Cited by 571Cell death mechanisms and regulationNF-κB Signaling PathwaysImmune Response and Inflammation

The DOI matches its Crossref record; 152 of the 152 references it cites were found in a registry or an index.

Initiation and execution mechanisms of necroptosis: an overview

Open access

Grootjans, Sasker, Vanden Berghe, Tom, Vandenabeele, Peter·2017·Cell Death & Differentiation

DOI 10.1038/cdd.2017.65PMC PMC5520172

Open this paper in CoChat — free account Open PDF

Abstract

Necroptosis is a form of regulated cell death, which is induced by ligand binding to TNF family death domain receptors, pattern recognizing receptors and virus sensors. The common feature of these receptor systems is the implication of proteins, which contain a receptor interaction protein kinase (RIPK) homology interaction motif (RHIM) mediating recruitment and activation of receptor-interacting protein kinase 3 (RIPK3), which ultimately activates the necroptosis executioner mixed lineage kinase domain-like (MLKL). In case of the TNF family members, the initiator is the survival- and cell death-regulating RIPK1 kinase, in the case of Toll-like receptor 3/4 (TLR3/4), a RHIM-containing adaptor, called TRIF, while in the case of Z-DNA-binding protein ZBP1/DAI, the cytosolic viral sensor itself contains a RHIM domain. In this review, we discuss the different protein complexes that serve as nucleation platforms for necroptosis and the mechanism of execution of necroptosis. Transgenic models (knockout, kinase-dead knock-in) and pharmacologic inhibition indicate that RIPK1, RIPK3 or MLKL are implicated in many inflammatory, degenerative and infectious diseases. However, the conclusion of necroptosis being solely involved in the etiology of diseases is blurred by the pleiotropic roles of RIPK1 and RIPK3 in other cellular processes such as apoptosis and inflammasome activation.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1038/cdd.2017.65

