RIP3 mediates the embryonic lethality of caspase-8-deficient mice

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216

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

Cho, Y., Challa, S., Moquin, D., Genga, R., Ray, T. D., Guildford, M., & Chan, F. K.-M. (2009) · Cell · doi:10.1016/j.cell.2009.05.037 · Cited by 2,435

Receptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-α

He, S., Wang, L., Miao, L., Wang, T., Du, F., Zhao, L., & Wang, X. (2009) · Cell · doi:10.1016/j.cell.2009.05.021 · Cited by 2,214

Fas triggers an alternative, caspase-8–independent cell death pathway using the kinase RIP as effector molecule

Holler, N., Zaru, R., Micheau, O., Thome, M., Attinger, A., Valitutti, S., Bodmer, J.-L., Schneider, P., Seed, B., & Tschopp, J. (2000) · Nature Immunology · doi:10.1038/82732 · Cited by 1,987

RIP3, an Energy Metabolism Regulator That Switches TNF-Induced Cell Death from Apoptosis to Necrosis

Zhang, D.-W., Shao, J., Lin, J., Zhang, N., Lu, B.-J., Lin, S.-C., Dong, M.-Q., & Han, J. (2009) · Science · doi:10.1126/science.1172308 · Cited by 1,931

Restoration of p53 function leads to tumour regression in vivo

Ventura, A., Kirsch, D. G., McLaughlin, M. E., Tuveson, D. A., Grimm, J., Lintault, L., Newman, J., Reczek, E. E., Weissleder, R., & Jacks, T. (2007) · Nature · doi:10.1038/nature05541 · Cited by 1,820

Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally.

Varfolomeev, E., Schuchmann, M., Luria, V., Chiannilkulchai, N., Beckmann, J., Mett, I., Rebrikov, D., Brodianski, V. M., Kemper, O., Kollet, O., et al. (1998) · Immunity · doi:10.1016/s1074-7613(00)80609-3 · Cited by 1,332

Regulation of an ATG7 - beclin 1 Program of Autophagic Cell Death by Caspase-8

Yu, L., Alva, A. S., Su, H. C., Dutt, P., Freundt, E. C., Welsh, S. J., Baehrecke, E. H., & Lenardo, M. J. (2004) · Science · doi:10.1126/science.1096645 · Cited by 1,249

Identification of Lps2 as a key transducer of MyD88-independent TIR signalling

Hoebe, K. H. N., Du, X., Georgel, P., Janssen, E. M., Tabeta, K., Kim, S. O., Goode, J., Lin, P., Mann, N., Mudd, S., et al. (2003) · Nature · doi:10.1038/nature01889 · Cited by 1,232

The many roles of FAS receptor signaling in the immune system

Strasser, A., Jost, P. J., & Nagata, S. (2009) · Immunity · doi:10.1016/j.immuni.2009.01.001 · Cited by 968

Cell death signaling and immune regulation: new perspectives on targeted therapy for sepsis

Wu, H., Cui, J., Huang, J., Feng, Y., Zhao, J., Zhu, Y., Deng, X., Li, X., Zhang, W., & Wang, C. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00784-w · Cited by 32

Targeting RIP Kinases in Chronic Inflammatory Disease

Speir, M., Djajawi, T. M., Conos, S. A., Tye, H., & Lawlor, K. E. (2021) · Biomolecules · doi:10.3390/biom11050646 · Cited by 30

Caspases Switch off the m 6 A RNA Modification Pathway to Foster the Replication of a Ubiquitous Human Tumor Virus

Zhang, K., Zhang, Y., Maharjan, Y., Sugiokto, F. G., Wan, J., & Li, R. (2021) · mBio · doi:10.1128/mbio.01706-21 · Cited by 29

Role of programmed necrosis and cell death in intestinal inflammation

Dagenais, M., Douglas, T., & Saleh, M. (2014) · Current Opinion in Gastroenterology · doi:10.1097/mog.0000000000000117 · Cited by 30

