Fundamental Mechanisms of Regulated Cell Death and Implications for Heart Disease

Cardiac autophagy is a maladaptive response to hemodynamic stress

Zhu, H., Tannous, P., Johnstone, J. L., Kong, Y., Shelton, J. M., Richardson, J. A., Le, V., Levine, B., Rothermel, B. A., & Hill, J. A. (2007) · Journal of Clinical Investigation · doi:10.1172/jci27523 · Cited by 764

Cell Death in the Pathogenesis of Heart Disease: Mechanisms and Significance

Whelan, R. S., Kaplinskiy, V., & Kitsis, R. N. (2010) · Annual Review of Physiology · doi:10.1146/annurev.physiol.010908.163111 · Cited by 759

Unsolved mysteries: How does lipid peroxidation cause ferroptosis?

Feng, H., & Stockwell, B. R. (2018) · PLOS Biology · doi:10.1371/journal.pbio.2006203 · Cited by 759

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

Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase TRAF2

Alvarez, S. E., Harikumar, K. B., Hait, N. C., Allegood, J., Strub, G. M., Kim, E. Y., Maceyka, M., Jiang, H., Luo, C., Kordula, T., et al. (2010) · Nature · doi:10.1038/nature09128 · Cited by 752

A Nonapoptotic Cell Death Process, Entosis, that Occurs by Cell-in-Cell Invasion

Overholtzer, M., Mailleux, A. A., Mouneimne, G., Normand, G., Schnitt, S. J., King, R. W., Cibas, E. S., & Brugge, J. S. (2007) · Cell · doi:10.1016/j.cell.2007.10.040 · Cited by 748

Inhibition of Ca2+-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase

Halestrap, A. P., & Davidson, A. M. (1990) · Biochemical Journal · doi:10.1042/bj2680153 · Cited by 747

Identification of Omi/HtrA2 as a Mitochondrial Apoptotic Serine Protease That Disrupts Inhibitor of Apoptosis Protein-Caspase Interaction

Hegde, R., Srinivasula, S. M., Zhang, Z., Wassell, R., Mukattash, R., Cilenti, L., DuBois, G., Lazebnik, Y., Zervos, A. S., Fernandes-Alnemri, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109721200 · Cited by 745

Autosis and autophagic cell death: the dark side of autophagy

Liu, Y., & Levine, B. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.143 · Cited by 742

TRIF Licenses Caspase-11-Dependent NLRP3 Inflammasome Activation by Gram-Negative Bacteria

Rathinam, V. A. K., Vanaja, S. K., Waggoner, L., Sokolovska, A., Becker, C., Stuart, L. M., Leong, J. M., & Fitzgerald, K. A. (2012) · Cell · doi:10.1016/j.cell.2012.07.007 · Cited by 729

Mechanism of XIAP-Mediated Inhibition of Caspase-9

Shiozaki, E. N., Chai, J., Rigotti, D. J., Riedl, S. J., Li, P., Srinivasula, S. M., Alnemri, E. S., Fairman, R., & Shi, Y. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00054-6 · Cited by 719

Apoptosis-inducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death

Yu, S.-W., Andrabi, S. A., Wang, H., Kim, N. S., Poirier, G. G., Dawson, T. M., & Dawson, V. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606528103 · Cited by 718

How Do Cytotoxic Lymphocytes Kill Cancer Cells?

Martínez-Lostao, L., Anel, A., & Pardo, J. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-0685 · Cited by 717

Deubiquitination of NLRP3 by BRCC3 Critically Regulates Inflammasome Activity

Py, B. F., Kim, M.-S., Vakifahmetoglu-Norberg, H., & Yuan, J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.11.009 · Cited by 715

Cyclosporine before PCI in Patients with Acute Myocardial Infarction

Cung, T.-T., Morel, O., Cayla, G., Rioufol, G., Garcia-Dorado, D., Angoulvant, D., Bonnefoy-Cudraz, E., Guérin, P., Elbaz, M., Delarche, N., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1505489 · Cited by 713

Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B

Darmon, A. J., Nicholson, D. W., & Bleackley, R. C. (1995) · Nature · doi:10.1038/377446a0 · Cited by 707

Nicotinic Acid, Nicotinamide, and Nicotinamide Riboside: A Molecular Evaluation of NAD + Precursor Vitamins in Human Nutrition

Bogan, K. L., & Brenner, C. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155443 · Cited by 707

Akt Activation Preserves Cardiac Function and Prevents Injury After Transient Cardiac Ischemia In Vivo

Matsui, T., Tao, J., del Monte, F., Lee, K.-H., Li, L., Picard, M., Force, T. L., Franke, T. F., Hajjar, R. J., & Rosenzweig, A. (2001) · Circulation · doi:10.1161/01.cir.104.3.330 · Cited by 701

BAX activation is initiated at a novel interaction site

Gavathiotis, E., Suzuki, M., Davis, M. L., Pitter, K., Bird, G. H., Katz, S. G., Tu, H.-C., Kim, H., Cheng, E. H.-Y., Tjandra, N., et al. (2008) · Nature · doi:10.1038/nature07396 · Cited by 700

Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: An update

Soldani, C., & Scovassi, A. I. (2002) · Apoptosis · doi:10.1023/a:1016119328968 · Cited by 697

Autoantibodies against cardiac troponin I are responsible for dilated cardiomyopathy in PD-1-deficient mice

Okazaki, T., Tanaka, Y., Nishio, R., Mitsuiye, T., Mizoguchi, A., Wang, J., Ishida, M., Hiai, H., Matsumori, A., Minato, N., et al. (2003) · Nature Medicine · doi:10.1038/nm955 · Cited by 689

ESCRT-III Acts Downstream of MLKL to Regulate Necroptotic Cell Death and Its Consequences

Gong, Y.-N., Guy, C., Olauson, H., Becker, J. U., Yang, M., Fitzgerald, P., Linkermann, A., & Green, D. R. (2017) · Cell · doi:10.1016/j.cell.2017.03.020 · Cited by 689

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

The Adaptor MAVS Promotes NLRP3 Mitochondrial Localization and Inflammasome Activation

Subramanian, N., Natarajan, K., Clatworthy, M. R., Wang, Z., & Germain, R. N. (2013) · Cell · doi:10.1016/j.cell.2013.02.054 · Cited by 678

Fas Preassociation Required for Apoptosis Signaling and Dominant Inhibition by Pathogenic Mutations

Siegel, R. M., Frederiksen, J. K., Zacharias, D. A., Chan, F. K.-M., Johnson, M., Lynch, D., Tsien, R. Y., & Lenardo, M. J. (2000) · Science · doi:10.1126/science.288.5475.2354 · Cited by 662

Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death

Suzuki, Y., Nakabayashi, Y., & Takahashi, R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161506698 · Cited by 654

Poly(ADP-ribose) (PAR) polymer is a death signal

Andrabi, S. A., Kim, N. S., Yu, S.-W., Wang, H., Koh, D. W., Sasaki, M., Klaus, J. A., Otsuka, T., Zhang, Z., Koehler, R. C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606526103 · Cited by 643

PD-L1-deficient mice show that PD-L1 on T cells, antigen-presenting cells, and host tissues negatively regulates T cells

Latchman, Y. E., Liang, S. C., Wu, Y., Chernova, T., Sobel, R. A., Klemm, M., Kuchroo, V. K., Freeman, G. J., & Sharpe, A. H. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307252101 · Cited by 636

Cardiovascular Toxic Effects of Targeted Cancer Therapies

Moslehi, J. J. (2016) · New England Journal of Medicine · doi:10.1056/nejmra1100265 · Cited by 635

A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors.

Duckett, C. S., Nava, V. E., Gedrich, R. W., Clem, R. J., Van Dongen, J. L., Gilfillan, M. C., Shiels, H., Hardwick, J. M., & Thompson, C. B. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00629.x · Cited by 633

Bcl-xL Retrotranslocates Bax from the Mitochondria into the Cytosol

Edlich, F., Banerjee, S., Suzuki, M., Cleland, M. M., Arnoult, D., Wang, C., Neutzner, A., Tjandra, N., & Youle, R. J. (2011) · Cell · doi:10.1016/j.cell.2011.02.034 · Cited by 630

Transgenic Gαq overexpression induces cardiac contractile failure in mice

D’Angelo, D. D., Sakata, Y., Lorenz, J. N., Boivin, G. P., Walsh, R. A., Liggett, S. B., & Dorn, G. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.15.8121 · Cited by 629

The inflammasome promotes adverse cardiac remodeling following acute myocardial infarction in the mouse

Mezzaroma, E., Toldo, S., Farkas, D., Seropian, I. M., Van Tassell, B. W., Salloum, F. N., Kannan, H. R., Menna, A. C., Voelkel, N. F., & Abbate, A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108586108 · Cited by 629

Attenuation of Ischemia/Reperfusion Injury in Rats by a Caspase Inhibitor

Yaoita, H., Ogawa, K., Maehara, K., & Maruyama, Y. (1998) · Circulation · doi:10.1161/01.cir.97.3.276 · Cited by 626

Role of Bax and Bak in mitochondrial morphogenesis

Karbowski, M., Norris, K. L., Cleland, M. M., Jeong, S.-Y., & Youle, R. J. (2006) · Nature · doi:10.1038/nature05111 · Cited by 625

RIP3 Induces Apoptosis Independent of Pronecrotic Kinase Activity

Mandal, P., Berger, S. B., Pillay, S., Moriwaki, K., Huang, C., Guo, H., Lich, J. D., Finger, J., Kasparcova, V., Votta, B., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.10.021 · Cited by 618

Adaptive Immune Resistance: How Cancer Protects from Immune Attack

Ribas, A. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0563 · Cited by 613

Autosis is a Na + ,K + -ATPase–regulated form of cell death triggered by autophagy-inducing peptides, starvation, and hypoxia–ischemia

Liu, Y., Shoji-Kawata, S., Sumpter, R. M., Wei, Y., Ginet, V., Zhang, L., Posner, B., Tran, K. A., Green, D. R., Xavier, R. J., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1319661110 · Cited by 607

Disruption of Mitochondrial Function during Apoptosis Is Mediated by Caspase Cleavage of the p75 Subunit of Complex I of the Electron Transport Chain

Ricci, J.-E., Muñoz-Pinedo, C., Fitzgerald, P., Bailly-Maitre, B., Perkins, G. A., Yadava, N., Scheffler, I. E., Ellisman, M. H., & Green, D. R. (2004) · Cell · doi:10.1016/j.cell.2004.05.008 · Cited by 602

Stepwise Activation of BAX and BAK by tBID, BIM, and PUMA Initiates Mitochondrial Apoptosis

Kim, H., Tu, H.-C., Ren, D., Takeuchi, O., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J.-D., & Cheng, E. H.-Y. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.030 · Cited by 600

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

A Unified Model of Mammalian BCL-2 Protein Family Interactions at the Mitochondria

Llambi, F., Moldoveanu, T., Tait, S. W. G., Bouchier-Hayes, L., Temirov, J., McCormick, L. L., Dillon, C. P., & Green, D. R. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.10.001 · Cited by 596

Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis

Zong, W.-X., Li, C., Hatzivassiliou, G., Lindsten, T., Yu, Q.-C., Yuan, J., & Thompson, C. B. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302084 · Cited by 595

Parthanatos: mitochondrial‐linked mechanisms and therapeutic opportunities

Fatokun, A. A., Dawson, V. L., & Dawson, T. M. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12416 · Cited by 594

RIPK1 Regulates RIPK3-MLKL-Driven Systemic Inflammation and Emergency Hematopoiesis

Rickard, J. A., O’Donnell, J. A., Evans, J. M., Lalaoui, N., Poh, A. R., Rogers, T., Vince, J. E., Lawlor, K. E., Ninnis, R. L., Anderton, H., et al. (2014) · Cell · doi:10.1016/j.cell.2014.04.019 · Cited by 593

An uncoupling channel within the c-subunit ring of the F 1 F O ATP synthase is the mitochondrial permeability transition pore

Alavian, K. N., Beutner, G., Lazrove, E., Sacchetti, S., Park, H.-A., Licznerski, P., Li, H., Nabili, P., Hockensmith, K., Graham, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401591111 · Cited by 592

NF-κB Inducers Upregulate cFLIP, a Cycloheximide-Sensitive Inhibitor of Death Receptor Signaling

Kreuz, S., Siegmund, D., Scheurich, P., & Wajant, H. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.12.3964-3973.2001 · Cited by 583

Structural Basis of Caspase-7 Inhibition by XIAP

Chai, J., Shiozaki, E., Srinivasula, S. M., Wu, Q., Dataa, P., Alnemri, E. S., & Shi, Y. (2001) · Cell · doi:10.1016/s0092-8674(01)00272-0 · Cited by 581

The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology

Bernardi, P., Rasola, A., Forte, M., & Lippe, G. (2015) · Physiological Reviews · doi:10.1152/physrev.00001.2015 · Cited by 577

