page
- Verhagen, 2000, Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins, Cell, 102, 43, 10.1016/S0092-8674(00)00009-X · DOI · Paper page
- Vince, 2007, IAP Antagonists Target cIAP1 to Induce TNFalpha-Dependent Apoptosis, Cell, 131, 682, 10.1016/j.cell.2007.10.037 · DOI · Paper page
- Wang, 1998, NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation, Science, 281, 1680, 10.1126/science.281.5383.1680 · DOI · Paper page
- Wright, 2007, Regulation of Early Wave of Germ Cell Apoptosis and Spermatogenesis by Deubiquitinating Enzyme CYLD, Dev. Cell, 13, 705, 10.1016/j.devcel.2007.09.007 · DOI
- Wu, 2006, Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation, Nat. Cell Biol., 8, 398, 10.1038/ncb1384 · DOI · Paper page
- Wu, 2000, Structural basis of IAP recognition by Smac/DIABLO, Nature, 408, 1008, 10.1038/35050012 · DOI · Paper page
- Yang, 2004, Smac/DIABLO selectively reduces the levels of c-IAP1 and c-IAP2 but not that of XIAP and livin in HeLa cells, J. Biol. Chem., 279, 16963, 10.1074/jbc.M401253200 · DOI
- Yang, 2000, Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli, Science, 288, 874, 10.1126/science.288.5467.874 · DOI · Paper page
- Zheng, 2006, Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1, Mol. Cell. Biol., 26, 3505, 10.1128/MCB.26.9.3505-3513.2006 · DOI
- Zou, 1999, An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9, J. Biol. Chem., 274, 11549, 10.1074/jbc.274.17.11549 · DOI · Paper page
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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
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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
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Oeckinghaus, A., Hayden, M. S., & Ghosh, S. (2011) · Nature Immunology · doi:10.1038/ni.2065 · Cited by 1,942
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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
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
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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
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Wang, Z., Jiang, H., Chen, S., Du, F., & Wang, X. (2012) · Cell · doi:10.1016/j.cell.2011.11.030 · Cited by 949
Self-citationTargeting IAP proteins for therapeutic intervention in cancer
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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
Self-citationRegulated 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
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Initiation and execution mechanisms of necroptosis: an overview
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Li, D., Xu, T., Cao, Y., Wang, H., Li, L., Chen, S., Wang, X., & Shen, Z. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1505244112 · Cited by 167
Self-citationPpm1b 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
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Buchheit, C. L., Rayavarapu, R. R., & Schafer, Z. T. (2012) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2012.04.007 · Cited by 115
Ghosh, S., Khazaei, M., Moien-Afshari, F., Ang, L. S., Granville, D. J., Verchere, C. B., Dunn, S. R., McCue, P., Mizisin, A., Sharma, K., et al. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90548.2008 · Cited by 113
Bellail, A. C., Olson, J. J., Yang, X., Chen, Z. J., & Hao, C. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-11-0172 · Cited by 113
Gentle, I. E., Wong, W. W.-L., Evans, J. M., Bankovacki, A., Cook, W. D., Khan, N. R., Nachbur, U., Rickard, J., Anderton, H., Moulin, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.216226 · Cited by 96
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Spit, M., Rieser, E., & Walczak, H. (2019) · Journal of Cell Science · doi:10.1242/jcs.208512 · Cited by 94
Chessari, G., Buck, I. M., Day, J. E. H., Day, P. J., Iqbal, A., Johnson, C. N., Lewis, E. J., Martins, V., Miller, D., Reader, M., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00706 · Cited by 90
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
Opportunities and challenges in combination gene cancer therapy
Nastiuk, K. L., & Krolewski, J. J. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.12.005 · Cited by 85
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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
The Tumor Suppressor Hace1 Is a Critical Regulator of TNFR1-Mediated Cell Fate
Tortola, L., Nitsch, R., Bertrand, M. J. M., Kogler, M., Redouane, Y., Kozieradzki, I., Uribesalgo, I., Fennell, L. M., Daugaard, M., Klug, H., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.032 · Cited by 64
Jinesh G., G., Chunduru, S., & Kamat, A. M. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.1211623 · Cited by 60
NF-κB and Extrinsic Cell Death Pathways – Entwined Do-or-Die Decisions for T cells
Blanchett, S., Boal-Carvalho, I., Layzell, S., & Seddon, B. (2021) · Trends in Immunology · doi:10.1016/j.it.2020.10.013 · Cited by 58
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
Huai, J., Vögtle, F.-N., Jöckel, L., Li, Y., Kiefer, T., Ricci, J.-E., & Borner, C. (2013) · Journal of Cell Science · doi:10.1242/jcs.129999 · Cited by 43
Diverse functions within the IAP family
Rumble, J. M., & Duckett, C. S. (2008) · Journal of Cell Science · doi:10.1242/jcs.040303 · Cited by 40
Zeng, F., Wen, W., Cui, W., Zheng, W., Liu, Y., Sun, X., Hou, N., Ma, D., Yuan, Y., Shi, H., et al. (2018) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2018.10.015 · Cited by 16
TRADD mediates the tumor necrosis factor-induced apoptosis of L929 cells in the absence of RIP3
Chang, X., Wang, L., Wang, Z., Wu, S., Zhu, X., Hu, S., Wang, Y., Yu, J., & Chen, G. (2017) · Scientific Reports · doi:10.1038/s41598-017-16390-6 · Cited by 13
Self-citation
Metadata
- Authors
- Wang, L., Du, F., & Wang, X.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2008-05
- Volume
- 133
- Issue
- 4
- Pages
- 693-703
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1998423564
- Cited by
- 1,351
- References
- 7
- FWCI
- 26.30
- Type
- journal article
- Language
- en
- Open access
- bronze
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1939 d)
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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.