Strategies Used by Bacteria to Grow in Macrophages

Mitchell, G., Chen, C., & Portnoy, D. A. (2017) · ASM Press eBooks · doi:10.1128/9781555819194.ch40 · Cited by 29

Caspase-8 inactivation in T cells increases necroptosis and suppresses autoimmunity in Bim−/− mice

Bohgaki, T., Mozo, J., Salmena, L., Matysiak‐Zablocki, E., Bohgaki, M., Sanchez, O. H., Strasser, A., Hakem, A., & Hakem, R. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201103053 · Cited by 31

Regulation of RIPK1 Phosphorylation: Implications for Inflammation, Cell Death, and Therapeutic Interventions

Du, J., & Wang, Z. (2024) · Biomedicines · doi:10.3390/biomedicines12071525 · Cited by 28

Induced Necroptosis and Its Role in Cancer Immunotherapy

Zhang, Z., Zhang, F., Xie, W., Niu, Y., Wang, H., Li, G., Zhao, L., Wang, X., & Xie, W. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910760 · Cited by 28

Programmed cardiomyocyte death in myocardial infarction

Wu, H., Lan, Q., He, Y.-X., Xue, J.-Y., Liu, H., Zou, Y., Liu, P., Luo, G., Chen, M., & Liu, M. (2025) · APOPTOSIS · doi:10.1007/s10495-025-02075-3 · Cited by 29

Commensal Microbiota Are Required for Systemic Inflammation Triggered by Necrotic Dendritic Cells

Young, J. A., He, T. H., Reizis, B., & Winoto, A. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.04.033 · Cited by 28

Down the rabbit hole: Is necroptosis truly an innate response to infection?

Pearson, J. S., & Murphy, J. M. (2017) · Cellular Microbiology · doi:10.1111/cmi.12750 · Cited by 28

Caspase-8 mutations associated with head and neck cancer differentially retain functional properties related to TRAIL-induced apoptosis and cytokine induction

Cui, Z., Dabas, H., Leonard, B. C., Shiah, J. V., Grandis, J. R., & Johnson, D. E. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04066-z · Cited by 28

N4BP1 coordinates ubiquitin-dependent crosstalk within the IκB kinase family to limit Toll-like receptor signaling and inflammation

Gitlin, A. D., Maltzman, A., Kanno, Y., Heger, K., Reja, R., Schubert, A. F., Wierciszewski, L. J., Pantua, H., Kapadia, S. B., Harris, S. F., et al. (2024) · Immunity · doi:10.1016/j.immuni.2024.04.004 · Cited by 28

Masters, marionettes and modulators: intersection of pathogen virulence factors and mammalian death receptor signaling

Silke, J., & Hartland, E. L. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2013.05.011 · Cited by 28

Necroptosis Is Involved in CD4+ T Cell-Mediated Microvascular Endothelial Cell Death and Chronic Cardiac Allograft Rejection

Kwok, C. Y., Pavlosky, A., Lian, D., Jiang, J., Huang, X., Yin, Z., Liu, W., Haig, A. R., Jevnikar, A. M., & Zhang, Z. (2016) · Transplantation · doi:10.1097/tp.0000000000001578 · Cited by 29

The flick of a switch: which death program to choose?

Vandenabeele, P., & Melino, G. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.65 · Cited by 28

Inflammatory cell death PANoptosis is induced by the anti-cancer curaxin CBL0137 via eliciting the assembly of ZBP1-associated PANoptosome

Li, Y., Zhou, Z.-Y., Liang, Y., You, Y.-P., Ke, H.-Y., Yuan, T., Yang, H., Xu, R., Xu, L., Ouyang, D., et al. (2024) · Inflammation Research · doi:10.1007/s00011-024-01858-9 · Cited by 27

