Phosphorylation-Driven Assembly of the RIP1-RIP3 Complex Regulates Programmed Necrosis and Virus-Induced Inflammation

Inflammation and cancer

Coussens, L. M., & Werb, Z. (2002) · Nature · doi:10.1038/nature01322 · Cited by 15,111 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 1,932 · see citing works

How dying cells alert the immune system to danger

Kono, H., & Rock, K. L. (2008) · Nature Reviews Immunology · doi:10.1038/nri2215 · Cited by 1,737 · see citing works

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 1,352 · see citing works

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 · see citing works

The Death Domain Kinase RIP Mediates the TNF-Induced NF-κB Signal

Kelliher, M. A., Grimm, S., Ishida, Y., Kuo, F., Stanger, B. Z., & Leder, P. (1998) · Immunity · doi:10.1016/s1074-7613(00)80535-x · Cited by 1,102 · see citing works

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 · see citing works

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 · see citing works

RIP1 is an essential mediator of Toll-like receptor 3–induced NF-κB activation

Meylan, E., Burns, K., Hofmann, K., Blancheteau, V., Martinon, F., Kelliher, M. A., & Tschopp, J. (2004) · Nature Immunology · doi:10.1038/ni1061 · Cited by 848 · see citing works

Cleavage of the death domain kinase RIP by Caspase-8 prompts TNF-induced apoptosisPreprint

Lin, Y., Devin, A., Rodriguez, Y., & Liu, Z.-G. (1999) · Genes & Development · doi:10.1101/gad.13.19.2514 · Cited by 835 · see citing works

Death receptor signal transducers: nodes of coordination in immune signaling networks

Wilson, N., Dixit, V., & Ashkenazi, A. (2009) · Nature Immunology · doi:10.1038/ni.1714 · Cited by 569 · see citing works

RIP mediates tumor necrosis factor receptor 1 activation of NF‐kappaB but not Fas/APO‐1‐initiated apoptosis.

Ting, A. T., Pimentel‐Muiños, F. X., & Seed, B. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01007.x · Cited by 550 · see citing works

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 544 · see citing works

TNF-Induced Activation of the Nox1 NADPH Oxidase and Its Role in the Induction of Necrotic Cell Death

Kim, Y., Morgan, M. J., Choksi, S., & Liu, Z.-G. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.04.021 · Cited by 517 · see citing works

A Role for Tumor Necrosis Factor Receptor-2 and Receptor-interacting Protein in Programmed Necrosis and Antiviral Responses

Chan, F. K.-M., Shisler, J. L., Bixby, J. G., Felices, M., Zheng, L., APPEL, M. C., Orenstein, J. O., Moss, B., & Lenardo, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305633200 · Cited by 463 · see citing works

To kill or be killed: viral evasion of apoptosis

Benedict, C. A., Norris, P. S., & Ware, C. F. (2002) · Nature Immunology · doi:10.1038/ni1102-1013 · Cited by 432 · see citing works

Tumor Necrosis Factor-induced Nonapoptotic Cell Death Requires Receptor-interacting Protein-mediated Cellular Reactive Oxygen Species Accumulation

Lin, Y., Choksi, S., Shen, H., Yang, Q., Hur, G. M., Kim, Y. S., Tran, J. H., Nedospasov, S. A., & Liu, Z.-G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313141200 · Cited by 411 · see citing works

Activation of Glycogen Synthase Kinase 3β Disrupts the Binding of Hexokinase II to Mitochondria by Phosphorylating Voltage-Dependent Anion Channel and Potentiates Chemotherapy-Induced Cytotoxicity

Pastorino, J. G., Hoek, J. B., & Shulga, N. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1925 · Cited by 398 · see citing works

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 · see citing works

Rip1 Mediates the Trif-dependent Toll-like Receptor 3- and 4-induced NF-κB Activation but Does Not Contribute to Interferon Regulatory Factor 3 Activation

Hermance, N. M., Khurana, S., Lee, T. H.-Y., Fitzgerald, K. A., & Kelliher, M. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506831200 · Cited by 345 · see citing works

Disruption of Hsp90 Function Results in Degradation of the Death Domain Kinase, Receptor-interacting Protein (RIP), and Blockage of Tumor Necrosis Factor-induced Nuclear Factor-κB Activation

Lewis, J., Devin, A., Miller, A., Lin, Y., Rodriguez, Y., Neckers, L., & Liu, Z.-G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10519 · Cited by 331 · see citing works

