Old, new and emerging functions of caspases

The Inflammasome

Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066

Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis

Li, H., Zhu, H., Xu, C.-J., & Yuan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81590-1 · Cited by 4,445

Mutation of the mouse klotho gene leads to a syndrome resembling ageing

Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837

Self-eating and self-killing: crosstalk between autophagy and apoptosis

Maiuri, M. C., Zalckvar, E., Kimchi, A., & Kroemer, G. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2239 · Cited by 3,638

Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009

Kroemer, G., Galluzzi, L., Vandenabeele, P., Abrams, J., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., El-Deiry, W. S., Golstein, P., Green, D. R., et al. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2008.150 · Cited by 3,399

Pyroptosis: host cell death and inflammation

Bergsbaken, T., Fink, S. L., & Cookson, B. T. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2070 · Cited by 3,288

Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy

Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3722 · Cited by 3,219

Cryopyrin activates the inflammasome in response to toxins and ATP

Mariathasan, S., Weiss, D. S., Newton, K., McBride, J., O'Rourke, K., Roose-Girma, M., Lee, W. P., Weinrauch, Y., Monack, D. M., & Dixit, V. M. (2006) · Nature · doi:10.1038/nature04515 · Cited by 3,080

Caspase Functions in Cell Death and DiseasePreprint

McIlwain, D. R., Berger, T., & Mak, T. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008656 · Cited by 2,702

A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes

Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J. G., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,613

Mechanisms and Functions of Inflammasomes

Lamkanfi, M., & Dixit, V. M. (2014) · Cell · doi:10.1016/j.cell.2014.04.007 · Cited by 2,579

Non-canonical inflammasome activation targets caspase-11

Kayagaki, N., Warming, S., Lamkanfi, M., Walle, L. V., Louie, S., Dong, J., Newton, K., Qu, Y., Liu, J., Heldens, S., et al. (2011) · Nature · doi:10.1038/nature10558 · Cited by 2,530

The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme

Ji, Y. (1993) · Cell · doi:10.1016/0092-8674(93)90485-9 · Cited by 2,497

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

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

Inflammatory caspases are innate immune receptors for intracellular LPS

Shi, J., Zhao, Y., Wang, Y., Gao, W., Ding, J., Li, P., Hu, L., & Shao, F. (2014) · Nature · doi:10.1038/nature13683 · Cited by 2,285

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

Genetic control of programmed cell death in the nematode C. elegans

Ellis, H. (1986) · Cell · doi:10.1016/0092-8674(86)90004-8 · Cited by 1,828

Involvement of the bcl -2 Gene in Human Follicular Lymphoma

Tsujimoto, Y., Cossman, J., Jaffe, E. S., & Croce, C. M. (1985) · Science · doi:10.1126/science.3874430 · Cited by 1,787

NALP3 Forms an IL-1β-Processing Inflammasome with Increased Activity in Muckle-Wells Autoinflammatory Disorder

Agostini, L., Martinon, F., Burns, K., McDermott, M. F., Hawkins, P. N., & Tschopp, J. (2004) · Immunity · doi:10.1016/s1074-7613(04)00046-9 · Cited by 1,768

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

Altered Cytokine Export and Apoptosis in Mice Deficient in Interleukin-1β Converting Enzyme

Kuida, K., Lippke, J. A., Ku, G., Harding, M. W., Livingston, D. J., Su, M. S. S., & Flavell, R. A. (1995) · Science · doi:10.1126/science.7535475 · Cited by 1,631

Pro-inflammatory programmed cell death

Cookson, B. T., & Brennan, M. A. (2001) · Trends in Microbiology · doi:10.1016/s0966-842x(00)01936-3 · Cited by 1,422

Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock

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Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria

Miao, E. A., Leaf, I. A., Treuting, P. M., Mao, D. P., Dors, M., Sarkar, A., Warren, S. E., Wewers, M. D., & Aderem, A. (2010) · Nature Immunology · doi:10.1038/ni.1960 · Cited by 1,336

Shigella flexneri induces apoptosis in infected macrophages

Zychlinsky, A., Prévost, M., & Sansonetti, P. (1992) · Nature · doi:10.1038/358167a0 · Cited by 1,259

Caspase-1 processes IFN-γ-inducing factor and regulates LPS-induced IFN- γ production