Implications of inflammatory cell death-PANoptosis in health and disease

Bae, H., Jang, Y., Karki, R., & Han, J. (2024) · Archives of Pharmacal Research · doi:10.1007/s12272-024-01506-0 · Cited by 28

Contribution of cell death signaling to blood vessel formation

Tisch, N., & de Almodóvar, C. R. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03738-x · Cited by 27

Update of cellular responses to the efferocytosis of necroptosis and pyroptosis

Purnama, C. A., Meiliana, A., Barliana, M. I., & Lestari, K. (2023) · Cell Division · doi:10.1186/s13008-023-00087-6 · Cited by 27

An overview of programmed cell death: Apoptosis and pyroptosis—Mechanisms, differences, and significance in organism physiology and pathophysiology

Kowalski, S., Karska, J., Łapińska, Z., Hetnał, B., Saczko, J., & Kulbacka, J. (2023) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30413 · Cited by 27

Cloaked in ubiquitin, a killer hides in plain sight: the molecular regulation of RIPK 1

Justus, S. J., & Ting, A. T. (2015) · Immunological Reviews · doi:10.1111/imr.12304 · Cited by 27

Signaling by cell surface death receptors: Alterations in head and neck cancer

Leonard, B. C., & Johnson, D. E. (2017) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.10.006 · Cited by 29

Crucial Roles of the RIP Homotypic Interaction Motifs of RIPK3 in RIPK1-Dependent Cell Death and Lymphoproliferative Disease

Zhang, H., Li, X., Li, M., Li, F., Li, F., Wang, L., Zhang, Y., Zhang, Y., Luo, Y., Wang, H., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107650 · Cited by 27

Defective prelamin A processing promotes unconventional necroptosis driven by nuclear RIPK1

Yang, Y., Zhang, J., Lv, M., Cui, N., Shan, B., Sun, Q., Yan, L., Zhang, M., Zou, C., Yuan, J., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01374-2 · Cited by 27

Developmental checkpoints guarded by regulated necrosis

Dillon, C. P., Tummers, B., Baran, K., & Green, D. R. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2188-z · Cited by 28

Synthetic Biology Reveals the Uniqueness of the RIP Kinase Domain

Chirieleison, S. M., Kertesy, S. B., & Abbott, D. W. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1502631 · Cited by 26

The NuRD chromatin-remodeling complex enzyme CHD4 prevents hypoxia-induced endothelial Ripk3 transcription and murine embryonic vascular rupture

Colijn, S., Gao, S., Ingram, K. G., Menendez, M. T., Muthukumar, V., Silasi‐Mansat, R., Chmielewska, J. J., Hinsdale, M. E., Lupu, F., & Griffin, C. T. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0376-8 · Cited by 26

A unique death pathway keeps RIPK1 D325A mutant mice in check at embryonic day 10.5

Zhang, Y., Huang, K., Zhang, Y., Tao, H., Li, L., Ruan, C., Sun, Y.-H., Shi, W., Han, W., Wu, S., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001304 · Cited by 26

Unwinding the modalities of necrosome activation and necroptosis machinery in neurological diseases

Gupta, R. V., Kumari, S., Tripathi, R. S., Ambasta, R. K., & Kumar, P. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101855 · Cited by 27

Acute lung injury: a view from the perspective of necroptosis

Dong, J., Liu, W., Liu, W., Wen, Y., Liu, Q., Wang, H.-T., Xiang, G.-H., Liu, Y., & Hao, H. (2024) · Inflammation Research · doi:10.1007/s00011-024-01879-4 · Cited by 27

Antiviral T Cell Response Triggers Cytomegalovirus Hepatitis in Mice

Livingston‐Rosanoff, D., Daley‐Bauer, L. P., García, A., McCormick, A. L., Huang, J., & Mocarski, E. S. (2012) · Journal of Virology · doi:10.1128/jvi.01752-12 · Cited by 26