The hallmarks of successful anticancer immunotherapy

Galluzzi, L., Chan, T. A., Kroemer, G., Wolchok, J. D., & López-Soto, A. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aat7807 · Cited by 575

Cardiac angiogenic imbalance leads to peripartum cardiomyopathy

Patten, I. S., Rana, S., Shahul, S., Rowe, G. C., Jang, C., Liu, L., Hacker, M. R., Rhee, J. S., Mitchell, J., Mahmood, F., et al. (2012) · Nature · doi:10.1038/nature11040 · Cited by 572

Xk-Related Protein 8 and CED-8 Promote Phosphatidylserine Exposure in Apoptotic Cells

Suzuki, J., Denning, D. P., Imanishi, E., Horvitz, H. R., & Nagata, S. (2013) · Science · doi:10.1126/science.1236758 · Cited by 569

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

Crystal Structure of the Bcl-XL-Beclin 1 Peptide Complex

Oberstein, A., Jeffrey, P. D., & Shi, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700492200 · Cited by 563

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

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

FADD and Caspase-8 Mediate Priming and Activation of the Canonical and Noncanonical Nlrp3 Inflammasomes

Gurung, P., Anand, P. K., Malireddi, R. K. S., Vande Walle, L., Van Opdenbosch, N., Dillon, C. P., Weinlich, R., Green, D. R., Lamkanfi, M., & Kanneganti, T.-D. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302839 · Cited by 558

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

Exploring the TRAILs less travelled: TRAIL in cancer biology and therapy

von Karstedt, S., Montinaro, A., & Walczak, H. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2017.28 · Cited by 556

c-IAP1 and c-IAP2 Are Critical Mediators of Tumor Necrosis Factor α (TNFα)-induced NF-κB Activation

Varfolomeev, E., Goncharov, T., Fedorova, A. V., Dynek, J. N., Zobel, K., Deshayes, K., Fairbrother, W. J., & Vucic, D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c800128200 · Cited by 552

CD80 (B7-1) Binds Both CD28 and CTLA-4 with a Low Affinity and Very Fast Kinetics

van der Merwe, P. A., Bodian, D. L., Daenke, S., Linsley, P., & Davis, S. J. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.3.393 · Cited by 551

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 551

Transcriptional regulation of bcl-2 by nuclear factor κB and its significance in prostate cancer

Catz, S. D., & Johnson, J. L. (2001) · Oncogene · doi:10.1038/sj.onc.1204926 · Cited by 538

RIPK1 maintains epithelial homeostasis by inhibiting apoptosis and necroptosis

Dannappel, M., Vlantis, K., Kumari, S., Polykratis, A., Kim, C., Wachsmuth, L., Eftychi, C., Lin, J., Corona, T., Hermance, N., et al. (2014) · Nature · doi:10.1038/nature13608 · Cited by 534

The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death

Yuan, J., & Horvitz, H. R. (1990) · Developmental Biology · doi:10.1016/0012-1606(90)90174-h · Cited by 529

The 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosis

Liu, X., Li, P., Widlak, P., Zou, H., Luo, X., Garrard, W. T., & Wang, X. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.15.8461 · Cited by 529

The Death Domain Superfamily in Intracellular Signaling of Apoptosis and Inflammation

Park, H. H., Lo, Y.-C., Lin, S.-C., Wang, L., Yang, J. K., & Wu, H. (2007) · Annual Review of Immunology · doi:10.1146/annurev.immunol.25.022106.141656 · Cited by 526

Enhanced Gαq signaling: A common pathway mediates cardiac hypertrophy and apoptotic heart failure

Adams, J. W., Sakata, Y., Davis, M. G., Sah, V. P., Wang, Y., Liggett, S. B., Chien, K. R., Brown, J. H., & Dorn, G. W. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.10140 · Cited by 525

Caspase-mediated cleavage of phospholipid flippase for apoptotic phosphatidylserine exposure

Segawa, K., Kurata, S., Yanagihashi, Y., Brummelkamp, T. R., Matsuda, F., & Nagata, S. (2014) · Science · doi:10.1126/science.1252809 · Cited by 525

The NLRP3 inflammasome is up-regulated in cardiac fibroblasts and mediates myocardial ischaemia–reperfusion injury

Sandanger, Ø., Ranheim, T., Vinge, L. E., Bliksøen, M., Alfsnes, K., Finsen, A. V., Dahl, C. P., Askevold, E. T., Florholmen, G., Christensen, G., et al. (2013) · Cardiovascular Research · doi:10.1093/cvr/cvt091 · Cited by 524

Critical reappraisal confirms that Mitofusin 2 is an endoplasmic reticulum–mitochondria tether

Naon, D., Zaninello, M., Giacomello, M., Varanita, T., Grespi, F., Lakshminaranayan, S., Serafini, A., Semenzato, M., Herkenne, S., Hernández-Alvarez, M. I., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606786113 · Cited by 521

Requirement for Casper (c-FLIP) in Regulation of Death Receptor–Induced Apoptosis and Embryonic Development

Yeh, W.-C., Itie, A., Elia, A. J., Ng, M., Shu, H.-B., Wakeham, A., Mirtsos, C., Suzuki, N., Bonnard, M., Goeddel, D. V., et al. (2000) · Immunity · doi:10.1016/s1074-7613(00)80214-9 · Cited by 515

Linking cellular stress responses to systemic homeostasis

Galluzzi, L., Yamazaki, T., & Kroemer, G. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0068-0 · Cited by 515

Cardiovascular toxicities associated with immune checkpoint inhibitors

Hu, J.-R., Florido, R., Lipson, E. J., Naidoo, J., Ardehali, R., Tocchetti, C. G., Lyon, A. R., Padera, R. F., Johnson, D. B., & Moslehi, J. (2019) · Cardiovascular Research · doi:10.1093/cvr/cvz026 · Cited by 508

Negative regulation of the NLRP3 inflammasome by A20 protects against arthritis

Vande Walle, L., Van Opdenbosch, N., Jacques, P., Fossoul, A., Verheugen, E., Vogel, P., Beyaert, R., Elewaut, D., Kanneganti, T.-D., van Loo, G., et al. (2014) · Nature · doi:10.1038/nature13322 · Cited by 506

Mst1 inhibits autophagy by promoting the interaction between Beclin1 and Bcl-2

Maejima, Y., Kyoi, S., Zhai, P., Liu, T., Li, H., Ivessa, A., Sciarretta, S., Del Re, D. P., Zablocki, D. K., Hsu, C.-P., et al. (2013) · Nature Medicine · doi:10.1038/nm.3322 · Cited by 499