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 · see citing works

RIP3, a Novel Apoptosis-inducing Kinase

Sun, X., Lee, J., Navas, T. A., Baldwin, D. T., Stewart, T. A., & Dixit, V. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.24.16871 · Cited by 240 · see citing works

Caspase inhibition causes hyperacute tumor necrosis factor–induced shock via oxidative stress and phospholipase A2

Cauwels, A., Janssen, B. J., Waeytens, A., Cuvelier, C. A., & Brouckaert, P. (2003) · Nature Immunology · doi:10.1038/ni914 · Cited by 217 · see citing works

Innate immunity against vaccinia virus is mediated by TLR2 and requires TLR-independent production of IFN-β

Zhu, J., Martinez, J., Huang, X., & Yang, Y. (2006) · Blood · doi:10.1182/blood-2006-06-027136 · Cited by 207 · see citing works

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 · see citing works

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 · see citing works

Induction of Necrotic-Like Cell Death by Tumor Necrosis Factor Alpha and Caspase Inhibitors: Novel Mechanism for Killing Virus-Infected Cells

Li, M. O., & Beg, A. A. (2000) · Journal of Virology · doi:10.1128/jvi.74.16.7470-7477.2000 · Cited by 144 · see citing works

Identification of RIP3, a RIP-like kinase that activates apoptosis and NFκB

Yu, P., Huang, B. C. B., Shen, M., Quast, J., Chan, E., Xu, X. M., Nolan, G. P., Payan, D. G., & Luo, Y. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80239-5 · Cited by 140 · see citing works

Antiviral Activity of Tumor Necrosis Factor (TNF) Is Mediated via p55 and p75 TNF Receptors

Ruby, J. C., Bluethmann, H., & Peschon, J. J. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.9.1591 · Cited by 121 · see citing works

The RIP‐like kinase, RIP3, induces apoptosis and NF‐κB nuclear translocation and localizes to mitochondria

Kasof, G. M., Prosser, J. C., Liu, D., Lorenzi, M. V., & Gomes, B. C. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01473-3 · Cited by 120 · see citing works

Negative regulation of mitochondrial VDAC channels by C-Raf kinase

Mellay, V. L., Troppmair, J., Benz, R., & Rapp, U. R. (2002) · BMC Cell Biology · doi:10.1186/1471-2121-3-14 · Cited by 65 · see citing works

Mouse Receptor Interacting Protein 3 Does Not Contain a Caspase-Recruiting or a Death Domain but Induces Apoptosis and Activates NF-κB

Pazdernik, N., Donner, D., Goebl, M., & Harrington, M. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.6500 · Cited by 59 · see citing works

Regulation of NF-κB Activity and Keratinocyte Differentiation by the RIP4 Protein: Implications for Cutaneous Wound Repair

Adams, S., Pankow, S., Werner, S., et al. (2006) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700588 · Cited by 50 · see citing works

Post-transcriptional regulation of E2A proteins via lipopolysaccharide and CD40 signaling

Meyer, K. B., & Mufti, D. A. H. (2000) · European Journal of Immunology · doi:10.1002/1521-4141(200002)30:2 · Cited by 8 · see citing works

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 · see citing works

Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012

Galluzzi, L., Vitale, I., Abrams, J. M., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., Dawson, T. M., Dawson, V. L., El-Deiry, W. S., Fulda, S., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.96 · Cited by 2,421 · see citing works

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 · see citing works

Glutaminolysis and transferrin regulate ferroptosis

Gao, M., Monian, P., Quadri, N., Ramasamy, R., & Jiang, X. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.011 · Cited by 2,069 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Necroptosis

Linkermann, A., & Green, D. R. (2014) · New England Journal of Medicine · doi:10.1056/nejmra1310050 · Cited by 1,103 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Macrophage defense mechanisms against intracellular bacteria

Weiss, G., & Schaible, U. E. (2015) · Immunological Reviews · doi:10.1111/imr.12266 · Cited by 989 · see citing works

TNF and ROS crosstalk in inflammation

Blaser, H., Dostert, C., Mak, T. W., & Brenner, D. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.12.002 · Cited by 1,008 · see citing works

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 · see citing works

Necroptosis and RIPK1-mediated neuroinflammation in CNS diseases

Yuan, J., Amin, P., & Ofengeim, D. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-018-0093-1 · Cited by 967 · see citing works