Novel Ser/Thr Protein Phosphatases in Cell Death Regulation

Sun, H., & Wang, Y. (2012) · Physiology · doi:10.1152/physiol.00034.2011 · Cited by 28

Necroptosis of Intestinal Epithelial Cells Induces Type 3 Innate Lymphoid Cell-Dependent Lethal Ileitis

Shindo, R., Ohmuraya, M., Komazawa‐Sakon, S., Miyake, S., Deguchi, Y., Yamazaki, S., Nishina, T., Yoshimoto, T., Kakuta, S., Koike, M., et al. (2019) · iScience · doi:10.1016/j.isci.2019.05.011 · Cited by 26

Caspase-8 restricts antiviral CD8 T cell hyperaccumulation

Feng, Y., Daley‐Bauer, L. P., Roback, L., Guo, H., Koehler, H. S., Potempa, M., Lanier, L. L., & Mocarski, E. S. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904319116 · Cited by 26

SPATA2: more than a missing link

Schlicher, L., Brauns‐Schubert, P., Schubert, F., & Maurer, U. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.26 · Cited by 26

Hierarchical Cell Death Program Disrupts the Intracellular Niche Required for Burkholderia thailandensis Pathogenesis

Place, D. E., Christgen, S. L., Tuladhar, S., Vogel, P., Malireddi, R. K. S., & Kanneganti, T. (2021) · mBio · doi:10.1128/mbio.01059-21 · Cited by 25

Myeloid caspase-8 restricts RIPK3-dependent proinflammatory IL-1β production and CD4 T cell activation in autoimmune demyelination

Kim, S.-J., Lu, H. C., Steelman, A. J., & Li, J. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2117636119 · Cited by 25

Combinatorial treatment of CD95L and gemcitabine in pancreatic cancer cells induces apoptotic and RIP1-mediated necroptotic cell death network

Pietkiewicz, S., Eils, R., Krammer, P. H., Giese, N., & Lavrik, I. N. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.10.005 · Cited by 25

An updated view on the functions of caspases in inflammation and immunity

Songane, M., Khair, M., & Saleh, M. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.01.001 · Cited by 27

A novel function of RIP1 in postnatal development and immune homeostasis by protecting against RIP3-dependent necroptosis and FADD-mediated apoptosis

Dowling, J. P., Nair, A., & Zhang, J. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00012 · Cited by 24

Cell Death Pathways in Mutant Rhodopsin Rat Models Identifies Genotype-Specific Targets Controlling Retinal Degeneration

viringipurampeer, I. A., Gregory, C. Y., Metcalfe, A. L., Bashar, E., Moritz, O. L., & Gregory-Evans, K. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1192-8 · Cited by 27

Cell death in culture: Molecular mechanisms, detections, and inhibition strategies

Patil, A. A., Bhor, S. A., & Rhee, W. J. (2020) · Journal of Industrial and Engineering Chemistry · doi:10.1016/j.jiec.2020.08.009 · Cited by 27

Hearing Impairment in a Mouse Model of Diabetes Is Associated with Mitochondrial Dysfunction, Synaptopathy, and Activation of the Intrinsic Apoptosis Pathway

Lyu, A., Kim, T., Shin, S.-A., Kim, E.-H., Yu, Y., Gajbhiye, A., Kwon, H.-C., Je, A. R., Huh, Y. H., Park, M. J., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168807 · Cited by 24

Advances in the Study of the Ubiquitin-Editing Enzyme A20

Bai, W., Huo, S., Li, J., & Shao, J. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.845262 · Cited by 25

RIPK3 and caspase 8 collaborate to limit herpes simplex encephalitis

Guo, H., Koehler, H. S., Mocarski, E. S., & Dix, R. D. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010857 · Cited by 24

Inactivation of caspase 8 in liver parenchymal cells confers protection against murine obstructive cholestasis