Ferroptotic cell death and TLR4/Trif signaling initiate neutrophil recruitment after heart transplantation

Li, W., Feng, G., Gauthier, J. M., Lokshina, I., Higashikubo, R., Evans, S., Liu, X., Hassan, A., Tanaka, S., Cicka, M., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci126428 · Cited by 492

NLRP3 Phosphorylation Is an Essential Priming Event for Inflammasome Activation

Song, N., Liu, Z.-S., Xue, W., Bai, Z.-F., Wang, Q.-Y., Dai, J., Liu, X., Huang, Y.-J., Cai, H., Zhan, X.-Y., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.017 · Cited by 487

Programmed cell death—I. Cytology of degeneration in the intersegmental muscles of the Pernyi silkmoth

Lockshin, R. A., & Williams, C. M. (1965) · Journal of Insect Physiology · doi:10.1016/0022-1910(65)90099-5 · Cited by 486

CD80 (B7) and CD86 (B70) provide similar costimulatory signals for T cell proliferation, cytokine production, and generation of CTL.

Lanier, L. L., O'Fallon, S., Somoza, C., Phillips, J. H., Linsley, P. S., Okumura, K., Ito, D., & Azuma, M. (1995) · The Journal of Immunology · doi:10.4049/jimmunol.154.1.97 · Cited by 480

Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins

Boyd, J. M., Malstrom, S., Subramanian, T., Venkatesh, L. K., Schaeper, U., Elangovan, B., D'Sa-Eipper, C., & Chinnadurai, G. (1994) · Cell · doi:10.1016/0092-8674(94)90202-x · Cited by 477

Poly(ADP-ribose) (PAR) binding to apoptosis-inducing factor is critical for PAR polymerase-1-dependent cell death (parthanatos)

Wang, Y., Kim, N. S., Haince, J.-F., Kang, H. C., David, K. K., Andrabi, S. A., Poirier, G. G., Dawson, V. L., & Dawson, T. M. (2011) · Science Signaling · doi:10.1126/scisignal.2000902 · Cited by 476

BID, BIM, and PUMA Are Essential for Activation of the BAX- and BAK-Dependent Cell Death Program

Ren, D., Tu, H.-C., Kim, H., Wang, G. X., Bean, G. R., Takeuchi, O., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J.-D., & Cheng, E. H.-Y. (2010) · Science · doi:10.1126/science.1190217 · Cited by 473

Mitochondrial fatty acid oxidation alterations in heart failure, ischaemic heart disease and diabetic cardiomyopathy

Fillmore, N., Mori, J., & Lopaschuk, G. D. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12475 · Cited by 468

Structural Basis of Caspase Inhibition by XIAP

Huang, Y., Park, Y. C., Rich, R. L., Segal, D., Myszka, D. G., & Wu, H. (2001) · Cell · doi:10.1016/s0092-8674(01)00273-2 · Cited by 467

Apoptosis‐inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis

Daugas, E., Nochy, D., Ravagnan, L., Loeffler, M., Susin, S. A., Zamzami, N., & Kroemer, G. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01731-2 · Cited by 466

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

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

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

The mitochondrial permeability transition: A current perspective on its identity and role in ischaemia/reperfusion injury

Halestrap, A. P., & Richardson, A. P. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.08.018 · Cited by 461

Role of the c subunit of the F O ATP synthase in mitochondrial permeability transition

Bonora, M., Bononi, A., De Marchi, E., Giorgi, C., Lebiedzinska, M., Marchi, S., Patergnani, S., Rimessi, A., Suski, J. M., Wojtala, A., et al. (2013) · Cell Cycle · doi:10.4161/cc.23599 · Cited by 458

Diastolic and Systolic Heart Failure Are Distinct Phenotypes Within the Heart Failure Spectrum

Borlaug, B. A., & Redfield, M. M. (2011) · Circulation · doi:10.1161/circulationaha.110.954388 · Cited by 456

The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3

Song, H., Liu, B., Huai, W., Yu, Z., Wang, W., Zhao, J., Han, L., Jiang, G., Zhang, L., Gao, C., et al. (2016) · Nature Communications · doi:10.1038/ncomms13727 · Cited by 451

Parthanatos, a messenger of death

David, K. K. (2009) · Frontiers in Bioscience · doi:10.2741/3297 · Cited by 450

TNF receptor 2 pathway: drug target for autoimmune diseases

Faustman, D., & Davis, M. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3030 · Cited by 446

Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain

Feng, S., Yang, Y., Mei, Y., Ma, L., Zhu, D.-E., Hoti, N., Castanares, M., & Wu, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.05.016 · Cited by 446

Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death

Vucic, D., Dixit, V. M., & Wertz, I. E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3143 · Cited by 444

Endogenous tumor necrosis factor protects the adult cardiac myocyte against ischemic-induced apoptosis in a murine model of acute myocardial infarction

Kurrelmeyer, K. M., Michael, L. H., Baumgarten, G., Taffet, G. E., Peschon, J. J., Sivasubramanian, N., Entman, M. L., & Mann, D. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.070036297 · Cited by 440

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 & Differentiation · doi:10.1038/cdd.2016.46 · Cited by 438

Sphingolipid Metabolism Cooperates with BAK and BAX to Promote the Mitochondrial Pathway of Apoptosis

Chipuk, J. E., McStay, G. P., Bharti, A., Kuwana, T., Clarke, C. J., Siskind, L. J., Obeid, L. M., & Green, D. R. (2012) · Cell · doi:10.1016/j.cell.2012.01.038 · Cited by 436

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

Pathologic Basis of Disease

Niles, N. R. (1974) · JAMA: The Journal of the American Medical Association · doi:10.1001/jama.1974.03230510076043 · Cited by 431

Macrophage migration inhibitory factor stimulates AMP-activated protein kinase in the ischaemic heart

Miller, E. J., Li, J., Leng, L., McDonald, C., Atsumi, T., Bucala, R., & Young, L. H. (2008) · Nature · doi:10.1038/nature06504 · Cited by 429

Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation

Sahara, S., Aoto, M., Eguchi, Y., Imamoto, N., Yoneda, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/43678 · Cited by 429

Myocardial Protection at a Crossroads: The Need for Translation Into Clinical Therapy

Bolli, R., Becker, L., Gross, G., Mentzer, R., Balshaw, D., & Lathrop, D. A. (2004) · Circulation Research · doi:10.1161/01.res.0000137171.97172.d7 · Cited by 428

Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum

Oakes, S. A., Scorrano, L., Opferman, J. T., Bassik, M. C., Nishino, M., Pozzan, T., & Korsmeyer, S. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408352102 · Cited by 428