Cites

152 of 152 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Hallmarks of Cancer: The Next Generation
Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590
Ferroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death
Dixon, S. J., Lemberg, K. M., Lamprecht, M. R., Skouta, R., Zaitsev, E. M., Gleason, C. E., Patel, D. N., Bauer, A. J., Cantley, A. M., Yang, W. S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.042 · Cited by 18,691
Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics
Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,673
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167
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
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
Mixed Lineage Kinase Domain-like Protein Mediates Necrosis Signaling Downstream of RIP3 Kinase
Sun, L., Wang, H., Wang, Z., He, S., Chen, S., Liao, D., Wang, L., Yan, J., Liu, W., Lei, X., et al. (2012) · Cell · doi:10.1016/j.cell.2011.11.031 · Cited by 2,698
Gasdermin D is an executor of pyroptosis and required for interleukin-1β secretion
He, W.-T., Wan, H., Hu, L., Chen, P., Wang, X., Huang, Z., Yang, Z.-H., Zhong, C.-Q., & Han, J. (2015) · Cell Research · doi:10.1038/cr.2015.139 · Cited by 2,517
Phosphorylation-Driven Assembly of the RIP1-RIP3 Complex Regulates Programmed Necrosis and Virus-Induced Inflammation
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
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
Self-citation
Involvement of MACH, a Novel MORT1/FADD-Interacting Protease, in Fas/APO-1- and TNF Receptor–Induced Cell Death
Boldin, M. P., Goncharov, T. M., Goltseve, Y. V., & Wallach, D. (1996) · Cell · doi:10.1016/s0092-8674(00)81265-9 · Cited by 2,292
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
Self-citation
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
TRADD–TRAF2 and TRADD–FADD Interactions Define Two Distinct TNF Receptor 1 Signal Transduction Pathways
Hsu, H., Shu, H., Pan, M., & Goeddel, D. V. (1996) · Cell · doi:10.1016/s0092-8674(00)80984-8 · Cited by 1,998
Fas triggers an alternative, caspase-8–independent cell death pathway using the kinase RIP as effector molecule
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
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
Self-citation
Mixed Lineage Kinase Domain-like Protein MLKL Causes Necrotic Membrane Disruption upon Phosphorylation by RIP3
Wang, H., Sun, L., Su, L., Rizo, J., Liu, L., Wang, L., Wang, F., & Wang, X. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.003 · Cited by 1,606
Cell Death in Development
Vaux, D. L., & Korsmeyer, S. J. (1999) · Cell · doi:10.1016/s0092-8674(00)80564-4 · Cited by 1,564
Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death
Rogers, C., Fernandes-Alnemri, T., Mayes, L., Alnemri, D., Cingolani, G., & Alnemri, E. S. (2017) · Nature Communications · doi:10.1038/ncomms14128 · Cited by 1,510 · cited 1×
“In this case, proteolytic cleavage of deafness-associated tumor supressor (DFNA5) by caspase-3 triggers secondary necrosis.(24) Figure 1 gives an overview of different types of regulated cell death, and of the core pathways involved in the initiation and execution of cell death.”
Background
TNF-α Induces Two Distinct Caspase-8 Activation Pathways
Wang, L., Du, F., & Wang, X. (2008) · Cell · doi:10.1016/j.cell.2008.03.036 · Cited by 1,398
Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis
Cai, Z., Jitkaew, S., Zhao, J., Chiang, H.-C., Choksi, S., Liu, J., Ward, Y., Wu, L.-G., & Liu, Z.-G. (2014) · Nature Cell Biology · doi:10.1038/ncb2883 · Cited by 1,322
The RIP1/RIP3 Necrosome Forms a Functional Amyloid Signaling Complex Required for Programmed Necrosis
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
The Pseudokinase MLKL Mediates Necroptosis via a Molecular Switch Mechanism
Murphy, J. M., Czabotar, P. E., Hildebrand, J. M., Lucet, I. S., Zhang, J.-G., Alvarez-Diaz, S., Lewis, R., Lalaoui, N., Metcalf, D., Webb, A. I., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.06.018 · Cited by 1,220
CELL DEATHS IN NORMAL VERTEBRATE ONTOGENY
Glucksmann, A. (1951) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/j.1469-185x.1951.tb00774.x · Cited by 1,208
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
Self-citation
Identification of a Molecular Signaling Network that Regulates a Cellular Necrotic Cell Death Pathway
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
Inhibition of Caspases Increases the Sensitivity of L929 Cells to Necrosis Mediated by Tumor Necrosis Factor
Vercammen, D., Beyaert, R., Denecker, G., Goossens, V., Loo, G., Declercq, W., Grooten, J., Fiers, W., & Vandenabeele, P. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.9.1477 · Cited by 925
Self-citation
Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis
Zhao, J., Jitkaew, S., Cai, Z., Choksi, S., Li, Q., Luo, J., & Liu, Z.-G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200012109 · Cited by 925
Tumor necrosis factor can induce both apoptic and necrotic forms of cell lysis.
Laster, S. M., Wood, J. G., & Gooding, L. R. (1988) · The Journal of Immunology · doi:10.4049/jimmunol.141.8.2629 · Cited by 909
Apaf1 (CED-4 Homolog) Regulates Programmed Cell Death in Mammalian Development
Cecconi, F., Álvarez-Bolado, G., Meyer, B. I., Roth, K. A., & Gruß, P. (1998) · Cell · doi:10.1016/s0092-8674(00)81732-8 · Cited by 894
cIAPs Block Ripoptosome Formation, a RIP1/Caspase-8 Containing Intracellular Cell Death Complex Differentially Regulated by cFLIP Isoforms