Ghayur, T., Banerjee, S., Hugunin, M., Butler, D., Herzog, L., Carter, A. B., Quintal, L. J., Sekut, L., Talanian, R. V., Paskind, M. P., et al. (1997) · Nature · doi:10.1038/386619a0 · Cited by 1,204

The Human Protein Atlas—a tool for pathology

Pontén, F., Jirström, K., & Uhlén, M. (2008) · The Journal of Pathology · doi:10.1002/path.2440 · Cited by 1,171

Caspase‐1‐induced pyroptotic cell death

Miao, E. A., Rajan, J. V., & Aderem, A. A. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01044.x · Cited by 1,162

Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction

Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150

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

Caspase 3–mediated stimulation of tumor cell repopulation during cancer radiotherapy

Huang, Q., Li, F., Liu, X., Li, W., Shi, W., Liu, F.-F., O'Sullivan, B., He, Z., Peng, Y., Tan, A.-C., et al. (2011) · Nature Medicine · doi:10.1038/nm.2385 · Cited by 886

Caspase function in programmed cell death

Kumar, S. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402060 · Cited by 863

The Ripoptosome, a Signaling Platform that Assembles in Response to Genotoxic Stress and Loss of IAPs

Tenev, T., Bianchi, K., Darding, M., Broemer, M., Langlais, C., Wållberg, F., Zachariou, A., Lopez, J. S., MacFarlane, M., Cain, K., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.006 · Cited by 837

Caspase 8 is deleted or silenced preferentially in childhood neuroblastomas with amplification of MYCN

Teitz, T., Wei, T., Valentine, M. B., Vanin, E. F., Grenet, J. A., Valentine, V. A., Behm, F. G., Look, A. T., Lahti, J. M., & Kidd, V. J. (2000) · Nature Medicine · doi:10.1038/75007 · Cited by 809

Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency

Chun, H. J., Zheng, L., Ahmad, M., Wang, J., Speirs, C. K., Siegel, R. M., Dale, J. K., Puck, J. M., Davis, J., Hall, C. G., et al. (2002) · Nature · doi:10.1038/nature01063 · Cited by 706

Genetic Interaction of PGE2 and Wnt Signaling Regulates Developmental Specification of Stem Cells and Regeneration

Goessling, W., North, T. E., Loewer, S., Lord, A. M., Lee, S., Stoick-Cooper, C. L., Weidinger, G., Puder, M., Daley, G. Q., Moon, R. T., et al. (2009) · Cell · doi:10.1016/j.cell.2009.01.015 · Cited by 704

Murine Caspase-11, an ICE-Interacting Protease, Is Essential for the Activation of ICE

Wang, S., Miura, M., Jung, Y., Zhu, H., Li, E., & Yuan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)80943-5 · Cited by 699

Salmonella induces macrophage death by caspase‐1‐dependent necrosis

Brennan, M. A., & Cookson, B. T. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02103.x · Cited by 685

The PIDDosome, a Protein Complex Implicated in Activation of Caspase-2 in Response to Genotoxic Stress

Tinel, A., & Tschopp, J. (2004) · Science · doi:10.1126/science.1095432 · Cited by 665

Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death

Ofengeim, D., & Yuan, J. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3683 · Cited by 635

Salmonella typhimurium invasion induces apoptosis in infected macrophages.

Monack, D. M., Raupach, B., Hromockyj, A. E., & Falkow, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9833 · Cited by 621

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 598

Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme.Preprint

Kumar, S., Kinoshita, M., Noda, M., Copeland, N. G., & Jenkins, N. A. (1994) · Genes & Development · doi:10.1101/gad.8.14.1613 · Cited by 595

Identification of Bacterial Muramyl Dipeptide as Activator of the NALP3/Cryopyrin Inflammasome

Martinon, F., Agostini, L., Meylan, E., & Tschopp, J. (2004) · Current Biology · doi:10.1016/j.cub.2004.10.027 · Cited by 579

The inhibitors of apoptosis (IAPs) as cancer targets

Hunter, A. M., LaCasse, E. C., & Korneluk, R. G. (2007) · Apoptosis · doi:10.1007/s10495-007-0087-3 · Cited by 565

Regulation of proliferation, survival and apoptosis by members of the TNF superfamily

Gaur, U., & Aggarwal, B. B. (2003) · Biochemical Pharmacology · doi:10.1016/s0006-2952(03)00490-8 · Cited by 556

Identification of a set of genes with developmentally down-regulated expression in the mouse brain

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Caspase 3 activity is required for skeletal muscle differentiation