Inhibition of the Sodium-Hydrogen Exchanger With Cariporide to Prevent Myocardial Infarction in High-Risk Ischemic Situations: Main Results of the GUARDIAN Trial

Théroux, P., Chaitman, B. R., Danchin, N., Erhardt, L., Meinertz, T., Schroeder, J. S., Tognoni, G., White, H. D., Willerson, J. T., & Jessel, A. (2000) · Circulation · doi:10.1161/01.cir.102.25.3032 · Cited by 428

Functional complementation between FADD and RIP1 in embryos and lymphocytes

Zhang, H., Zhou, X., McQuade, T., Li, J., Chan, F. K.-M., & Zhang, J. (2011) · Nature · doi:10.1038/nature09878 · Cited by 427

Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms

Saleh, M., Vaillancourt, J. P., Graham, R. K., Huyck, M., Srinivasula, S. M., Alnemri, E. S., Steinberg, M. H., Nolan, V., Baldwin, C. T., Hotchkiss, R. S., et al. (2004) · Nature · doi:10.1038/nature02451 · Cited by 422

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

Overexpression of Bcl-2 attenuates apoptosis and protects against myocardial I/R injury in transgenic mice

Chen, Z., Chua, C. C., Ho, Y.-S., Hamdy, R. C., & Chua, B. H. L. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.280.5.h2313 · Cited by 421

A nuclease that mediates cell death induced by DNA damage and poly(ADP-ribose) polymerase-1

Wang, Y., An, R., Umanah, G. K., Park, H., Nambiar, K., Eacker, S. M., Kim, B., Bao, L., Harraz, M. M., Chang, C., et al. (2016) · Science · doi:10.1126/science.aad6872 · Cited by 421

Membrane Remodeling Induced by the Dynamin-Related Protein Drp1 Stimulates Bax Oligomerization

Montessuit, S., Somasekharan, S. P., Terrones, O., Lucken-Ardjomande, S., Herzig, S., Schwarzenbacher, R., Manstein, D. J., Bossy-Wetzel, E., Basañez, G., Meda, P., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.017 · Cited by 420

Myocyte Death in the Failing Human Heart Is Gender Dependent

Guerra, S., Leri, A., Wang, X., Finato, N., Di Loreto, C., Beltrami, C. A., Kajstura, J., & Anversa, P. (1999) · Circulation Research · doi:10.1161/01.res.85.9.856 · Cited by 417

CaMKII determines mitochondrial stress responses in heart

Joiner, M.-L. A., Koval, O. M., Li, J., He, B. J., Allamargot, C., Gao, Z., Luczak, E. D., Hall, D. D., Fink, B. D., Chen, B., et al. (2012) · Nature · doi:10.1038/nature11444 · Cited by 409

Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation

Kraus, W. L. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.006 · Cited by 409

Ca2+- and mitochondrial-dependent cardiomyocyte necrosis as a primary mediator of heart failure

Nakayama, H., Chen, X., Baines, C. P., Klevitsky, R., Zhang, X., Zhang, H., Jaleel, N., Chua, B. H. L., Hewett, T. E., Robbins, J., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31060 · Cited by 405

Necroptosis and Inflammation

Newton, K., & Manning, G. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014830 · Cited by 402

Mechanisms of Cell Death in Heart Disease

Konstantinidis, K., Whelan, R. S., & Kitsis, R. N. (2012) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.111.224915 · Cited by 391

Functional consequences of caspase activation in cardiac myocytes

Communal, C., Sumandea, M., de Tombe, P., Narula, J., Solaro, R. J., & Hajjar, R. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092022999 · Cited by 390

Cyclophilin D controls mitochondrial pore–dependent Ca2+ exchange, metabolic flexibility, and propensity for heart failure in mice

Elrod, J. W., Wong, R., Mishra, S., Vagnozzi, R. J., Sakthievel, B., Goonasekera, S. A., Karch, J., Gabel, S., Farber, J., Force, T., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci43171 · Cited by 384

The Fas–FADD death domain complex structure unravels signalling by receptor clustering

Scott, F. L., Stec, B., Pop, C., Dobaczewska, M. K., Lee, J. J., Monosov, E., Robinson, H., Salvesen, G. S., Schwarzenbacher, R., & Riedl, S. J. (2009) · Nature · doi:10.1038/nature07606 · Cited by 384

Anti–PD-1–Related Pneumonitis during Cancer Immunotherapy

Nishino, M., Sholl, L. M., Hatabu, H., Ramaiya, N. H., & Hodi, F. S. (2015) · New England Journal of Medicine · doi:10.1056/nejmc1505197 · Cited by 373

Therapeutic applications of PARP inhibitors: Anticancer therapy and beyond

Curtin, N. J., & Szabo, C. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.006 · Cited by 369

MLKL, the Protein that Mediates Necroptosis, Also Regulates Endosomal Trafficking and Extracellular Vesicle Generation

Yoon, S., Kovalenko, A., Bogdanov, K., & Wallach, D. (2017) · Immunity · doi:10.1016/j.immuni.2017.06.001 · Cited by 368

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., Vazquez, J., Benedict, C. A., & Tschopp, J. (2009) · EMBO reports · doi:10.1038/embor.2009.109 · Cited by 367

Regulation of CD95/Fas signaling at the DISC

Lavrik, I. N., & Krammer, P. H. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.155 · Cited by 355

Hypoxia induces the expression of the pro-apoptotic gene BNIP3

Guo, K., Searfoss, G., Krolikowski, D., Pagnoni, M., Franks, C., Clark, K., Yu, K. T., Jaye, M., & Ivashchenko, Y. (2001) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4400810 · Cited by 352

ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases

Koseki, T., Inohara, N., Chen, S., & Núñez, G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.5156 · Cited by 347

Protective effects of the mechanistic target of rapamycin against excess iron and ferroptosis in cardiomyocytes

Baba, Y., Higa, J. K., Shimada, B. K., Horiuchi, K. M., Suhara, T., Kobayashi, M., Woo, J. D., Aoyagi, H., Marh, K. S., Kitaoka, H., et al. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00452.2017 · Cited by 347

Necroptosis in development and diseases

Shan, B., Pan, H., Najafov, A., & Yuan, J. (2018) · Genes & Development · doi:10.1101/gad.312561.118 · Cited by 347

Granzyme B Short-Circuits the Need for Caspase 8 Activity during Granule-Mediated Cytotoxic T-Lymphocyte Killing by Directly Cleaving Bid

Barry, M., Heibein, J. A., Pinkoski, M. J., Lee, S.-F., Moyer, R. W., Green, D. R., & Bleackley, R. C. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.11.3781-3794.2000 · Cited by 345

Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis

Yang, Q.-H., Church-Hajduk, R., Ren, J., Newton, M. L., & Du, C. (2003) · Genes & Development · doi:10.1101/gad.1097903 · Cited by 335

The E1B 19K/Bcl-2–binding Protein Nip3 is a Dimeric Mitochondrial Protein that Activates Apoptosis

Chen, G., Ray, R., Dubik, D., Shi, L., Cizeau, J., Bleackley, R. C., Saxena, S., Gietz, R. D., & Greenberg, A. H. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.12.1975 · Cited by 332

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

Amiloride delays the ischemia-induced rise in cytosolic free calcium.