Cubero, F. J., Peng, J., Liao, L., Su, H., Zhao, G., Zoubek, M. E., Macías‐Rodríguez, R. U., Ruiz‐Margáin, A., Reißing, J., Zimmermann, H. W., et al. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2018.08.015 · Cited by 24

A critical role for cellular inhibitor of protein 2 (cIAP2) in colitis-associated colorectal cancer and intestinal homeostasis mediated by the inflammasome and survival pathways

Dagenais, M., Dupaul-Chicoine, J., Champagne, C., Skeldon, A. M., Morizot, A., & Saleh, M. (2015) · Mucosal Immunology · doi:10.1038/mi.2015.46 · Cited by 24

Targeting caspase-8: a new strategy for combating hepatocellular carcinoma

Chen, H., Lin, Y., Chen, J., Luo, X., Kan, Y., He, Y., Zhu, R., Jin, J., Li, D., Wang, Y., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1501659 · Cited by 23

The conservation and uniqueness of the caspase family in the basal chordate, amphioxus

Xu, L., Yuan, S., Li, J., Ruan, J., Huang, S., Yang, M., Huang, H., Chen, S., Ren, Z., & Xu, A. (2011) · BMC Biology · doi:10.1186/1741-7007-9-60 · Cited by 23

Complex role of nicotinamide adenine dinucleotide in the regulation of programmed cell death pathways

Preyat, N., & Léo, O. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.08.110 · Cited by 23

Kuguaglycoside C , a constituent of M omordica charantia, induces caspase‐independent cell death of neuroblastoma cells

Tabata, K., Hamano, A., Akihisa, T., & Suzuki, T. (2012) · Cancer Science · doi:10.1111/cas.12021 · Cited by 23

CrmA orthologs from diverse poxviruses potently inhibit caspases-1 and -8, yet cleavage site mutagenesis frequently produces caspase-1-specific variants

Bloomer, D. T., Kitevska, T., Pantaki-Eimany, D., Ji, Y., Miles, M. A., Heras, B., & Hawkins, C. J. (2019) · Biochemical Journal · doi:10.1042/bcj20190202 · Cited by 23

Multiple ways to die: Non-apoptotic forms of cell death

Tsujimoto, Y. (2012) · Acta Oncologica · doi:10.3109/0284186x.2011.648340 · Cited by 23

Triad3a induces the degradation of early necrosome to limit RipK1-dependent cytokine production and necroptosis

Alturki, N. A., McComb, S., Ariana, A., Rijal, D., Korneluk, R. G., Sun, S., Alnemri, E. S., & Sad, S. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0672-0 · Cited by 25

Processes exacerbating apoptosis in non-alcoholic steatohepatitis

Afonso, M. B., Castro, R. E., & Rodrigues, C. M. P. (2019) · Clinical Science · doi:10.1042/cs20190068 · Cited by 25

In situ vaccination caused by diverse irradiation-driven cell death programs

Wang, Y., Li, Y., Yang, Y., Swift, M. L., Zhang, Z., Wu, S., Sun, Y., & Yang, K. (2024) · Theranostics · doi:10.7150/thno.86004 · Cited by 25

The importance of murine phospho-MLKL-S345 in situ detection for necroptosis assessment in vivo

Kelepouras, K., Saggau, J., Varanda, A. B., Zrilić, M., Kiefer, C., Rakhsh-Khorshid, H., Lisewski, I., Uranga-Murillo, I., Arias, M. A., Pardo, J., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01313-6 · Cited by 23

RIPK3 modulates growth factor receptor expression in endothelial cells to support angiogenesis

Gao, S., & Griffin, C. T. (2021) · Angiogenesis · doi:10.1007/s10456-020-09763-5 · Cited by 22

Fas/CD95 Signaling Pathway in Damage-Associated Molecular Pattern (DAMP)-Sensing Receptors

Galli, G., Vacher, P., Ryffel, B., Blanco, P., & Legembre, P. (2022) · Cells · doi:10.3390/cells11091438 · Cited by 23