Fernando, P., Kelly, J. F., Balazsi, K., Slack, R. S., & Megeney, L. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162172899 · Cited by 551

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

Caspase-3 Activation via Mitochondria Is Required for Long-Term Depression and AMPA Receptor Internalization

Li, Z., Jo, J., Jia, J., Lo, S., Whitcomb, D. J., Jiao, S., Cho, K., & Sheng, M. (2010) · Cell · doi:10.1016/j.cell.2010.03.053 · Cited by 533

Apoptotic Cells Activate the “Phoenix Rising” Pathway to Promote Wound Healing and Tissue Regeneration

Li, F., Huang, Q., Jiang, C., Peng, Y., Roop, D. R., Bedford, J. S., & Li, C. (2010) · Science Signaling · doi:10.1126/scisignal.2000634 · Cited by 510

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

Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunityPreprint

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Down-regulation of caspase 3 in breast cancer: a possible mechanism for chemoresistance

Devarajan, E., Şahin, A. A., Chen, J. S., Krishnamurthy, R. R., Aggarwal, N., Brun, A.-M., Sapino, A., Zhang, F., Sharma, D., Yang, X.-H., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1206044 · Cited by 466

Caspase Activation Is Required for T Cell Proliferation

Kennedy, N. J., Kataoka, T., Tschopp, J., & Budd, R. C. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.12.1891 · Cited by 456

Inflammaging: disturbed interplay between autophagy and inflammasomes

Salminen, A., Kaarniranta, K., & Kauppinen, A. (2012) · Aging · doi:10.18632/aging.100444 · Cited by 453

Inflammation-induced tumorigenesis in the colon is regulated by caspase-1 and NLRC4

Hu, B., Elinav, E., Huber, S., Booth, C. J., Strowig, T., Jin, C., Eisenbarth, S. C., & Flavell, R. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016814108 · Cited by 452

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 434

Caspase-8 Serves Both Apoptotic and Nonapoptotic Roles1

Kang, T., Ben-Moshe, T., Varfolomeev, E., Pewzner‐Jung, Y., Yogev, N., Jurewicz, A., Waisman, A., Brenner, O., Haffner, R., Gustafsson, E., et al. (2004) · Journal of Immunology · doi:10.4049/jimmunol.173.5.2976 · Cited by 425

Apoptotic Cells Provide an Unexpected Source of Wnt3 Signaling to Drive Hydra Head Regeneration

Chera, S., Ghila, L., Dobretz, K., Wenger, Y., Bauer, C. R., Buzgariu, W., Martinou, J., & Galliot, B. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.07.014 · Cited by 424

Many stimuli pull the necrotic trigger, an overview

Vanlangenakker, N., Berghe, T. V., & Vandenabeele, P. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.164 · Cited by 418

Alice in caspase land. A phylogenetic analysis of caspases from worm to man

Lamkanfi, M. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400989 · Cited by 401

Caspase Activation Is Required for Terminal Erythroid Differentiation

Zermati, Y., Garrido, C., Amsellem, S., Fishelson, S., Bouscary, D., Valensi, F., Varet, B. R., Solary, É., & Hermine, O. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.2.247 · Cited by 400

Early Activation of Caspases during T Lymphocyte Stimulation Results in Selective Substrate Cleavage in Nonapoptotic Cells

Alam, A., Cohen, L. Y., Aouad, S. M., & Sékaly, R. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.12.1879 · Cited by 390

Interleukin 1 and interleukin 18 as mediators of inflammation and the aging process

Dinarello, C. A. (2006) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/83.2.447s · Cited by 385

Cell death by autophagy: facts and apparent artefacts

Denton, D., Nicolson, S., & Kumar, S. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.146 · Cited by 381

Intracellular DNA recognition

Hornung, V., & Latz, E. (2010) · Nature reviews. Immunology · doi:10.1038/nri2690 · Cited by 366

Compensatory Proliferation Induced by Cell Death in the Drosophila Wing Disc Requires Activity of the Apical Cell Death Caspase Dronc in a Nonapoptotic Role

Huh, J. R., Guo, M., & Hay, B. A. (2004) · Current Biology · doi:10.1016/j.cub.2004.06.015 · Cited by 354

Caspase-mediated processing of the Drosophila NF-κB factor Relish

Stöven, S., Silverman, N. S., Junell, A., Hedengren-Olcott, M., Erturk, D., Engström, Y., Maniatis, T., & Hultmark, D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1035902100 · Cited by 351