Murphy, E., Perlman, M., London, R. E., & Steenbergen, C. (1991) · Circulation Research · doi:10.1161/01.res.68.5.1250 · Cited by 330

Cutting Edge: RIPK1 Kinase Inactive Mice Are Viable and Protected from TNF-Induced Necroptosis In Vivo

Polykratis, A., Hermance, N., Zelic, M., Roderick, J., Kim, C., 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 328

Apoptosis of Endothelial Cells Precedes Myocyte Cell Apoptosis in Ischemia/Reperfusion Injury

Scarabelli, T., Stephanou, A., Rayment, N., Pasini, E., Comini, L., Curello, S., Ferrari, R., Knight, R., & Latchman, D. (2001) · Circulation · doi:10.1161/01.cir.104.3.253 · Cited by 328

Necrostatin: A Potentially Novel Cardioprotective Agent?

Smith, C. C. T., 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 326

Regulation of RIPK1 activation by TAK1-mediated phosphorylation dictates apoptosis and necroptosis

Geng, J., Ito, Y., Shi, L., Amin, P., Chu, J., Ouchida, A. T., Mookhtiar, A. K., Zhao, H., Xu, D., Shan, B., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00406-w · Cited by 325

The mitochondrial permeability transition pore and its role in myocardial ischemia reperfusion injury

Ong, S.-B., Samangouei, P., Kalkhoran, S. B., & Hausenloy, D. J. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.11.005 · Cited by 323

Sequential Activation of Poly(ADP-Ribose) Polymerase 1, Calpains, and Bax Is Essential in Apoptosis-Inducing Factor-Mediated Programmed Necrosis

Moubarak, R. S., Yuste, V. J., Artus, C., Bouharrour, A., Greer, P. A., Menissier-de Murcia, J., & Susin, S. A. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02141-06 · Cited by 322

MK2 Phosphorylates RIPK1 to Prevent TNF-Induced Cell Death

Jaco, I., Annibaldi, A., Lalaoui, N., Wilson, R., Tenev, T., Laurien, L., Kim, C., Jamal, K., Wicky John, S., Liccardi, G., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.003 · Cited by 320

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

Inducible Expression of BNIP3 Provokes Mitochondrial Defects and Hypoxia-Mediated Cell Death of Ventricular Myocytes

Regula, K. M., Ens, K., & Kirshenbaum, L. A. (2002) · Circulation Research · doi:10.1161/01.res.0000029232.42227.16 · Cited by 318

NLRP3 inflammasome assembly is regulated by phosphorylation of the pyrin domain

Stutz, A., Kolbe, C.-C., Stahl, R., Horvath, G. L., Franklin, B. S., van Ray, O., Brinkschulte, R., Geyer, M., Meissner, F., & Latz, E. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20160933 · Cited by 317

RIP3, a kinase promoting necroptotic cell death, mediates adverse remodelling after myocardial infarction

Luedde, M., Lutz, M., Carter, N., Sosna, J., Jacoby, C., Vucur, M., Gautheron, J., Roderburg, C., Borg, N., Reisinger, F., et al. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu146 · Cited by 315

Granzyme B–Mediated Cytochrome C Release Is Regulated by the Bcl-2 Family Members Bid and Bax

Heibein, J. A., Goping, I. S., Barry, M., Pinkoski, M. J., Shore, G. C., Green, D. R., & Bleackley, R. C. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.10.1391 · Cited by 311

BH3-Triggered Structural Reorganization Drives the Activation of Proapoptotic BAX

Gavathiotis, E., Reyna, D. E., Davis, M. L., Bird, G. H., & Walensky, L. D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.019 · Cited by 310

Inflammation and NLRP3 Inflammasome Activation Initiated in Response to Pressure Overload by Ca 2+ /Calmodulin-Dependent Protein Kinase II δ Signaling in Cardiomyocytes Are Essential for Adverse Cardiac Remodeling

Suetomi, T., Willeford, A., Brand, C. S., Cho, Y., Ross, R. S., Miyamoto, S., & Brown, J. H. (2018) · Circulation · doi:10.1161/circulationaha.118.034621 · Cited by 304

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

Caspase Inhibition Reduces Myocyte Cell Death Induced by Myocardial Ischemia and Reperfusion In Vivo

Holly, T. A., Drincic, A., Byun, Y., Nakamura, S., Harris, K., Klocke, F. J., & Cryns, V. L. (1999) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1999.1006 · Cited by 303

Inhibition of ischemic cardiomyocyte apoptosis through targeted ablation of Bnip3 restrains postinfarction remodeling in mice

Diwan, A., Krenz, M., Syed, F. M., Wansapura, J., Ren, X., Koesters, A. G., Li, H., Kirshenbaum, L. A., Hahn, H. S., Robbins, J., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32490 · Cited by 301

Caspase-14 protects against epidermal UVB photodamage and water loss

Denecker, G., Hoste, E., Gilbert, B., Hochepied, T., Ovaere, P., Lippens, S., Van den Broecke, C., Van Damme, P., D'Herde, K., Hachem, J.-P., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1597 · Cited by 298

The pH Hypothesis of Postconditioning: Staccato Reperfusion Reintroduces Oxygen and Perpetuates Myocardial Acidosis

Cohen, M. V., Yang, X.-M., & Downey, J. M. (2007) · Circulation · doi:10.1161/circulationaha.106.675710 · Cited by 297

Mitochondrial death protein Nix is induced in cardiac hypertrophy and triggers apoptotic cardiomyopathy

Yussman, M. G., Toyokawa, T., Odley, A., Lynch, R. A., Wu, G., Colbert, M. C., Aronow, B. J., Lorenz, J. N., & Dorn, G. W. (2002) · Nature Medicine · doi:10.1038/nm719 · Cited by 296

Requiem for the ‘vulnerable plaque’