Feoktistova, 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 878
MLKL Compromises Plasma Membrane Integrity by Binding to Phosphatidylinositol Phosphates
Dondelinger, Y., Declercq, W., Montessuit, S., Roelandt, R., Gonçalves, A. C., Bruggeman, I., Hulpiau, P., Weber, K., Sehon, C. A., Marquis, R. W., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.026 · Cited by 840
Self-citation
The Ripoptosome, a Signaling Platform that Assembles in Response to Genotoxic Stress and Loss of IAPs
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 837
Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death
Chen, X., Li, W., Ren, J., Huang, D., He, W., Song, Y., Yang, C., Li, W., Zheng, X., Chen, P., et al. (2013) · Cell Research · doi:10.1038/cr.2013.171 · Cited by 803
CaMKII is a RIP3 substrate mediating ischemia- and oxidative stress–induced myocardial necroptosis
Zhang, T., Zhang, Y., Cui, M., Jin, L., Wang, Y., Lv, F., Liu, Y., Zheng, W., Shang, H., Zhang, J., et al. (2016) · Nature Medicine · doi:10.1038/nm.4017 · Cited by 790
DAI/ZBP1/DLM-1 Complexes with RIP3 to Mediate Virus-Induced Programmed Necrosis that Is Targeted by Murine Cytomegalovirus vIRA
Upton, J. W., Kaiser, W. J., & Mocarski, E. S. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.01.016 · Cited by 758
Toll-like receptors activate programmed necrosis in macrophages through a receptor-interacting kinase-3–mediated pathway
He, S., Liang, Y., Shao, F., & Wang, X. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116302108 · Cited by 751
The morphology of various types of cell death in prenatal tissues
Schweichel, J. ‐., & Merker, H. ‐. (1973) · Teratology · doi:10.1002/tera.1420070306 · Cited by 738
Converging roles of caspases in inflammasome activation, cell death and innate immunity
Man, S. M., & Kanneganti, T. (2015) · Nature reviews. Immunology · doi:10.1038/nri.2015.7 · Cited by 717
Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations
Melo, M. N., Ferré, R., & Castanho, M. A. R. B. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2095 · Cited by 711
Apoptosis and necrosis: Detection, discrimination and phagocytosis
Krysko, D. V., Berghe, T. V., D'Herde, K. G. M. A., & Vandenabeele, P. (2008) · Methods · doi:10.1016/j.ymeth.2007.12.001 · Cited by 707
Self-citation
Activity of Protein Kinase RIPK3 Determines Whether Cells Die by Necroptosis or Apoptosis
Newton, K., Dugger, D. L., Wickliffe, K. E., Kapoor, N., de Almagro, M. C., Vucic, D., Komuves, L., Ferrando, R. E., French, D. M., Webster, J., et al. (2014) · Science · doi:10.1126/science.1249361 · Cited by 687
RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL
Lawlor, K. E., Khan, N. R., Mildenhall, A., Gerlic, M., Croker, B. A., D’Cruz, A. A., Hall, C. M., Spall, S. K., Anderton, H., Masters, S. L., et al. (2015) · Nature Communications · doi:10.1038/ncomms7282 · Cited by 660
RIPK1 and NF-κB signaling in dying cells determines cross-priming of CD8 + T cells
Yatim, N., Jusforgues-Saklani, H., Orozco, S. L., Schulz, O., da Silva, R. B., Sousa, C. R. E., Green, D. R., Oberst, A., & Albert, M. L. (2015) · Science · doi:10.1126/science.aad0395 · Cited by 643
Mitophagy-dependent necroptosis contributes to the pathogenesis of COPD
Mizumura, K., Cloonan, S. M., Nakahira, K., Bhashyam, A. R., Cervo, M., Kitada, T., Glass, K., Owen, C. A., Mahmood, A., Washko, G. R., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci74985 · Cited by 611
RIP Kinase-Dependent Necrosis Drives Lethal Systemic Inflammatory Response Syndrome
Duprez, L., Takahashi, N., Hauwermeiren, F. V., Vandendriessche, B., Goossens, V., Berghe, T. V., Declercq, W., Libert, C., Cauwels, A., & Vandenabeele, P. (2011) · Immunity · doi:10.1016/j.immuni.2011.09.020 · Cited by 607
Self-citation
Activation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell death
Hildebrand, J. M., Tanzer, M. C., Lucet, I. S., Young, S. N., Spall, S. K., Sharma, P., Pierotti, C., Garnier, J.-M., Dobson, R. C. J., Webb, A. I., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408987111 · Cited by 598
Two independent pathways of regulated necrosis mediate ischemia–reperfusion injury
Linkermann, A., Bräsen, J. H., Darding, M., Jin, M. K., Sanz, A. B., Heller, J.-O., Zen, F. D., Weinlich, R., Ortíz, A., Walczak, H., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305538110 · Cited by 575
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
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
Self-citation
Kinase RIP3 Is Dispensable for Normal NF-κBs, Signaling by the B-Cell and T-Cell Receptors, Tumor Necrosis Factor Receptor 1, and Toll-Like Receptors 2 and 4
Newton, K., Sun, X., & Dixit, V. M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.4.1464-1469.2004 · Cited by 554
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
Methylation-dependent loss of RIP3 expression in cancer represses programmed necrosis in response to chemotherapeutics
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
Active MLKL triggers the NLRP3 inflammasome in a cell-intrinsic manner
Conos, S. A., Chen, K. W., De Nardo, D., Hara, H., Whitehead, L., Núñez, G., Masters, S. L., Murphy, J. M., Schroder, K., Vaux, D. L., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613305114 · Cited by 485
RIP1, a kinase on the crossroads of a cell's decision to live or die
Festjens, N., Berghe, T. V., Cornelis, S., & Vandenabeele, P. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402085 · Cited by 467
Self-citation
Necrostatin-1 analogues: critical issues on the specificity, activity and in vivo use in experimental disease models