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 · see citing works

Pyroptosis is driven by non-selective gasdermin-D pore and its morphology is different from MLKL channel-mediated necroptosis

Chen, X., He, W.-T., Hu, L., Li, J., Fang, Y., Wang, X., Xu, X., Wang, Z., Huang, K., & Han, J. (2016) · Cell Research · doi:10.1038/cr.2016.100 · Cited by 831 · see citing works

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 · see citing works

T cell lipid peroxidation induces ferroptosis and prevents immunity to infection

Matsushita, M., Freigang, S., Schneider, C., Conrad, M., Bornkamm, G. W., & Kopf, M. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20140857 · Cited by 672 · see citing works

Regulated 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 · see citing works

Tnf dually mediates resistance and susceptibility to mycobacteria via mitochondrial reactive oxygen species

Roca, F. J., & Ramakrishnan, L. (2013) · Cell · doi:10.1016/j.cell.2013.03.022 · Cited by 592 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Identification of the PANoptosome: A Molecular Platform Triggering Pyroptosis, Apoptosis, and Necroptosis (PANoptosis)

Christgen, S., Zheng, M., Kesavardhana, S., Karki, R., Malireddi, R. K. S., Banoth, B., Place, D. E., Briard, B., Sharma, B. R., Tuladhar, S., et al. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00237 · Cited by 588 · see citing works

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 · see citing works

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 · see citing works

Ferroptosis, but Not Necroptosis, Is Important in Nephrotoxic Folic Acid–Induced AKI

Martin-Sanchez, D., Ruiz-Andres, O., Poveda, J., Carrasco, S., Cannata-Ortiz, P., Sanchez-Niño, M. D., Ruiz Ortega, M., Egido, J., Linkermann, A., Ortiz, A., et al. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2015121376 · Cited by 564 · see citing works

From pyroptosis, apoptosis and necroptosis to PANoptosis: A mechanistic compendium of programmed cell death pathways

Wang, Y., & Kanneganti, T.-D. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.07.038 · Cited by 545 · see citing works

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 · see citing works

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 · see citing works

Mechanisms of innate and adaptive immunity to the Pfizer-BioNTech BNT162b2 vaccine

Li, C., Lee, A., Grigoryan, L., Arunachalam, P. S., Scott, M. K. D., Trisal, M., Wimmers, F., Sanyal, M., Weidenbacher, P. A., Feng, Y., et al. (2022) · Nature Immunology · doi:10.1038/s41590-022-01163-9 · Cited by 505 · see citing works

Inhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation

Vince, J. E., Wong, W. W.-L., Gentle, I., Lawlor, K. E., Allam, R., O'Reilly, L., Mason, K., Gross, O., Ma, S., Guarda, G., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.012 · Cited by 491 · see citing works

TBK1 Suppresses RIPK1-Driven Apoptosis and Inflammation during Development and in Aging

Xu, D., Jin, T., Zhu, H., Chen, H., Ofengeim, D., Zou, C., Mifflin, L., Pan, L., Amin, P., Li, W., et al. (2018) · Cell · doi:10.1016/j.cell.2018.07.041 · Cited by 461 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Microglia: Agents of the CNS Pro-Inflammatory Response

Rodríguez-Gómez, J. A., Kavanagh, E., Engskog-Vlachos, P., Engskog, M. K. R., Herrera, A. J., Espinosa-Oliva, A. M., Joseph, B., Hajji, N., Venero, J. L., & Burguillos, M. A. (2020) · Cells · doi:10.3390/cells9071717 · Cited by 365 · see citing works

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 · see citing works

Platelets mediate increased endothelium permeability in dengue through NLRP3-inflammasome activation

Hottz, E. D., Lopes, J. F., Freitas, C., Valls-de-Souza, R., Oliveira, M. F., Bozza, M. T., Da Poian, A. T., Weyrich, A. S., Zimmerman, G. A., Bozza, F. A., et al. (2013) · Blood · doi:10.1182/blood-2013-05-504449 · Cited by 348 · see citing works

A Death Effector Domain Chain DISC Model Reveals a Crucial Role for Caspase-8 Chain Assembly in Mediating Apoptotic Cell Death

Dickens, L. S., Boyd, R. S., Jukes-Jones, R., Hughes, M. A., Robinson, G. L., Fairall, L., Schwabe, J. W. R., Cain, K., & MacFarlane, M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.004 · Cited by 349 · see citing works