Libby, P., & Pasterkamp, G. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv349 · Cited by 295

Rheb is a Critical Regulator of Autophagy During Myocardial Ischemia: Pathophysiological Implications in Obesity and Metabolic Syndrome

Sciarretta, S., Zhai, P., Shao, D., Maejima, Y., Robbins, J., Volpe, M., Condorelli, G., & Sadoshima, J. (2012) · Circulation · doi:10.1161/circulationaha.111.078212 · Cited by 292

RIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition

Kaiser, W. J., Daley-Bauer, L. P., Thapa, R. J., Mandal, P., Berger, S. B., Huang, C., Sundararajan, A., Guo, H., Roback, L., Speck, S. H., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401857111 · Cited by 291

Programmed Necrosis, Not Apoptosis, in the Heart

Kung, G., Konstantinidis, K., & Kitsis, R. N. (2011) · Circulation Research · doi:10.1161/circresaha.110.225730 · Cited by 291

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

Bax regulates primary necrosis through mitochondrial dynamics

Whelan, R. S., Konstantinidis, K., Wei, A.-C., Chen, Y., Reyna, D. E., Jha, S., Yang, Y., Calvert, J. W., Lindsten, T., Thompson, C. B., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201608109 · Cited by 290

LUBAC-Recruited CYLD and A20 Regulate Gene Activation and Cell Death by Exerting Opposing Effects on Linear Ubiquitin in Signaling Complexes

Draber, P., Kupka, S., Reichert, M., Draberova, H., Lafont, E., de Miguel, D., Spilgies, L., Surinova, S., Taraborrelli, L., Hartwig, T., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.009 · Cited by 290

PD-1 Protects against Inflammation and Myocyte Damage in T Cell-Mediated Myocarditis

Tarrio, M. L., Grabie, N., Bu, D.-X., Sharpe, A. H., & Lichtman, A. H. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200389 · Cited by 288

Endothelial Programmed Death-1 Ligand 1 (PD-L1) Regulates CD8 + T-Cell–Mediated Injury in the Heart

Grabie, N., Gotsman, I., DaCosta, R., Pang, H., Stavrakis, G., Butte, M. J., Keir, M. E., Freeman, G. J., Sharpe, A. H., & Lichtman, A. H. (2007) · Circulation · doi:10.1161/circulationaha.107.709360 · Cited by 288

IRAK-1 bypasses priming and directly links TLRs to rapid NLRP3 inflammasome activation

Lin, K.-M., Hu, W., Troutman, T. D., Jennings, M., Brewer, T., Li, X., Nanda, S., Cohen, P., Thomas, J. A., & Pasare, C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1320294111 · Cited by 288

Cellular death in morphogenesis of the avian wing

Saunders, J. W., Gasseling, M. T., & Saunders, L. C. (1962) · Developmental Biology · doi:10.1016/0012-1606(62)90008-8 · Cited by 284

The role of Fas ligand in immune privilege

Green, D. R., & Ferguson, T. A. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35103104 · Cited by 284

TBK1 and IKKε prevent TNF-induced cell death by RIPK1 phosphorylation

Lafont, E., Draber, P., Rieser, E., Reichert, M., Kupka, S., de Miguel, D., Draberova, H., von Mässenhausen, A., Bhamra, A., Henderson, S., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0229-6 · Cited by 283

Apoptosis-Inducing Factor Substitutes for Caspase Executioners in NMDA-Triggered Excitotoxic Neuronal Death

Wang, H., Yu, S.-W., Koh, D. W., Lew, J., Coombs, C., Bowers, W., Federoff, H. J., Poirier, G. G., Dawson, T. M., & Dawson, V. L. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3461-04.2004 · Cited by 282

cFLIP regulation of lymphocyte activation and development

Budd, R. C., Yeh, W.-C., & Tschopp, J. (2006) · Nature Reviews Immunology · doi:10.1038/nri1787 · Cited by 280

INACTIVATION OF OXIDATIVE AND PHOSPHORYLATIVE SYSTEMS IN MITOCHONDRIA BY PREINCUBATION WITH PHOSPHATE AND OTHER IONS

Hunter, F. E., & Ford, L. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52312-2 · Cited by 279

Necrotic Cell Death in C. elegans Requires the Function of Calreticulin and Regulators of Ca2+ Release from the Endoplasmic Reticulum

Xu, K., Tavernarakis, N., & Driscoll, M. (2001) · Neuron · doi:10.1016/s0896-6273(01)00432-9 · Cited by 277

The Fas–FADD death domain complex structure reveals the basis of DISC assembly and disease mutations

Wang, L., Yang, J. K., Kabaleeswaran, V., Rice, A. J., Cruz, A. C., Park, A. Y., Yin, Q., Damko, E., Jang, S. B., Raunser, S., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1920 · Cited by 276

Expression and regulation of the PD-L1 immunoinhibitory molecule on microvascular endothelial cells

Eppihimer, M., Gunn, J., Freeman, G., Greenfield, E., Chernova, T., Erickson, J., & Leonard, J. (2002) · Microcirculation · doi:10.1080/713774061 · Cited by 272

Inhibition of anoxia-induced injury in heart myocytes by cyclosporin A

Nazareth, W. (1991) · Journal of Molecular and Cellular Cardiology · doi:10.1016/0022-2828(91)90181-k · Cited by 271

MicroRNA-103/107 Regulate Programmed Necrosis and Myocardial Ischemia/Reperfusion Injury Through Targeting FADD

Wang, J.-X., Zhang, X.-J., Li, Q., Wang, K., Wang, Y., Jiao, J.-Q., Feng, C., Teng, S., Zhou, L.-Y., Gong, Y., et al. (2015) · Circulation Research · doi:10.1161/circresaha.117.305781 · Cited by 268

The Mitochondrial Antiviral Protein MAVS Associates with NLRP3 and Regulates Its Inflammasome Activity

Park, S., Juliana, C., Hong, S., Datta, P., Hwang, I., Fernandes-Alnemri, T., Yu, J.-W., & Alnemri, E. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301170 · Cited by 266

Bax- or Bak-Induced Mitochondrial Fission Can Be Uncoupled from Cytochrome c Release

Sheridan, C., Delivani, P., Cullen, S. P., & Martin, S. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.002 · Cited by 265

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

BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation

Llambi, F., Wang, Y.-M., Victor, B., Yang, M., Schneider, D. M., Gingras, S., Parsons, M. J., Zheng, J. H., Brown, S. A., Pelletier, S., et al. (2016) · Cell · doi:10.1016/j.cell.2016.02.026 · Cited by 261