Takahashi, N., Duprez, L., Grootjans, S., Cauwels, A., Nerinckx, W., DuHadaway, J. B., Goossens, V, Roelandt, R., Van Hauwermeiren, F., Libert, C., et al. (2012) · Cell Death & Disease · doi:10.1038/cddis.2012.176 · Cited by 465
Self-citation
Rip1 (Receptor-interacting protein kinase 1) mediates necroptosis and contributes to renal ischemia/reperfusion injury
Linkermann, A., Bräsen, J. H., Himmerkus, N., Liu, S., Huber, T. B., Kunzendorf, U., & Krautwald, S. (2012) · Kidney International · doi:10.1038/ki.2011.450 · Cited by 462
Mlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosis
Wu, J., Huang, Z., Ren, J., Zhang, Z., He, P., Li, Y., Ma, J., Chen, W., Zhang, Y., Zhou, X., et al. (2013) · Cell Research · doi:10.1038/cr.2013.91 · Cited by 462
Parthanatos, a messenger of death
David, K. K. (2009) · Frontiers in Bioscience · doi:10.2741/3297 · Cited by 450
RIPK3 deficiency or catalytically inactive RIPK1 provides greater benefit than MLKL deficiency in mouse models of inflammation and tissue injury
Newton, K., Dugger, D. L., Maltzman, A., Greve, J. M., Hedehus, M., Martin-McNulty, B., Carano, R. A. D., Cao, T. C., van Bruggen, N., Bernstein, L., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.46 · Cited by 447
NF-κB-Independent Role of IKKα/IKKβ in Preventing RIPK1 Kinase-Dependent Apoptotic and Necroptotic Cell Death during TNF Signaling
Dondelinger, Y., Jouan-Lanhouet, S., Divert, T., Theatre, E., Bertin, J., Gough, P. J., Giansanti, P., Heck, A. J. R., Dejardin, E., Vandenabeele, P., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.032 · Cited by 431
Self-citation
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
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
Apoptosis Induced by the Toll-Like Receptor Adaptor TRIF Is Dependent on Its Receptor Interacting Protein Homotypic Interaction Motif
Kaiser, W. J., & Offermann, M. K. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.8.4942 · Cited by 378
Cutting Edge: RIP1 Kinase Activity Is Dispensable for Normal Development but Is a Key Regulator of Inflammation in SHARPIN-Deficient Mice
Berger, S. B., Kasparcova, V., Hoffman, S., Swift, B., Dare, L., Schaeffer, M., Capriotti, C., Cook, M., Finger, J., Hughes-Earle, A., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400499 · Cited by 374
Identification of a Novel Homotypic Interaction Motif Required for the Phosphorylation of Receptor-interacting Protein (RIP) by RIP3
Sun, X., Yin, J., Starovasnik, M. A., Fairbrother, W. J., & Dixit, V. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109488200 · Cited by 371
Shikonin circumvents cancer drug resistance by induction of a necroptotic death
Han, W., Li, L., Qiu, S., Lu, Q., Pan, Q., Gu, Y., Luo, J., & Hu, X. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0511 · Cited by 365
DAI/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
Requirement for RNA and protein synthesis for induced regression of the tadpole tail in organ culture
Tata, J. R. (1966) · Developmental Biology · doi:10.1016/0012-1606(66)90050-9 · Cited by 363
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
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
Self-citation
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
What is apoptosis, and why is it important? Education and debate
Renehan, A. G., Booth, C. E., & Potten, C. S. (2001) · BMJ · doi:10.1136/bmj.322.7301.1536 · Cited by 337
Unconventional Roles of the NADPH Oxidase: Signaling, Ion Homeostasis, and Cell Death
Steinberg, B. E., & Grinstein, S. (2007) · Science s STKE · doi:10.1126/stke.3792007pe11 · Cited by 331
Inhibition of RIP1-dependent necrosis prevents adverse cardiac remodeling after myocardial ischemia–reperfusion in vivo
Oerlemans, M. I. F. J., Liu, J., Arslan, F., den Ouden, K., van Middelaar, B. J., Doevendans, P. A., & Sluijter, J. P. G. (2012) · Basic Research in Cardiology · doi:10.1007/s00395-012-0270-8 · Cited by 331
Cutting Edge: RIPK1 Kinase Inactive Mice Are Viable and Protected from TNF-Induced Necroptosis In Vivo
Polykratis, A., Hermance, N. M., Zelic, M., Roderick, J. E., KIM, C. S., Van, T.-M., Lee, T. H., Chan, F. K.-M., Pasparakis, M., & Kelliher, M. A. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400590 · Cited by 330
Necrostatin: A Potentially Novel Cardioprotective Agent?
Smith, C., Davidson, S. M., Lim, S. Y., Simpkin, J. C., Hothersall, J. S., & Yellon, D. M. (2007) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-007-6035-1 · Cited by 327
Interdigital cell death can occur through a necrotic and caspase-independent pathway
Chautan, M., Chazal, G., Cecconi, F., Gruß, P., & Golstein, P. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80425-4 · Cited by 325
RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition
Dondelinger, Y., Aguileta, M. A., Goossens, V, Dubuisson, C., Grootjans, S., Dejardin, E., Vandenabeele, P., & Bertrand, M. J. M. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.94 · Cited by 312
Self-citation
Cell death of motoneurons in the chick embryo spinal cord. I. A light and electron microscopic study of naturally occurring and induced cell loss during development
Chu‐Wang, I., & Oppenheim, R. W. (1978) · The Journal of Comparative Neurology · doi:10.1002/cne.901770105 · Cited by 311
Absence of receptor interacting protein kinase 3 prevents ethanol-induced liver injury
Roychowdhury, S., McMullen, M. R., Pisano, S. G., Liu, X., & Nagy, L. E. (2013) · Hepatology · doi:10.1002/hep.26200 · Cited by 304
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