Human caspase 12 has acquired deleterious mutations

Fischer, H., Koenig, U., Eckhart, L., & Tschachler, E. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00289-9 · Cited by 346

Stimulation of Toll-like receptor 3 and 4 induces interleukin-1β maturation by caspase-8

Maelfait, J., Vercammen, E., Janssens, S., Schotte, P., Haegman, M., Magez, S., & Beyaert, R. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20071632 · Cited by 335

Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice

Saleh, M., Mathison, J. C., Wolinski, M. K., Bensinger, S. J., Fitzgerald, P., Droin, N. M., Ulevitch, R. J., Green, D. R., & Nicholson, D. W. (2006) · Nature · doi:10.1038/nature04656 · Cited by 323

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

Specific involvement of caspases in the differentiation of monocytes into macrophages

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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

A Role for Caspases in Lens Fiber Differentiation

Ishizaki, Y., Jacobson, M. D., & RAFF, M. C. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.1.153 · Cited by 293

Aging Impairs the Unfolded Protein Response to Sleep Deprivation and Leads to Proapoptotic Signaling

Naidoo, N. N., Ferber, M., Master, M., Zhu, Y., & Pack, A. I. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5685-07.2008 · Cited by 292

Mitotic catastrophe constitutes a special case of apoptosis whose suppression entails aneuploidy

Castedo, M., Perfettini, J., Roumier, T., Valent, A., Raslová, H., Yakushijin, K., Horne, D. A., Feunteun, J., Lenoir, G., Medema, R. H., et al. (2004) · Oncogene · doi:10.1038/sj.onc.1207572 · Cited by 291

Caspase Activity Mediates the Differentiation of Embryonic Stem Cells

Fujita, J., Crane, A. M., Souza, M. K., Déjosez, M., Kyba, M., Flavell, R. A., Thomson, J. A., & Zwaka, T. P. (2008) · Cell stem cell · doi:10.1016/j.stem.2008.04.001 · Cited by 286

Potentiation of neuroblastoma metastasis by loss of caspase-8

Stupack, D. G., Teitz, T., Potter, M. D., Mikolon, D., Houghton, P. J., Kidd, V. J., Lahti, J. M., & Cheresh, D. A. (2006) · Nature · doi:10.1038/nature04323 · Cited by 276

Regulators of the Toll and Imd pathways in the Drosophila innate immune response

Tanji, T., & Ip, Y. T. (2005) · Trends in Immunology · doi:10.1016/j.it.2005.02.006 · Cited by 265

A crucial role of caspase-3 in osteogenic differentiation of bone marrow stromal stem cells

Miura, M., Chen, X., Allen, M. R., Bi, Y., Gronthos, S., Seo, B., Lakhani, S. A., Flavell, R. A., Feng, X., Robey, P. G., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20427 · Cited by 263

Beclin 1 cleavage by caspase-3 inactivates autophagy and promotes apoptosis

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Apoptotic and non-apoptotic roles of caspases in neuronal physiology and pathophysiology

Hyman, B. T., & Yuan, J. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3228 · Cited by 261

Identification of E2/E3 Ubiquitinating Enzymes and Caspase Activity Regulating Drosophila Sensory Neuron Dendrite Pruning

Kuo, C. T., Zhu, S., Younger, S. H., Jan, L. Y., & Jan, Y. N. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.014 · Cited by 256

Macrophage Activation Redirects Yersinia-Infected Host Cell Death from Apoptosis to Caspase-1-Dependent Pyroptosis

Bergsbaken, T., & Cookson, B. T. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030161 · Cited by 251

Epidermal differentiation does not involve the pro-apoptotic executioner caspases, but is associated with caspase-14 induction and processing

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Mitochondrial apoptosis is dispensable for NLRP3 inflammasome activation but non‐apoptotic caspase‐8 is required for inflammasome priming

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Distinct Mechanisms of Apoptosis-Induced Compensatory Proliferation in Proliferating and Differentiating Tissues in the Drosophila Eye

Fan, Y., & Bergmann, A. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.01.003 · Cited by 238

Control of the Cell Death Pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-Related Caspase Activator

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Apoptosis is required during early stages of tail regeneration in Xenopus laevis

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Local Pruning of Dendrites and Spines by Caspase-3-Dependent and Proteasome-Limited Mechanisms

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Control of Autophagic Cell Death by Caspase-10 in Multiple Myeloma

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Inactivating mutations of caspase-8 gene in colorectal carcinomas

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Developmental parameters of cell death in the wing disc of Drosophila

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Caspase-14 Is Required for Filaggrin Degradation to Natural Moisturizing Factors in the Skin

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Caspase-8 deficiency in epidermal keratinocytes triggers an inflammatory skin disease

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BCL2 Overexpression Associated With Chromosomal Amplification in Diffuse Large B-Cell Lymphoma

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Loss of caspase-1 and caspase-3 protein expression in human prostate cancer.