Survival Function of the FADD-CASPASE-8-cFLIPL Complex

Dillon, C. P., Oberst, A., Weinlich, R., Janke, L. J., Kang, T.-B., Ben-Moshe, T., Mak, T. W., Wallach, D., & Green, D. R. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.03.010 · Cited by 331 · see citing works

Mechanisms of drug-induced liver injury

Yuan, L., & Kaplowitz, N. (2013) · Clinics in Liver Disease · doi:10.1016/j.cld.2013.07.002 · Cited by 322 · see citing works

The Autophagy Machinery Controls Cell Death Switching between Apoptosis and Necroptosis

Goodall, M. L., Fitzwalter, B. E., Zahedi, S., Wu, M., Rodriguez, D., Mulcahy-Levy, J. M., Green, D. R., Morgan, M., Cramer, S. D., & Thorburn, A. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.04.018 · Cited by 314 · see citing works

CYLD Deubiquitinates RIP1 in the TNFα-Induced Necrosome to Facilitate Kinase Activation and Programmed Necrosis

Moquin, D. M., McQuade, T., & Chan, F. K.-M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076841 · Cited by 320 · see citing works

RIPK1 ensures intestinal homeostasis by protecting the epithelium against apoptosis

Takahashi, N., Vereecke, L., Bertrand, M. J. M., Duprez, L., Berger, S. B., Divert, T., Gonçalves, A., Sze, M., Gilbert, B., Kourula, S., et al. (2014) · Nature · doi:10.1038/nature13706 · Cited by 318 · see citing works

Widespread Mitochondrial Depletion via Mitophagy Does Not Compromise Necroptosis

Tait, S. W. G., Oberst, A., Quarato, G., Milasta, S., Haller, M., Wang, R., Karvela, M., Ichim, G., Yatim, N., Albert, M. L., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.034 · Cited by 303 · see citing works

The Adaptor Protein FADD Protects Epidermal Keratinocytes from Necroptosis In Vivo and Prevents Skin Inflammation

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 · see citing works

Bax and Bak function as the outer membrane component of the mitochondrial permeability pore in regulating necrotic cell death in mice

Karch, J., Kwong, J. Q., Burr, A. R., Sargent, M. A., Elrod, J. W., Peixoto, P. M., Martinez-Caballero, S., Osinska, H., Cheng, E. H.-Y., Robbins, J., et al. (2013) · eLife · doi:10.7554/elife.00772 · Cited by 290 · see citing works

Targeting macrophage necroptosis for therapeutic and diagnostic interventions in atherosclerosis

Karunakaran, D., Geoffrion, M., Wei, L., Gan, W., Richards, L., Shangari, P., DeKemp, E. M., Beanlands, R. A., Perisic, L., Maegdefessel, L., et al. (2016) · Science Advances · doi:10.1126/sciadv.1600224 · Cited by 293 · see citing works

The ubiquitin-modifying enzyme A20 restricts ubiquitination of the kinase RIPK3 and protects cells from necroptosis

Onizawa, M., Oshima, S., Schulze-Topphoff, U., Oses-Prieto, J. A., Lu, T., Tavares, R., Prodhomme, T., Duong, B., Whang, M. I., Advincula, R., et al. (2015) · Nature Immunology · doi:10.1038/ni.3172 · Cited by 284 · see citing works

XIAP Restricts TNF- and RIP3-Dependent Cell Death and Inflammasome Activation

Yabal, M., Müller, N., Adler, H., Knies, N., Groß, C. J., Damgaard, R. B., Kanegane, H., Ringelhan, M., Kaufmann, T., Heikenwälder, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.008 · Cited by 255 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

The Pseudokinase MLKL and the Kinase RIPK3 Have Distinct Roles in Autoimmune Disease Caused by Loss of Death-Receptor-Induced Apoptosis

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 · see citing works

The effects of neutrophil-generated hypochlorous acid and other hypohalous acids on host and pathogens

Ulfig, A., & Leichert, L. I. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03591-y · Cited by 239 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

HSP90 activity is required for MLKL oligomerisation and membrane translocation and the induction of necroptotic cell death

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 · see citing works

Human TBK1 deficiency leads to autoinflammation driven by TNF-induced cell death

Taft, J., Markson, M., Legarda, D., Patel, R., Chan, M., Malle, L., Richardson, A., Gruber, C., Martín-Fernández, M., Mancini, G. M. S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.07.026 · Cited by 151 · see citing works

cIAP1 and cIAP2 limit macrophage necroptosis by inhibiting Rip1 and Rip3 activation