Evaluation of Caspase Activation to Assess Innate Immune Cell Death

Han, J., Tweedell, R. E., & Kanneganti, T. (2023) · Journal of Visualized Experiments · doi:10.3791/64308 · Cited by 23

IAP antagonists sensitize murine osteosarcoma cells to killing by TNFα

Shekhar, T. M., Miles, M. A., Gupte, A., Taylor, S., Tascone, B., Walkley, C. R., & Hawkins, C. J. (2016) · Oncotarget · doi:10.18632/oncotarget.8980 · Cited by 22

Endosulfan inducing apoptosis and necroptosis through activation RIPK signaling pathway in human umbilical vascular endothelial cells

Zhang, L., Wei, J., Ren, L., Zhang, J., Yang, M. G., Li, J., Wang, J., Sun, Z., & Zhou, X. (2016) · Environmental Science and Pollution Research · doi:10.1007/s11356-016-7652-7 · Cited by 23

RIPK1-Associated Inborn Errors of Innate Immunity

Zhang, J., Jin, T., Aksentijevich, I. A., & Zhou, Q. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.676946 · Cited by 22

Pharmacological inhibition of caspase‐8 limits lung tumour outgrowth

Terlizzi, M., Crescenzo, V. G. D., Perillo, G., Galderisi, A., Pinto, A., & Sorrentino, R. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13176 · Cited by 22

RIPK3 in necroptosis and cancer

Morgan, M. J., & Kim, Y. (2025) · Molecules and Cells · doi:10.1016/j.mocell.2025.100199 · Cited by 21

Bypassing the guardian: regulated cell death pathways in p53-mutant cancers

Chung, J., & Knutson, B. A. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00751-5 · Cited by 22

Regulation of inflammatory processes by caspases

Beltrán‐Visiedo, M., Soler-Agesta, R., Sarosiek, K. A., Green, D. R., & Galluzzi, L. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00869-6 · Cited by 23

Detection of Necroptosis by Phospho-RIPK3 Immunohistochemical Labeling

Webster, J. D., Solon, M., Haller, S., & Newton, K. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8754-2_15 · Cited by 21

Herpes simplex virus 1 ICP6 impedes TNF receptor 1–induced necrosome assembly during compartmentalization to detergent-resistant membrane vesicles

Ali, M., Roback, L., & Mocarski, E. S. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004651 · Cited by 22

RIP1/RIP3/MLKL Mediates Myocardial Function Through Necroptosis in Experimental Autoimmune Myocarditis

Wu, Y., Zheng, Z., Cao, X., Yang, Q., Norton, V., Adini, A., Maiti, A. K., Adini, I., & Wu, H. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.696362 · Cited by 21

Albicanol inhibits the toxicity of profenofos to grass carp hepatocytes cells through the ROS/PTEN/PI3K/AKT axis

Xuan, L., Jinming, G., Guan, Y., Wang, H., Wu, H., & Chang, Y. (2021) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2021.11.014 · Cited by 21

Role of AMPK in Myocardial Ischemia‐Reperfusion Injury‐Induced Cell Death in the Presence and Absence of Diabetes

Kandula, N., Kumar, S., Mandlem, V., Siddabathuni, A., Singh, S. K., & Kosuru, R. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7346699 · Cited by 23

cFLIPS regulates alternative NLRP3 inflammasome activation in human monocytes

Gao, Y., Yu, S., Chen, M., Wang, X., Pan, L., Wei, B. K., & Meng, G. (2023) · Cellular and Molecular Immunology · doi:10.1038/s41423-023-01077-y · Cited by 21

The caspase-8/RIPK3 signaling axis in antigen presenting cells controls the inflammatory arthritic response

Dominguez, S. T., Montgomery, A. B., Haines, G. K., Bloomfield, C. L., & Cuda, C. M. (2017) · Arthritis Research & Therapy · doi:10.1186/s13075-017-1436-4 · Cited by 21

Senescence and cell death in chronic liver injury: roles and mechanisms underlying hepatocarcinogenesis

Xiao, M., Chen, W., Wang, C., Wu, Y., Zhu, S., Zeng, C., Cai, Y., Liu, C., & He, Z. (2017) · Oncotarget · doi:10.18632/oncotarget.23622 · Cited by 21

Use of a glycerin-based gel sheeting in scar management.