RIPK1 both positively and negatively regulates RIPK3 oligomerization and necroptosis
Orozco, S., Yatim, N., Werner, M. R., Tran, H., Gunja, S. Y., Tait, S. W., Albert, M. L., Green, D. R., & Oberst, A. (2014) · Cell Death & Differentiation · doi:10.1038/cdd.2014.76 · Cited by 294
Diverse Sequence Determinants Control Human and Mouse Receptor Interacting Protein 3 (RIP3) and Mixed Lineage Kinase domain-Like (MLKL) Interaction in Necroptotic Signaling
Chen, W., Zhou, Z., Li, L., Zhong, C., Zheng, X., Wu, X., Zhang, Y., Ma, H., Huang, D., Li, W., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.435545 · Cited by 272
Ultrastructural differences during embryonic cell death in normal and peripherally deprived ciliary ganglia.
Pilar, G., & Landmesser, L. T. (1976) · The Journal of Cell Biology · doi:10.1083/jcb.68.2.339 · Cited by 266
Caspase-8 scaffolding function and MLKL regulate NLRP3 inflammasome activation downstream of TLR3
Kang, S., Fernandes‐Alnemri, T., Rogers, C., Mayes, L., Wang, Y., Dillon, C. P., Roback, L., Kaiser, W. J., Oberst, A., Sagara, J., et al. (2015) · Nature Communications · doi:10.1038/ncomms8515 · Cited by 263
NEMO and RIP1 Control Cell Fate in Response to Extensive DNA Damage via TNF-α Feedforward Signaling
Biton, S., & Ashkenazi, A. (2011) · Cell · doi:10.1016/j.cell.2011.02.023 · Cited by 262
The Necroptosis Adaptor RIPK3 Promotes Injury-Induced Cytokine Expression and Tissue Repair
Moriwaki, K., Balaji, S., McQuade, T. J., Malhotra, N., Kang, J., & Chan, F. K.-M. (2014) · Immunity · doi:10.1016/j.immuni.2014.09.016 · Cited by 260
Receptor interacting protein kinase 3 is a critical early mediator of acetaminophen-induced hepatocyte necrosis in mice
Ramachandran, A., McGill, M. R., Xie, Y., Ni, H., Ding, W., & Jaeschke, H. (2013) · Hepatology · doi:10.1002/hep.26547 · Cited by 258
Intracellular regulation of TNF activity in health and disease
Varfolomeev, E. E., & Vucic, D. (2016) · Cytokine · doi:10.1016/j.cyto.2016.08.035 · Cited by 257
Differential roles of RIPK1 and RIPK3 in TNF-induced necroptosis and chemotherapeutic agent-induced cell death
Moriwaki, K., Bertin, J., Gough, P. J., Orlowski, G. M., & Chan, F. K. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.16 · Cited by 251
Sequential Engagement of Distinct MLKL Phosphatidylinositol-Binding Sites Executes Necroptosis
Quarato, G., Guy, C. S., Grace, C. R., Llambi, F., Nourse, A., Rodríguez, D. A., Wakefield, R., Frase, S., Moldoveanu, T., & Green, D. R. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.01.011 · Cited by 244
Toward an understanding of the protein interaction network of the human liver
Wang, J., Huo, K., Ma, L., Tang, L., Li, D., Huang, X., Yuan, Y., Li, C., Wang, W., Guan, W., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.67 · Cited by 243
MLKL Activation Triggers NLRP3-Mediated Processing and Release of IL-1β Independently of Gasdermin-D
Gutierrez, K. D., Davis, M. A., Daniels, B. P., Olsen, T. M., Ralli-Jain, P., Tait, S. W. G., Gale, M., & Oberst, A. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1601757 · Cited by 237
Necroptosis Is Active in Children With Inflammatory Bowel Disease and Contributes to Heighten Intestinal Inflammation
Pierdomenico, M., Negroni, A., Stronati, L., Vitali, R., Prete, E., Bertin, J., Gough, P. J., Aloi, M., & Cucchiara, S. (2013) · The American Journal of Gastroenterology · doi:10.1038/ajg.2013.403 · Cited by 223
Programmed Cell Death of Developing Mammalian Neurons after Genetic Deletion of Caspases
Oppenheim, R. W., Flavell, R. A., Vinsant, S. L., Prevette, D. M., Kuan, C.-Y., & RAKIC, P. T. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-13-04752.2001 · Cited by 216
Obatoclax (GX15-070) triggers necroptosis by promoting the assembly of the necrosome on autophagosomal membranes
Basit, F., Cristofanon, S., & Fulda, S. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.45 · Cited by 211
A novel role for RIP1 kinase in mediating TNFα production
Christofferson, D. E., Li, Y., Hitomi, J., Zhou, W., Upperman, C., Zhu, H., Gerber, S. A., Gygi, S. P., & Yuan, J. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.64 · Cited by 207
RIG-I RNA Helicase Activation of IRF3 Transcription Factor Is Negatively Regulated by Caspase-8-Mediated Cleavage of the RIP1 Protein
Rajput, A., Kovalenko, A., Bogdanov, K., Yang, S., Kang, T., Kim, J., Du, J., & Wallach, D. (2011) · Immunity · doi:10.1016/j.immuni.2010.12.018 · Cited by 203
Cytomegalovirus M45 Cell Death Suppression Requires Receptor-interacting Protein (RIP) Homotypic Interaction Motif (RHIM)-dependent Interaction with RIP1
Upton, J. W., Kaiser, W. J., & Mocarski, E. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c800051200 · Cited by 202
MLKL forms cation channels
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
Programmed necrosis, not apoptosis, is a key mediator of cell loss and DAMP-mediated inflammation in dsRNA-induced retinal degeneration
Murakami, Y., Matsumoto, H., Roh, M., Giani, A., Kataoka, K., Morizane, Y., Kayama, M., Thanos, A., Nakatake, S., Notomi, S., et al. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.109 · Cited by 199
Structural Insights into RIP3-Mediated Necroptotic Signaling
Xie, T., Peng, W., Yan, C., Wu, J., Gong, X., & Shi, Y. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.044 · Cited by 196
Type-I interferon signaling through ISGF3 complex is required for sustained Rip3 activation and necroptosis in macrophages