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Compensatory Proliferation in Drosophila Imaginal Discs Requires Dronc-Dependent p53 Activity

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A Caspase Cascade Regulating Developmental Axon Degeneration

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The biochemical mechanism of caspase-2 activation

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Caspase-1 inflammasomes in infection and inflammation

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The in vitro cleavage of the hAtg proteins by cell death proteases

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Association of a Common Variant of the CASP8 Gene With Reduced Risk of Breast Cancer

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DRONC Coordinates Cell Death and Compensatory Proliferation

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High Commitment of Embryonic Keratinocytes to Terminal Differentiation through a Notch1-caspase 3 Regulatory Mechanism

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Cutting Edge: Innate Immunity Conferred by B Cells Is Regulated by Caspase-8

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Altered apoptosis pathways in mantle cell lymphoma detected by oligonucleotide microarray

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CASPASE-8 Gene Is Inactivated by Somatic Mutations in Gastric Carcinomas

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Caspase-3 regulates cell cycle in B cells: a consequence of substrate specificity

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Cleavage of Atg3 protein by caspase-8 regulates autophagy during receptor-activated cell death

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Resistance to TRAIL-induced apoptosis in primitive neuroectodermal brain tumor cells correlates with a loss of caspase-8 expression

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Drosophila Caspase DRONC Is Required for Specific Developmental Cell Death Pathways and Stress-Induced Apoptosis

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A tumor suppressor function for caspase-2

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A non-apoptotic role for caspase-9 in muscle differentiation

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Caspase-2 activation in the absence of PIDDosome formation

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Caspase 2 and Caspase 3 Protein Levels as Predictors of Survival in Acute Myelogenous Leukemia

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Differential Inactivation of Caspase-8 in Lung Cancers

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Caspase-8 as a therapeutic target in cancer

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Proteolysis of Ambra1 during apoptosis has a role in the inhibition of the autophagic pro-survival response

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Caspase 3 in breast cancer.

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Caspase 2 in apoptosis, the DNA damage response and tumour suppression: enigma no more?

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Inactivating mutations of CASP10 gene in non-Hodgkin lymphomas

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The Caspase 8 Inhibitor c-FLIPL Modulates T-Cell Receptor-Induced Proliferation but Not Activation-Induced Cell Death of Lymphocytes

Lens, S. M. A., Kataoka, T., Fortner, K. A., Tinel, A., Ferrero, I., MacDonald, R., Hahne, M., Beermann, F., Attinger, A., Orbea, H. A., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5419-5433.2002 · Cited by 140

Activation of Caspases Is Required for Osteoblastic Differentiation

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Caspase-8 prevents sustained activation of NF-kappaB in monocytes undergoing macrophagic differentiation.

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Somatic mutations of CASP3 gene in human cancers

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Drosophila IKK-Related Kinase Regulates Nonapoptotic Function of Caspases via Degradation of IAPs

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Aggressive childhood neuroblastomas do not express caspase-8: an important component of programmed cell death

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Identification of Novel Mammalian Caspases Reveals an Important Role of Gene Loss in Shaping the Human Caspase Repertoire

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Hematopoietic Stem Cell Responsiveness to Exogenous Signals Is Limited by Caspase-3

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Caspase-14 Expression by Epidermal Keratinocytes is Regulated by Retinoids in a Differentiation-associated Manner

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Biologic activity of mitochondrial metabolites on aging and age-related hearing loss

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Loss of Caspase-8 Protects Mice Against Inflammation-Related Hepatocarcinogenesis but Induces Non-Apoptotic Liver Injury

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The inflammatory caspases: guardians against infections and sepsis

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Drosophila caspase transduces Shaggy/GSK‐3β kinase activity in neural precursor development

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CARDINAL, a Novel Caspase Recruitment Domain Protein, Is an Inhibitor of Multiple NF-κB Activation Pathways