Baum, T. M., & Busuito, M. J. (1998) · PubMed · Cited by 21

Necroptotic cell death consequences and disease relevance

Vince, J. E., Davidson, N., & Tanzer, M. C. (2025) · Nature Immunology · doi:10.1038/s41590-025-02298-1 · Cited by 21

Emerging therapeutic targets for Gaucher disease

Vitner, E. B., Vardi, A., Cox, T. M., & Futerman, A. H. (2014) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2014.981530 · Cited by 20

Necroptosis in human cancers with special emphasis on oral squamous cell carcinoma

Krishnan, R. P., Pandiar, D., Ramani, P., & Jayaraman, S. (2023) · Journal of Stomatology Oral and Maxillofacial Surgery · doi:10.1016/j.jormas.2023.101565 · Cited by 21

Myeloid OTULIN deficiency couples RIPK3-dependent cell death to Nlrp3 inflammasome activation and IL-1β secretion

Doglio, M. G., Verboom, L., Sosoranga, E. R., Frising, U. C., Asaoka, T., Gansemans, Y., Nieuwerburgh, F. V., Loo, G., & Wullaert, A. (2023) · Science Immunology · doi:10.1126/sciimmunol.adf4404 · Cited by 20

NEMO regulates a cell death switch in TNF signaling by inhibiting recruitment of RIPK3 to the cell death-inducing complex II

Pescatore, A., Esposito, E., Dráber, P., Walczak, H., & Ursini, M. V. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.245 · Cited by 20

Detecting Anastasis In Vivo by CaspaseTracker Biosensor

Tang, H. M., Fung, M. C., & Tang, H. L. (2018) · Journal of Visualized Experiments · doi:10.3791/54107 · Cited by 20

A Genetic System for Biasing the Sex Ratio in Mice

Yosef, I., Edry‐Botzer, L., Globus, R., Shlomovitz, I., Munitz, A., Gerlic, M., & Qimron, U. (2019) · EMBO Reports · doi:10.15252/embr.201948269 · Cited by 20

Caspase-1 activity affects AIM2 speck formation/stability through a negative feedback loop

Juruj, C., Lelogeais, V., Pierini, R., Perret, M., Py, B. F., Jamilloux, Y., Brož, P., Ader, F., Faure, M., & Henry, T. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00014 · Cited by 22

Caspase-8 is essential for maintaining chromosomal stability and suppressing B-cell lymphomagenesis

Hakem, A., Ghamrasni, S. E., Maire, G., Lemmers, B., Karásková, J., Jurisicova, A., Sanchez, O. H., Squire, J. A., & Hakem, R. (2012) · Blood · doi:10.1182/blood-2011-07-367532 · Cited by 20

Unravelling the Role of PANoptosis in Liver Diseases: Mechanisms and Therapeutic Implications

Xiong, W., Li, J., Tian, A., & Mao, X. (2025) · Liver International · doi:10.1111/liv.70000 · Cited by 19

Mitochondria as Regulators of Nonapoptotic Cell Death in Cancer

Malla, S., Neupane, R., Sood, S., Hussein, N. A., Abou-Dahech, M. S., Terrero, D., Ashby, C. R., Babu, R. J., & Tiwari, A. K. (2025) · MedComm · doi:10.1002/mco2.70244 · Cited by 20

Cell death proteins in sepsis: key players and modern therapeutic approaches

Yang, C. S., Coopersmith, C. M., & Lyons, J. D. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1347401 · Cited by 19