McComb, S., Cessford, E., Alturki, N. A., Joseph, J., Shutinoski, B., Startek, J. B., Gamero, A. M., Mossman, K. L., & Sad, S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1407068111 · Cited by 190
EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation
Pearson, J. S., Giogha, C., Mühlen, S., Nachbur, U., Pham, C. L. L., Zhang, Y., Hildebrand, J. M., Oates, C. V. L., Lung, T. W. F., Ingle, D. J., et al. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.258 · Cited by 183
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
Ca2+/Calmodulin-dependent Protein Kinase II (CaMKII) Regulates Cardiac Sodium Channel NaV1.5 Gating by Multiple Phosphorylation Sites
Ashpole, N. M., Herren, A. W., Ginsburg, K. S., Brogan, J. D., Johnson, D. E., Cummins, T., Bers, D. M., & Hudmon, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322537 · Cited by 173
Absence of RIPK3 predicts necroptosis resistance in malignant melanoma
Geserick, P., Wang, J., Schilling, R., Horn, S., Harris, P. A., Bertin, J., Gough, P. J., Feoktistova, M., & Leverkus, M. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.240 · Cited by 172
Necroptosis, in vivo detection in experimental disease models
Jouan-Lanhouet, S., Riquet, F. B., Duprez, L., Berghe, T. V., Takahashi, N., & Vandenabeele, P. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.08.010 · Cited by 166
Self-citation
Necrostatin-1 blocks both RIPK1 and IDO: consequences for the study of cell death in experimental disease models
Vandenabeele, P., Grootjans, S., Callewaert, N., & Takahashi, N. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.151 · Cited by 166
Self-citation
Genetic variation in 1253 immune and inflammation genes and risk of non-Hodgkin lymphoma
Cerhan, J. R., Ansell, S. M., Fredericksen, Z. S., Kay, N. E., Liebow, M., Call, T. G., Doǧan, A., Cunningham, J. M., Wang, A. H., Liu‐Mares, W., et al. (2007) · Blood · doi:10.1182/blood-2007-05-088682 · Cited by 162
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
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
Self-citation
The pseudokinase MLKL mediates programmed hepatocellular necrosis independently of RIPK3 during hepatitis
Günther, C., He, G.-W., Kremer, A. E., Murphy, J. M., Petrie, E. J., Amann, K., Vandenabeele, P., Linkermann, A., Poremba, C., Schleicher, U., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci87545 · Cited by 157
Self-citation
Competitive Control of Independent Programs of Tumor Necrosis Factor Receptor-Induced Cell Death by TRADD and RIP1
Zheng, L., Bidère, N., Staudt, D., Cubre, A., Orenstein, J. M., Chan, F. K.-M., & Lenardo, M. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.9.3505-3513.2006 · Cited by 155
Necroptosis is preceded by nuclear translocation of the signaling proteins that induce it
Yoon, S., Bogdanov, K., Kovalenko, A., & Wallach, D. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.92 · Cited by 151
Endoplasmic reticulum stress induces ligand-independent TNFR1-mediated necroptosis in L929 cells
Saveljeva, S., Laughlin, S. L. M., Vandenabeele, P., Samali, A., & Bertrand, M. J. M. (2015) · Cell Death and Disease · doi:10.1038/cddis.2014.548 · Cited by 150
Self-citation
Antigen-mediated T cell expansion regulated by parallel pathways of death
Ch’en, I. L., Beisner, D. R., Degterev, A., Lynch, C., Yuan, J., Hoffmann, A., & Hedrick, S. Μ. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808043105 · Cited by 140
RIP3 is downregulated in human myeloid leukemia cells and modulates apoptosis and caspase-mediated p65/RelA cleavage
Nugues, A.-L., Bouazzati, H. E., Hétuin, D., Berthon, C., Loyens, A., Bertrand, E., Jouy, N., Idziorek, T., & Quesnel, B. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.347 · Cited by 140
Dichotomy between RIP1- and RIP3-Mediated Necroptosis in Tumor Necrosis Factor-α-Induced Shock
Linkermann, A., Bräsen, J. H., Zen, F. D., Weinlich, R., Schwendener, R. A., Green, D. R., Kunzendorf, U., & Krautwald, S. (2012) · Molecular Medicine · doi:10.2119/molmed.2011.00423 · Cited by 138
The MLKL Channel in Necroptosis Is an Octamer Formed by Tetramers in a Dyadic Process
Huang, D., Zheng, X., Wang, Z.-A., Chen, X., He, W., Zhang, Y., Xu, J.-G., Zhao, H., Shi, W., Wang, X., et al. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00497-16 · Cited by 138
Ca V 1.2 β-subunit coordinates CaMKII-triggered cardiomyocyte death and afterdepolarizations
Koval, O. M., Guan, X., Wu, Y., Joiner, M.-L. A., Gao, Z., Chen, B., Grumbach, I. M., Luczak, E. D., Colbran, R. J., Song, L., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913760107 · Cited by 138
NF-κB Protects Cells from Gamma Interferon-Induced RIP1-Dependent Necroptosis
Thapa, R. J., Basagoudanavar, S. H., Nogusa, S., Irrinki, K. M., Mallilankaraman, K. B., Slifker, M. J., Beg, A. A., Madesh, M., & Balachandran, S. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05445-11 · Cited by 136
Necroptosis suppresses inflammation via termination of TNF- or LPS-induced cytokine and chemokine production
Kearney, C. J., Cullen, S. P., Tynan, G. A., Henry, C. M., Clancy, D. M., Lavelle, E. C., & Martin, S. J. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2014.222 · Cited by 135
Pronecrotic mixed lineage kinase domain‐like protein expression is a prognostic biomarker in patients with early‐stage resected pancreatic adenocarcinoma
Colbert, L. E., Fisher, S. B., Hardy, C. W., Hall, W. A., Saka, B., Shelton, J. W., Petrova, A. V., Warren, M. D., Pantazides, B. G., Gandhi, K., et al. (2013) · Cancer · doi:10.1002/cncr.28144 · Cited by 131
Positive and negative phosphorylation regulates RIP1- and RIP3-induced programmed necrosis