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Caspase-8 gene is frequently inactivated by the frameshift somatic mutation 1225_1226delTG in hepatocellular carcinomas

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Dimerization and Autoprocessing of the Nedd2 (Caspase-2) Precursor Requires both the Prodomain and the Carboxyl-terminal Regions

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Caspase-2 deficiency promotes aberrant DNA-damage response and genetic instability

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CpG island promoter hypermethylation of the pro-apoptotic gene caspase-8 is a common hallmark of relapsed glioblastoma multiforme

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Inactivating mutations of CASPASE-7 gene in human cancers

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Caspase-3 Modulates Regenerative Response After Stroke

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Caspase-2 is required for dendritic spine and behavioural alterations in J20 APP transgenic mice

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Caspase-2 deficiency enhances aging-related traits in mice

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Expression of active caspase‐3 in mitotic and postmitotic cells of the rat forebrain

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Inactivating mutations of the caspase-10 gene in gastric cancer

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Maturation of the olfactory sensory neurons by Apaf-1/caspase-9–mediated caspase activity

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Interleukin-1β converting enzyme (caspase-1) in intestinal inflammation

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Impaired antioxidant defence and accumulation of oxidative stress in caspase-2-deficient mice

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Caspase-8 deficiency in T cells leads to a lethal lymphoinfiltrative immune disorder

Salmena, L., & Hakem, R. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050683 · Cited by 86

Role of caspase‐8 in hepatocyte response to infection and injury in mice†

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A nonapoptotic role for CASP2/caspase 2

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Improvement of memory for context by inhibition of caspase‐1 in aged rats

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Loss of caspase‐2, ‐6 and ‐7 expression in gastric cancers

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Atg4D at the interface between autophagy and apoptosis

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Genetic deletion of caspase-2 accelerates MMTV/c-neu-driven mammary carcinogenesis in mice

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The Drosophila melanogaster Apaf-1 homologue ARK is required for most, but not all, programmed cell death

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Th-MYCN Mice with Caspase-8 Deficiency Develop Advanced Neuroblastoma with Bone Marrow Metastasis

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Loss of caspase-2 augments lymphomagenesis and enhances genomic instability in Atm -deficient mice

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Caspase Activity Is Required for Stimulated B Lymphocytes to Enter the Cell Cycle

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Tumor-Associated Alterations in Caspase-14 Expression in Epithelial Malignancies

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Decreased PARP and procaspase-2 protein levels are associated with cellular drug resistance in childhood acute lymphoblastic leukemia

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PIDDosome-independent tumor suppression by Caspase-2

Manzl, C., Peintner, L., Krumschnabel, G., Bock, F. J., Labi, V., Drach, M. C., Newbold, A., Johnstone, R. W., & Villunger, A. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.54 · Cited by 64

Loss of caspase-2, -6 and -7 expression in gastric cancers

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Caspases leave the beaten track: caspase-mediated activation of NF-κB

Lamkanfi, M., Declercq, W., Berghe, T. V., & Vandenabeele, P. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200509092 · Cited by 60

Green tea polyphenol induces caspase 14 in epidermal keratinocytes via MAPK pathways and reduces psoriasiform lesions in the flaky skin mouse model

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Genetic variation in caspase genes and risk of non-Hodgkin lymphoma: a pooled analysis of 3 population-based case-control studies

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FADD and caspase-8 are required for cytokine-induced proliferation of hemopoietic progenitor cells

Pellegrini, M., Bath, S., Marsden, V. S., Huang, D. C. S., Metcalf, D., Harris, A. W., & Strasser, A. (2005) · Blood · doi:10.1182/blood-2005-01-0284 · Cited by 59

The Enigmatic Roles of Caspases in Tumor Development

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A role for caspase-8 and c-FLIP L in proliferation and cell-cycle progression of primary hepatocytes

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Caspase‐6 as a novel early target in the treatment of Alzheimer's disease

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Innate immune responses to Chlamydia pneumoniae infection: role of TLRs, NLRs, and the inflammasome

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CASP3 Polymorphisms and Risk of Squamous Cell Carcinoma of the Head and Neck

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Non-apoptotic functions of caspase-7 during osteogenesis

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Mutational analysis of CASP10 gene in colon, breast, lung and hepatocellular carcinomas

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Regulation of urokinase plasminogen activator/plasmin- mediated invasion of melanoma cells by the integrin vitronectin receptor αVβ3

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