McComb, S., Cheung, H. H., Korneluk, R. G., Wang, S., Krishnan, L., & Sad, S. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2012.59 · Cited by 148 · see citing works

Modulatory profiling identifies mechanisms of small molecule-induced cell death

Wolpaw, A. J., Shimada, K., Skouta, R., Welsch, M. E., Akavia, U. D., Pe'er, D., Shaik, F., Bulinski, J. C., & Stockwell, B. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106149108 · Cited by 133 · see citing works

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 · see citing works

Casein kinase 1α: biological mechanisms and theranostic potential

Jiang, S., Zhang, M., Sun, J., & Yang, X. (2018) · Cell Communication and Signaling · doi:10.1186/s12964-018-0236-z · Cited by 130 · see citing works

Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity

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 · see citing works

Innate Immune Cell Trafficking and Function During Sterile Inflammation of the Liver

McDonald, B., & Kubes, P. (2016) · Gastroenterology · doi:10.1053/j.gastro.2016.09.048 · Cited by 123 · see citing works

The regulation of cancer cell death and metabolism by extracellular matrix attachment

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 · see citing works

Inhibition of BMI1 induces autophagy-mediated necroptosis

Dey, A., Mustafi, S. B., Saha, S., Kumar Dhar Dwivedi, S., Mukherjee, P., & Bhattacharya, R. (2016) · Autophagy · doi:10.1080/15548627.2016.1147670 · Cited by 97 · see citing works

HS-1371, a novel kinase inhibitor of RIP3-mediated necroptosis

Park, H.-H., Park, S.-Y., Mah, S., Park, J.-H., Hong, S.-S., Hong, S., & Kim, Y.-S. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0152-8 · Cited by 110 · see citing works

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 · see citing works

Poly IC Triggers a Cathepsin D- and IPS-1-Dependent Pathway to Enhance Cytokine Production and Mediate Dendritic Cell Necroptosis

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 · see citing works

In TNF-stimulated Cells, RIPK1 Promotes Cell Survival by Stabilizing TRAF2 and cIAP1, which Limits Induction of Non-canonical NF-κB and Activation of Caspase-8

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 · see citing works

TRAF2 is a biologically important necroptosis suppressor

Petersen, S. L., Chen, T. T., Lawrence, D. A., Marsters, S. A., Gonzalvez, F., & Ashkenazi, A. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2015.35 · Cited by 99 · see citing works

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 · see citing works

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 · see citing works

Interleukin-1α and brain inflammation

Brough, D., & Denes, A. (2015) · IUBMB Life · doi:10.1002/iub.1377 · Cited by 54 · see citing works

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 · see citing works

The interplay of autophagy and non-apoptotic cell death pathways

(2020) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2019.12.004 · Cited by 50 · see citing works

RIPK3 Mediates Necroptosis during Embryonic Development and Postnatal Inflammation in Fadd-Deficient Mice

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 · see citing works

RIP1 kinase activity-dependent roles in embryonic development of Fadd-deficient mice

Liu, Y., Fan, C., Zhang, Y., Yu, X., Wu, X., Zhang, X., Zhao, Q., Zhang, H., Xie, Q., Li, M., et al. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.78 · Cited by 42 · see citing works

TNFα-induced lysosomal membrane permeability (LMP) is downstream of MOMP and triggered by caspase-mediated p75 cleavage and ROS formation

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 · see citing works

RIP3 expression induces a death profile change in U2OS osteosarcoma cells after 5-ALA-PDT: RIP3 IN PDT-INDUCED CELL DEATH

Coupienne, I., Fettweis, G., & Piette, J. (2011) · Lasers in Surgery and Medicine · doi:10.1002/lsm.21088 · Cited by 41 · see citing works

FKBP12 mediates necroptosis by initiating RIPK1–RIPK3–MLKL signal transduction in response to TNF receptor 1 ligation

Wang, Z., Feng, J., Yu, J., & Chen, G. (2019) · Journal of Cell Science · doi:10.1242/jcs.227777 · Cited by 35 · see citing works

Muscle fiber necroptosis in pathophysiology of idiopathic inflammatory myopathies and its potential as target of novel treatment strategy

Kamiya, M., Kimura, N., Umezawa, N., Hasegawa, H., & Yasuda, S. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1191815 · Cited by 21 · see citing works