McQuade, T. J., Cho, Y., & Chan, F. K.-M. (2013) · Biochemical Journal · doi:10.1042/bj20130860 · Cited by 129
Mutations That Affect Neural Cell Lineages and Cell Fates during the Development of the Nematode Caenorhabditis elegansPreprint
Horvitz, H. R., Sternberg, P. W., Greenwald, I., Fixsen, W. D., & Ellis, H. M. (1983) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1983.048.01.050 · Cited by 127
Coordinated ubiquitination and phosphorylation of RIP1 regulates necroptotic cell death
de Almagro, M. C., Goncharov, T., Izrael-Tomasevic, A., Duttler, S., Kist, M., Varfolomeev, E. E., Wu, X., Lee, W. P., Murray, J. M., Webster, J. D., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.78 · Cited by 125
Accumulation of Cytosolic Calcium Induces Necroptotic Cell Death in Human Neuroblastoma
Nomura, M., Ueno, A., Saga, K., Fukuzawa, M., & Kaneda, Y. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-1283 · Cited by 119
A Morphologically Conserved Nonapoptotic Program Promotes Linker Cell Death in Caenorhabditis elegans
Abraham, M. C., Lu, Y., & Shaham, S. (2007) · Developmental Cell · doi:10.1016/j.devcel.2006.11.012 · Cited by 118
Low expression of mixed lineage kinase domain-like protein is associated with poor prognosis in ovarian cancer patients
Zhu, F., He, L., Peng, K., Liu, Y., & Xiong, J. (2013) · OncoTargets and Therapy · doi:10.2147/ott.s52805 · Cited by 115
RIP3-mediated necrotic cell death accelerates systematic inflammation and mortality
Meng, L., Jin, W., & Wang, X. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1514730112 · Cited by 109
Microarray analysis of promoter methylation in lung cancers
Fukasawa, M., Kimura, M., Morita, S., Matsubara, K., Yamanaka, S., Endo, C., Sakurada, A., Sato, M., Kondo, T., Horii, A., et al. (2006) · Journal of Human Genetics · doi:10.1007/s10038-005-0355-4 · Cited by 106
Manipulation of apoptosis and necroptosis signaling by herpesviruses
Guo, H., Kaiser, W. J., & Mocarski, E. S. (2015) · Medical Microbiology and Immunology · doi:10.1007/s00430-015-0410-5 · Cited by 99
Baculovirus inhibitor of apoptosis functions at or upstream of the apoptotic suppressor P35 to prevent programmed cell death
Manji, G. A., Hozak, R. R., LaCount, D. J., & Friesen, P. D. (1997) · Journal of Virology · doi:10.1128/jvi.71.6.4509-4516.1997 · Cited by 94
Upregulated RIP3 Expression Potentiates MLKL Phosphorylation–Mediated Programmed Necrosis in Toxic Epidermal Necrolysis
Kim, S. K., Kim, W., Yoon, J.-H., Ji, J., Morgan, M. J., Cho, H., Kim, Y. C., & Kim, Y. (2015) · Journal of Investigative Dermatology · doi:10.1038/jid.2015.90 · Cited by 85
Regulation of Kv4.3 currents by Ca2+/calmodulin-dependent protein kinase II
Sergeant, G. P., Ohya, S., Reihill, J. A., Perrino, B. A., Amberg, G. C., Imaizumi, Y., Horowitz, B., Sanders, K. M., & Koh, S. D. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00293.2004 · Cited by 79
Prognostic value of mixed lineage kinase domain-like protein expression in the survival of patients with gastric caner
Ertao, Z., Jianhui, C., Wang, K., Ye, Z., Wu, H., Chuangqi, C., Changjiang, Q., Sile, C., Yulong, H., & Shirong, C. (2016) · Tumor Biology · doi:10.1007/s13277-016-5229-1 · Cited by 79
Mixed lineage kinase domain-like protein is a prognostic biomarker for cervical squamous cell cancer.
Ruan, J., Mei, L., Zhu, Q., Shi, G., & Wang, H. (2015) · PubMed Central · Cited by 78
Dysfunctional HIV-Specific CD8+ T Cell Proliferation Is Associated with Increased Caspase-8 Activity and Mediated by Necroptosis
Gaiha, G. D., McKim, K. J., Woods, M. W., Pertel, T., Rohrbach, J., Barteneva, N. S., Chin, C. R., Liu, D., Soghoian, D. Z., Cesa, K. T., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.12.011 · Cited by 76
Towards a Genetic Definition of Cancer-Associated Inflammation
Prendergast, G. C., Metz, R. A., & Muller, A. J. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.091173 · Cited by 74
Akt Regulates TNFα Synthesis Downstream of RIP1 Kinase Activation during Necroptosis
McNamara, C. R., Ahuja, R., Osafo-Addo, A. D., Barrows, D., Kettenbach, A. N., Skidan, I. N., Teng, X., Cuny, G. D., Gerber, S. A., & Degterev, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056576 · Cited by 69
A Novel Zinc Finger Protein Interacts with Receptor-interacting Protein (RIP) and Inhibits Tumor Necrosis Factor (TNF)- and IL1-induced NF-κB Activation
Chen, D., Li, X., Zhai, Z., & Shu, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108675200 · Cited by 59
Post-translational modifications as key regulators of TNF-induced necroptosis
Liu, X., Shi, F., Li, Y., Yu, X., Peng, S., Li, W., Luo, X., & Cao, Y. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.197 · Cited by 56
IAPs and Cell Death
Silke, J., & Vince, J. E. (2016) · Current topics in microbiology and immunology · doi:10.1007/82_2016_507 · Cited by 46
Mechanisms of RIPK3‐induced inflammation
Shlomovitz, I., Zargrian, S., & Gerlic, M. (2016) · Immunology and Cell Biology · doi:10.1038/icb.2016.124 · Cited by 43
RIPK1 prevents aberrant ZBP1-initiated necroptosis
Berghe, T. V., & Kaiser, W. J. (2016) · Oncotarget · doi:10.18632/oncotarget.13926 · Cited by 29
Regulation of RIPK1's cell death function by phosphorylation
Dondelinger, Y., Vandenabeele, P., & Bertrand, M. J. M. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1112688 · Cited by 23
Self-citation
Adherence and fusion between the extremities of adjacent embryonic sacs in the pig.
Ashdown, R. R., & Marrable, A. W. (1967) · PubMed · Cited by 20