A microfluidics platform for simultaneous evaluation of sensitivity and side effects of anti-cancer drugs using a three-dimensional culture method

Kobayashi, Y., Hashizume, H., Takiguchi, S., Ji, J., Kawano, R., Koiwai, K., Yamamoto, H., Elbadawy, M., Omatsu, T., Abugomaa, A., et al. (2025) · Scientific Reports · doi:10.1038/s41598-024-84297-0 · Cited by 20

Apaf1 apoptotic function critically limits Sonic hedgehog signaling during craniofacial development

Long, A. B., Kaiser, W. J., Mocarski, E. S., & Caspary, T. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.97 · Cited by 19

Caspases and immunity in a deadly grip

Rodrigue‐Gervais, I. G., & Saleh, M. (2012) · Trends in Immunology · doi:10.1016/j.it.2012.09.005 · Cited by 20

Programmed cell death with a necrotic-like phenotype

Morgan, M. J., & Liu, Z.-G. (2013) · BioMolecular Concepts · doi:10.1515/bmc-2012-0056 · Cited by 20

An unexpected turn of fortune: targeting TRAIL-Rs in KRAS-driven cancer

von Karstedt, S., & Walczak, H. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-0249-4 · Cited by 19

RIPK3 Promotes Mefv Expression and Pyrin Inflammasome Activation via Modulation of mTOR Signaling

Sharma, D., Malik, A., Balakrishnan, A., Malireddi, R. K. S., & Kanneganti, T. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000244 · Cited by 19

RIPK1/RIPK3-Mediated Necroptosis is Involved in Sevoflurane-Induced Neonatal Neurotoxicity in the Rat Hippocampus

Xu, R., Zhu, Y., Jia, J., Li, W., & Lu, Y. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-021-01098-z · Cited by 19

Programmed Cell Death of Endothelial Cells in Myocardial Infarction and Its Potential Therapeutic Strategy

Wu, M., Huang, Z., Zeng, L., Wang, C., & Wang, D. (2022) · Cardiology Research and Practice · doi:10.1155/2022/6558060 · Cited by 19

Cellular FLICE-Inhibitory Protein Regulates Tissue Homeostasis

Nakano, H., Piao, X., Shindo, R., & Komazawa‐Sakon, S. (2015) · Current topics in microbiology and immunology · doi:10.1007/82_2015_448 · Cited by 19

Regulated Cell Death in Urinary Malignancies

Nie, Z., Chen, M., Gao, Y., Huang, D., Cao, H., Peng, Y., Guo, N., & Zhang, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.789004 · Cited by 18

Programmed Cell Death-Dependent Host Defense in Ocular Herpes Simplex Virus Infection

Guo, H., Koehler, H. S., Dix, R. D., & Mocarski, E. S. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.869064 · Cited by 20

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

Abstract SY27-01: Cutting both ways: Why FADD, FLIP, and Caspase-8 are required for embryonic development

Green, D. R. (2012) · Cancer Research · doi:10.1158/1538-7445.am2012-sy27-01

Apoptosis meets necrosis

Peter, M. E. (2011) · Nature · doi:10.1038/471310a · Cited by 191

Cleavage of RIPK1 by caspase-8 is crucial for limiting apoptosis and necroptosis

Newton, K., Wickliffe, K. E., Dugger, D. L., Maltzman, A., Roose‐Girma, M., Dohse, M., Kömüves, L. G., Webster, J. D., & Dixit, V. M. (2019) · Nature · doi:10.1038/s41586-019-1548-x · Cited by 559

Caspase-8 is the molecular switch for apoptosis, necroptosis and pyroptosis

Fritsch, M., Günther, S. D., Schwarzer, R., Albert, M., Schorn, F., Werthenbach, J. P., Schiffmann, L. M., Stair, N., Stocks, H., Seeger, J. M., et al. (2019) · Nature · doi:10.1038/s41586-019-1770-6 · Cited by 1,122