Caspase-14 reveals its secrets

Denecker, G., Ovaere, P., Vandenabeele, P., & Declercq, W. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709098 · Cited by 257

Co-operative and Hierarchical Binding of c-FLIP and Caspase-8: A Unified Model Defines How c-FLIP Isoforms Differentially Control Cell Fate

Hughes, M. A., Powley, I. R., Jukes-Jones, R., Horn, S., Feoktistova, M., Fairall, L., Schwabe, J. W. R., Leverkus, M., Cain, K., & MacFarlane, M. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.023 · Cited by 257

The Kinase Activity of Rip1 Is Not Required for Tumor Necrosis Factor-α-induced IκB Kinase or p38 MAP Kinase Activation or for the Ubiquitination of Rip1 by Traf2

Lee, T. H., Shank, J., Cusson, N., & Kelliher, M. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404206200 · Cited by 255

The Mitochondrial Permeability Transition

Halestrap, A. P. (2002) · Tissue Oxygenation in Acute Medicine · doi:10.1007/978-3-642-58268-4_12 · Cited by 252

Persistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase

He, J., Ford, H. C., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702357114 · Cited by 251

Phosphorylation and linear ubiquitin direct A20 inhibition of inflammation

Wertz, I. E., Newton, K., Seshasayee, D., Kusam, S., Lam, C., Zhang, J., Popovych, N., Helgason, E., Schoeffler, A., Jeet, S., et al. (2015) · Nature · doi:10.1038/nature16165 · Cited by 247

The Soluble Form of Bax Regulates Mitochondrial Fusion via MFN2 Homotypic Complexes

Hoppins, S., Edlich, F., Cleland, M. M., Banerjee, S., McCaffery, J. M., Youle, R. J., & Nunnari, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.11.030 · Cited by 243

Biallelic RIPK1 mutations in humans cause severe immunodeficiency, arthritis, and intestinal inflammation

Cuchet-Lourenço, D., Eletto, D., Wu, C., Plagnol, V., Papapietro, O., Curtis, J., Ceron-Gutierrez, L., Bacon, C. M., Hackett, S., Alsaleem, B., et al. (2018) · Science · doi:10.1126/science.aar2641 · Cited by 243

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

Immune Checkpoint Inhibitor Toxicity in 2018

Johnson, D. B., Chandra, S., & Sosman, J. A. (2018) · JAMA · doi:10.1001/jama.2018.13995 · Cited by 239

p38MAPK/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection

Menon, M. B., Gropengießer, J., Fischer, J., Novikova, L., Deuretzbacher, A., Lafera, J., Schimmeck, H., Czymmeck, N., Ronkina, N., Kotlyarov, A., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3614 · Cited by 238

Cutting Edge: TLR Signaling Licenses IRAK1 for Rapid Activation of the NLRP3 Inflammasome

Fernandes-Alnemri, T., Kang, S., Anderson, C., Sagara, J., Fitzgerald, K. A., & Alnemri, E. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301681 · Cited by 237

X-linked Inhibitor of Apoptosis Protein (XIAP) Inhibits Caspase-3 and -7 in Distinct Modes

Suzuki, Y., Nakabayashi, Y., Nakata, K., Reed, J. C., & Takahashi, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102415200 · Cited by 235

Autophagy is an adaptive response in desmin-related cardiomyopathy

Tannous, P., Zhu, H., Johnstone, J. L., Shelton, J. M., Rajasekaran, N. S., Benjamin, I. J., Nguyen, L., Gerard, R. D., Levine, B., Rothermel, B. A., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706802105 · Cited by 233

Activation of NF-κB by XIAP, the X Chromosome-linked Inhibitor of Apoptosis, in Endothelial Cells Involves TAK1

Hofer-Warbinek, R., Schmid, J. A., Stehlik, C., Binder, B. R., Lipp, J., & de Martin, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910346199 · Cited by 231

Structural Basis of Caspase Inhibition by XIAP Differential Roles of the Linker versus the BIR Domain

Huang, Y. (2001) · Cell · doi:10.1016/s0092-8674(02)02075-5 · Cited by 230

Characterization of a Novel Human Serine Protease That Has Extensive Homology to Bacterial Heat Shock Endoprotease HtrA and Is Regulated by Kidney Ischemia

Faccio, L., Fusco, C., Chen, A., Martinotti, S., Bonventre, J. V., & Zervos, A. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2581 · Cited by 228

Fas pathway is a critical mediator of cardiac myocyte death and MI during ischemia-reperfusion in vivo

Lee, P., Sata, M., Lefer, D. J., Factor, S. M., Walsh, K., & Kitsis, R. N. (2003) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00777.2002 · Cited by 226

NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22

Spalinger, M. R., Kasper, S., Gottier, C., Lang, S., Atrott, K., Vavricka, S. R., Scharl, S., Gutte, P. M., Grütter, M. G., Beer, H.-D., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci83669 · Cited by 226

The molecular and metabolic landscape of iron and ferroptosis in cardiovascular disease

Fang, X., Ardehali, H., Min, J., & Wang, F. (2023) · Nature Reviews Cardiology · doi:10.1038/s41569-022-00735-4 · Cited by 1,081

Alox15/15-HpETE Aggravates Myocardial Ischemia-Reperfusion Injury by Promoting Cardiomyocyte Ferroptosis

Cai, W., Liu, L., Shi, X., Liu, Y., Wang, J., Fang, X., Chen, Z., Ai, D., Zhu, Y., & Zhang, X. (2023) · Circulation · doi:10.1161/circulationaha.122.060257 · Cited by 445

Thrombin induces ACSL4-dependent ferroptosis during cerebral ischemia/reperfusion

Tuo, Q.-Z., Liu, Y., Xiang, Z., Yan, H.-F., Zou, T., Shu, Y., Ding, X.-L., Zou, J.-J., Xu, S., Tang, F., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00917-z · Cited by 330

ALOX15-launched PUFA-phospholipids peroxidation increases the susceptibility of ferroptosis in ischemia-induced myocardial damage

Ma, X.-H., Liu, J.-H.-Z., Liu, C.-Y., Sun, W.-Y., Duan, W.-J., Wang, G., Kurihara, H., He, R.-R., Li, Y.-F., Chen, Y., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01090-z · Cited by 281

Immune checkpoint inhibitor–associated myocarditis: manifestations and mechanisms

Moslehi, J., Lichtman, A. H., Sharpe, A. H., Galluzzi, L., & Kitsis, R. N. (2021) · Journal of Clinical Investigation · doi:10.1172/jci145186 · Cited by 237