Sorted by citations

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.
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
Self-citation
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
Fundamental Mechanisms of Regulated Cell Death and Implications for Heart Disease
Re, D. P. D., Amgalan, D., Linkermann, A., Liu, Q., & Kitsis, R. N. (2019) · Physiological Reviews · doi:10.1152/physrev.00022.2018 · Cited by 994
Targeting immunogenic cell death in cancer
Ahmed, A. S., & Tait, S. W. G. (2020) · Molecular Oncology · doi:10.1002/1878-0261.12851 · Cited by 964
NINJ1 mediates plasma membrane rupture during lytic cell death
Kayagaki, N., Kornfeld, O. S., Lee, B. L., Stowe, I. B., O’Rourke, K., Li, Q., Sandoval, W., Yan, D., Kang, J., Xu, M., et al. (2021) · Nature · doi:10.1038/s41586-021-03218-7 · Cited by 857

See all 571

Authors: Grootjans, S., Vanden Berghe, T., & Vandenabeele, P.
Affiliations: Ghent University (BE)
Corresponding author: Vandenabeele, Peter
ORCID: Grootjans, Sasker
Vandenabeele, Peter
Venue: Cell Death & Differentiation
Publisher: Springer Science and Business Media LLC
Published: 2017-05-12
Volume: 24
Issue: 7
Pages: 1184-1195
ISSN: 1350-9047 (ISSN-L)
1476-5403
DOI: 10.1038/cdd.2017.65
PMC: PMC5520172
OpenAlex: W2612992363
Cited by: 566
References: 152
Citations by year: 2026: 45 · 2025: 66 · 2024: 68 · 2023: 78 · 2022: 89 · 2021: 64 · 2020: 54 · 2019: 47 · 2018: 41 · 2017: 14
FWCI: 3.99
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
Locations: Cell Death and Differentiation (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Ghent University Academic Bibliography (Ghent University) (submittedVersion)
Funders: Belgian Federal Science Policy Office (IAP7/32)
Fonds Wetenschappelijk Onderzoek (G.0875.11, FWO G.0A45.12N, FWO G0E04.16N, G078713N, FWO G0787.13N, FWO G.0C37.14N, G0C3714N, G.0A45.12N, FWO G.0875.11, BOF16/MET_V/007, G0E0416N)
Universiteit Gent (BOF16/MET_V/007, 01M00709)
Vlaams Instituut voor Biotechnologie (BOF09/01M00709)
Vlaamse regering (BOF09/01M00709, BOF16/MET_V/007)
Fondation contre le Cancer (2012-188)
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: necroptosis, regulated cell death, RIPK3, RIPK1, MLKL, RHIM domain, Toll-like receptors, TRIF, ZBP1, DAI, pattern recognition receptors, inflammatory diseases, degenerative diseases, infectious diseases, apoptosis, inflammasome activation
MeSH terms: Amyloid, Animals, Humans, Models, Biological, Necrosis, Signal Transduction, Apoptosis, Receptor-Interacting Protein Serine-Threonine Kinases

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 ›

Are you an author, or do you see a problem with this page? Request a review

Initiation and execution mechanisms of necroptosis: an overview

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks