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 · see citing works

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 · see citing works

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 · see citing works

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 3,560 · see citing works

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 · see citing works

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 · see citing works

Pyroptosis: host cell death and inflammation

Bergsbaken, T., Fink, S. L., & Cookson, B. T. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2070 · Cited by 3,185 · see citing works

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 · see citing works

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

Thornberry, N., Bull, H., Calaycay, J., Chapman, K., Howard, A., Kostura, M., Miller, D. K., Molineaux, S., Weidner, J., Auniņš, J., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,725 · see citing works

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 2,607 · see citing works

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 · see citing works

Mechanisms and Functions of Inflammasomes

Lamkanfi, M., & Dixit, V. M. (2014) · Cell · doi:10.1016/j.cell.2014.04.007 · Cited by 2,521 · see citing works

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 · see citing works

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

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

Molecular mechanisms of necroptosis: an ordered cellular explosion

Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382 · see citing works

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 · see citing works

Identification of RIP1 kinase as a specific cellular target of necrostatins

Degterev, A., Hitomi, J., Germscheid, M., Ch'en, I. L., Korkina, O., Teng, X., Abbott, D., Cuny, G. D., Yuan, C., Wagner, G., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.83 · Cited by 2,059 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Regulated necrosis: the expanding network of non-apoptotic cell death pathways

Berghe, T. V., Linkermann, A., Jouan-Lanhouet, S., Walczak, H., & Vandenabeele, P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3737 · Cited by 1,735 · see citing works

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 1,606 · see citing works

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 · see citing works

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

Li, P., Allen, H., Banerjee, S., Franklin, S., Herzog, L., Johnston, C. G., McDowell, J., Paskind, M. P., Rodman, L., Salfeld, J. G., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90490-5 · Cited by 1,408 · see citing works

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 · see citing works

Shigella flexneri induces apoptosis in infected macrophages

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

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 · see citing works

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 · see citing works

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 1,139 · see citing works

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 1,126 · see citing works

Essential versus accessory aspects of cell death: recommendations of the NCCD 2015

Galluzzi, L., Bravo-San Pedro, J. M., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Alnemri, E. S., Altucci, L., Andrews, D., Annicchiarico-Petruzzelli, M., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.137 · Cited by 1,002 · see citing works

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 · see citing works

Caspase function in programmed cell death

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

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 818 · see citing works

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 · see citing works

Overweight as an avoidable cause of cancer in Europe

Bergström, A., Pisani, P., Tenet, V., Wolk, A., & Adami, H. (2001) · International Journal of Cancer · doi:10.1002/1097-0215(200002)9999:9999 · Cited by 772 · see citing works

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 · see citing works

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 699 · see citing works

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 · see citing works

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 674 · see citing works

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 · see citing works

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 · see citing works

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 615 · see citing works

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 · see citing works

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 589 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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

Kumar, S., Tomooka, Y., & Noda, M. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91747-e · Cited by 552 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity.Preprint

Salmena, L., Lemmers, B., Hakem, A., Matysiak-Zablocki, E., Murakami, K., Au, P. Y. B., Berry, D., Tamblyn, L., Shehabeldin, A., Migon, E., et al. (2003) · Genes & Development · doi:10.1101/gad.1063703 · Cited by 517 · see citing works

Inflammaging: disturbed interplay between autophagy and inflammasomes

Salminen, A., Kaarniranta, K., & Kauppinen, A. (2012) · Aging · doi:10.18632/aging.100444 · Cited by 511 · see citing works

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 494 · see citing works

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

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

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 423 · see citing works

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

Chera, S., Ghila, L., Dobretz, K., Wenger, Y., Bauer, C., Buzgariu, W. C., Martinou, J., & Galliot, B. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.07.014 · Cited by 418 · see citing works

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 407 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Intracellular DNA recognition

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

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 · see citing works

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 349 · see citing works

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 · see citing works

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 327 · see citing works

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 · see citing works

RIPK1 ensures intestinal homeostasis by protecting the epithelium against apoptosis

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

Specific involvement of caspases in the differentiation of monocytes into macrophages

Sordet, O., Rébé, C., Plenchette, S., Zermati, Y., Hermine, O., Vainchenker, W., Garrido, C., Solary, É., & Dubrez, L. (2002) · Blood · doi:10.1182/blood-2002-06-1778 · Cited by 313 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 282 · see citing works

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 282 · see citing works

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 · see citing works

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 · see citing works

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 262 · see citing works

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 · see citing works

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

Zhu, Y., Zhao, L., Liu, L., Gao, P., Tian, W., Wang, X., Jin, H., Xu, H., & Chen, Q. (2010) · Protein & Cell · doi:10.1007/s13238-010-0048-4 · Cited by 254 · see citing works

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 · see citing works

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 249 · see citing works

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

Lippens, S., Kockx, M., Knaapen, M., Mortier, L., Polakowska, R., Verheyen, A., Garmyn, M., Zwijsen, A., Formstecher, P., Huylebroeck, D., et al. (2000) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4400785 · Cited by 245 · see citing works

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

Allam, R., Lawlor, K. E., Yu, E. C.-W., Mildenhall, A., Moujalled, D. M., Lewis, R. S., Ke, F., Mason, K. D., White, M. J., Stacey, K. J., et al. (2014) · EMBO Reports · doi:10.15252/embr.201438463 · Cited by 238 · see citing works

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 · see citing works

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

Kanuka, H., Sawamoto, K., Inohara, N., Matsuno, K., Okano, H., & Miura, M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80386-x · Cited by 236 · see citing works

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

Tseng, A.-S. K., Adams, D. S., Qiu, D., Koustubhan, P., & Levin, M. G. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.10.048 · Cited by 235 · see citing works

Caspase-mediated cleavage of ATG6/Beclin-1 links apoptosis to autophagy in HeLa cells

Cho, D., Jo, Y. K., Hwang, J. J., Lee, Y. M., Roh, S. A., & Kim, J. C. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.09.004 · Cited by 230 · see citing works

Inactivating mutations of caspase-8 gene in colorectal carcinomas

Kim, H. S., Lee, J. W., Soung, Y. H., Park, W. S., Kim, S. Y., Lee, J., Park, J. Y., Cho, Y. G., Kim, C. J., Jeong, S. W., et al. (2003) · Gastroenterology · doi:10.1016/s0016-5085(03)01059-x · Cited by 230 · see citing works

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

Ertürk, A., Wang, Y., & Sheng, M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3121-13.2014 · Cited by 229 · see citing works

Terminal Differentiation of Human Keratinocytes and Stratum Corneum Formation is Associated with Caspase-14 Activation

Eckhart, L., Declercq, W., Ban, J., Rendl, M., Lengauer, B., Mayer, C., Lippens, S., Vandenabeele, P., & Tschachler, E. (2000) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2000.00205.x · Cited by 224 · see citing works

Developmental parameters of cell death in the wing disc of Drosophila

Milán, M., Campuzano, S., & Garcı́a-Bellido, A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.11.5691 · Cited by 223 · see citing works

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

Lamy, L., Ngo, V. N., Emre, N. C. T., Shaffer, A. L., Yang, Y., Tian, E., Nair, V., Kruhlak, M. J., Zingone, A., Landgren, O., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.017 · Cited by 222 · see citing works

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

Hoste, E., Kemperman, P. M. J. H., Devos, M., Denecker, G., Kežić, S., Yau, N. L. H., Gilbert, B., Lippens, S., Groote, P. D., Roelandt, R., et al. (2011) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.153 · Cited by 214 · see citing works

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

Kovalenko, A., Kim, J., Kang, T., Rajput, A., Bogdanov, K., Dittrich‐Breiholz, O., Kracht, M., Brenner, O. J., & Wallach, D. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20090616 · Cited by 212 · see citing works

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

Monni, O. M., Joensuu, H., Franssila, K., Klefström, J. T., Alitalo, K. K., & Knuutila, S. (1997) · Blood · doi:10.1182/blood.v90.3.1168 · Cited by 212 · see citing works

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

Norman, J., Cohen, G., & Bampton, E. (2010) · Autophagy · doi:10.4161/auto.6.8.13337 · Cited by 209 · see citing works

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

Winter, R., Kramer, A., Borkowski, A., & Kyprianou, N. (2001) · PubMed · Cited by 208 · see citing works

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

Wells, B. S., Yoshida, E., & Johnston, L. A. (2006) · Current Biology · doi:10.1016/j.cub.2006.07.046 · Cited by 206 · see citing works

A Caspase Cascade Regulating Developmental Axon Degeneration

Simon, D. J., Weimer, R. M., McLaughlin, T., Kallop, D. Y., Stanger, K., Yang, J. H., O’Leary, D. D. M., Hannoush, R. N., & Tessier‐Lavigne, M. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.3012-12.2012 · Cited by 201 · see citing works

The biochemical mechanism of caspase-2 activation

Baliga, B. C., Read, S. H., & Kumar, S. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401492 · Cited by 200 · see citing works

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

Macpherson, G. R., Healey, C. S., Teare, M. D., Balasubramanian, S. P., Reed, M., Pharoah, P. D. P., Ponder, B. A. J., Meuth, M., Bhattacharyya, N. P., & Cox, A. (2004) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/dji001 · Cited by 196 · see citing works

Caspase-1 inflammasomes in infection and inflammation

Lamkanfi, M., Kanneganti, T., Franchi, L., & Núñez, G. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.1206756 · Cited by 194 · see citing works

DRONC Coordinates Cell Death and Compensatory Proliferation

Kondo, S., Senoo‐Matsuda, N., Hiromi, Y., & Miura, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00183-06 · Cited by 194 · see citing works

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

Okuyama, R., Nguyen, B.-C., Talora, C., Ogawa, E., di Vignano, A. T., Lioumi, M., Chiorino, G., Tagami, H., Woo, M., & Dotto, G. P. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00098-x · Cited by 185 · see citing works

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

Beisner, D. R., Ch’en, I. L., Kolla, R. V., Hoffmann, A., & Hedrick, S. Μ. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.6.3469 · Cited by 181 · see citing works

Altered apoptosis pathways in mantle cell lymphoma detected by oligonucleotide microarray

Hofmann, W., de Vos, S., Tsukasaki, K., Wachsman, W., Pinkus, G. S., SAID, J. W., & Koeffler, H. P. (2001) · Blood · doi:10.1182/blood.v98.3.787 · Cited by 178 · see citing works

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

Soung, Y. H., Lee, J. W., Kim, S. Y., Jang, J., Park, Y. G., Park, W. S., Nam, S. W., Lee, J. Y., Yoo, N. J., & Lee, S. H. (2005) · Cancer Research · doi:10.1158/0008-5472.815.65.3 · Cited by 177 · see citing works

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

Woo, M., Hakem, R., Furlonger, C. L., Hakem, A., Duncan, G. S., Sasaki, T., Bouchard, D., Lu, L., Wu, G. E., Paige, C. J., et al. (2003) · Nature Immunology · doi:10.1038/ni976 · Cited by 176 · see citing works

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

Grotzer, M. A., Eggert, A., Zuzak, T. J., Janss, A. J., Marwaha, S., Wiewrodt, B. R., Ikegaki, N., Brodeur, G. M., & Phillips∥, P. C. (2000) · Oncogene · doi:10.1038/sj.onc.1203816 · Cited by 174 · see citing works

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

Daish, T. J., Mills, K., & Kumar, S. (2004) · Developmental Cell · doi:10.1016/j.devcel.2004.09.018 · Cited by 171 · see citing works

A tumor suppressor function for caspase-2

Ho, L. H., Taylor, R. L., Dorstyn, L., Cakouros, D., Bouillet, P., & Kumar, S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811928106 · Cited by 167 · see citing works

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

Oral, Ö., Arslan, D. Ö., Itah, Z., Naghavi, A., Deveci, R., Karaçalı, S., & Gözüaçık, D. (2012) · APOPTOSIS · doi:10.1007/s10495-012-0735-0 · Cited by 167 · see citing works

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

Murray, T. V., McMahon, J. M., Howley, B. A., Stanley, A., Ritter, T., Mohr, A., Zwacka, R. M., & Fearnhead, H. O. (2008) · Journal of Cell Science · doi:10.1242/jcs.024547 · Cited by 167 · see citing works

Differential Inactivation of Caspase-8 in Lung Cancers

Shivapurkar, N., Toyooka, S., Eby, M. T., Huang, C., Sathyanarayana, U. G., Cunningham, H. T., Reddy, J., Brambilla, E., Takahashi, T., Minna, J. D., et al. (2002) · Cancer Biology & Therapy · doi:10.4161/cbt.1.1.45 · Cited by 160 · see citing works

Caspase-2 activation in the absence of PIDDosome formation

Manzl, C., Krumschnabel, G., Bock, F. J., Sohm, B., Labi, V., Baumgartner, F., Logette, E., Tschopp, J., & Villunger, A. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200811105 · Cited by 157 · see citing works

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

Estrov, Z. E., Thall, P. F., Talpaz, M., Estey, E. H., Kantarjian, H. M., Andreeff, M., Harris, D., Van, Q., Walterscheid, M., & Kornblau, S. M. (1998) · Blood · doi:10.1182/blood.v92.9.3090 · Cited by 156 · see citing works

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

Pagliarini, V., Wirawan, E., Romagnoli, A., Ciccosanti, F., Lisi, G., Lippens, S., Cecconi, F., Fimia, G. M., Vandenabeele, P., Corazzari, M., et al. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.27 · Cited by 149 · see citing works

Caspase-8 as a therapeutic target in cancer

Stupack, D. G. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.07.022 · Cited by 147 · see citing works

Inactivating mutations of CASP10 gene in non-Hodgkin lymphomas

Shin, M. S., Kim, H. S., Kang, C. S., Park, W. S., Kim, S. Y., Lee, S. N., Lee, J., Park, J. Y., Jang, J. J., Kim, C. W., et al. (2002) · Blood · doi:10.1182/blood.v99.11.4094 · Cited by 147 · see citing works

Caspase 3 in breast cancer.

O’Donovan, N., Crown, J. P., Stunell, H., Hill, A. D. K., McDermott, E. W. M., O’Higgins, N. J., & Duffy, M. J. (2003) · PubMed · Cited by 145 · see citing works

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

Kumar, S. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2745 · Cited by 142 · see citing works

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 · see citing works

Activation of Caspases Is Required for Osteoblastic Differentiation

Mogi, M., & Togari, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307055200 · Cited by 139 · see citing works

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

Rébé, C., Cathelin, S., Launay, S., Filomenko, R., Prévotat, L., L'ollivier, C., Gyan, E., Micheau, O., Grant, S., Dubart-Kupperschmitt, A., et al. (2007) · Blood · doi:10.1182/blood-2006-03-011585 · Cited by 138 · see citing works

Somatic mutations of CASP3 gene in human cancers

Soung, Y. H., Lee, J.-W., Kim, S., Park, W.-S., Nam, S., Lee, J., Yoo, N. J., & Lee, S. (2004) · Human Genetics · doi:10.1007/s00439-004-1129-3 · Cited by 131 · see citing works

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

Kuranaga, E., Kanuka, H., Tonoki, A., Takemoto, K., Tomioka, T., Kobayashi, M., Hayashi, S., & Miura, M. (2006) · Cell · doi:10.1016/j.cell.2006.05.048 · Cited by 130 · see citing works

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

Teitz, T., Lahti, J. M., & Kidd, V. J. (2001) · Journal of Molecular Medicine · doi:10.1007/s001090100233 · Cited by 130 · see citing works

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

Eckhart, L., Ballaun, C., Hermann, M., VandeBerg, J. L., Sipos, W., Uthman, A., Fischer, H., & Tschachler, E. (2008) · Molecular Biology and Evolution · doi:10.1093/molbev/msn012 · Cited by 128 · see citing works

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

Janzen, V., Fleming, H. E., Riedt, T., Karlsson, G., Riese, M. J., Celso, C. L., Reynolds, G., Milne, C. D., Paige, C. J., Karlsson, S., et al. (2008) · Cell stem cell · doi:10.1016/j.stem.2008.03.012 · Cited by 125 · see citing works

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

Rendl, M., Ban, J., Mrass, P., Mayer, C., Lengauer, B., Eckhart, L., Declerq, W., & Tschachler, E. (2002) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2002.19532.x · Cited by 123 · see citing works

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

Seidman, M. D., Khan, M. A., Bai, U., Shirwany, N. A., & Quirk, W. S. (2000) · American Journal of Otolaryngology · doi:10.1016/s0196-0709(00)80003-4 · Cited by 122 · see citing works

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

Liedtke, C., Bangen, J., Freimuth, J., Beraza, N., Lambertz, D., Cubero, F. J., Hatting, M., Karlmark, K. R., Streetz, K. L., Krombach, G. A., et al. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.08.037 · Cited by 121 · see citing works

The inflammatory caspases: guardians against infections and sepsis

Scott, A., & Saleh, M. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402026 · Cited by 119 · see citing works

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

Kanuka, H., Kuranaga, E., Takemoto, K., Hiratou, T., Okano, H., & Miura, M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600822 · Cited by 115 · see citing works

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

Bouchier‐Hayes, L., Conroy, H., Egan, H., Adrain, C., Creagh, E. M., MacFarlane, M., & Martin, S. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107373200 · Cited by 112 · see citing works

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

Soung, Y. H., Lee, J. W., Kim, S. Y., Sung, Y. J., Park, W. S., Nam, S. W., Kim, S. H., Lee, J. Y., Yoo, N. J., & Lee, S. H. (2004) · Oncogene · doi:10.1038/sj.onc.1208244 · Cited by 111 · see citing works

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

Butt, A. J., Harvey, N. L., Parasivam, G., & Kumar, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.6763 · Cited by 110 · see citing works

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

Dorstyn, L., Puccini, J., Wilson, C. H., Shalini, S., Nicola, M., Moore, S., & Kumar, S. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2012.36 · Cited by 104 · see citing works

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

Martínez, R., Setién, F., Völter, C., Casado, S., Quesada, M. P., Schackert, G., & Esteller, M. (2007) · Carcinogenesis · doi:10.1093/carcin/bgm014 · Cited by 103 · see citing works

Inactivating mutations of CASPASE-7 gene in human cancers

Soung, Y. H., Lee, J. W., Kim, H. S., Park, W. S., Kim, S. Y., Lee, J., Park, J. Y., Cho, Y. G., Kim, C. J., Park, Y. G., et al. (2003) · Oncogene · doi:10.1038/sj.onc.1206727 · Cited by 101 · see citing works

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

Pozueta, J., Lefort, R., Ribé, E. M., Troy, C. M., Arancio, O., & Shelanski, M. L. (2013) · Nature Communications · doi:10.1038/ncomms2927 · Cited by 100 · see citing works

Caspase-3 Modulates Regenerative Response After Stroke

Fan, W., Dai, Y., Xu, H., Zhu, X., Cai, P., Wang, L., Sun, C., Hu, C., Zheng, P., & Zhao, B. (2013) · Stem Cells · doi:10.1002/stem.1503 · Cited by 97 · see citing works

Caspase-2 deficiency enhances aging-related traits in mice

Zhang, Y., Padalecki, S. S., CHAUDHURI, A., deWaal, E., Goins, B., Grubbs, B. G., Ikeno, Y., Richardson, A. G., MUNDY, G., & HERMAN, B. (2006) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2006.11.030 · Cited by 96 · see citing works

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

Yan, X., Najbauer, J., Woo, C. C., Dashtipour, K., Ribak, C. E., & Leon, M. (2001) · The Journal of Comparative Neurology · doi:10.1002/cne.1121 · Cited by 94 · see citing works

Inactivating mutations of the caspase-10 gene in gastric cancer

Park, W. S., Lee, J., Shin, M. S., Park, J. Y., Kim, H. S., Lee, J. H., Kim, Y. S., Lee, S. H., Xiao, W., Park, C. H., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1205394 · Cited by 93 · see citing works

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

Ohsawa, S., Hamada, S., Kuida, K., Yoshida, H., Igaki, T., & Miura, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910488107 · Cited by 90 · see citing works

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

Siegmund, B. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01064-x · Cited by 89 · see citing works

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

Shalini, S., Dorstyn, L., Wilson, C., Puccini, J., Ho, L. H., & Kumar, S. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.13 · Cited by 87 · see citing works

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 · see citing works

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

Moshe, T. B., Barash, H., Kang, T., Kim, J., Kovalenko, A., Gross, E., Schuchmann, M., Abramovitch, R., Galun, E., & Wallach, D. (2007) · Hepatology · doi:10.1002/hep.21495 · Cited by 83 · see citing works

A nonapoptotic role for CASP2/caspase 2

Tiwari, M., Sharma, L. K., Vanegas, D., Callaway, D. A., Bai, Y., Lechleiter, J. D., & Herman, B. A. (2014) · Autophagy · doi:10.4161/auto.28528 · Cited by 75 · see citing works

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

Gemma, C., Fister, M., Hudson, C., & Bickford, P. C. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04334.x · Cited by 74 · see citing works

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

Yoo, N. J., LEE, J. W., Kim, Y. J., Soung, Y. H., KIM, S. Y., Nam, S. W., Park, W. S., Lee, J. Y., & Lee, S. H. (2004) · Apmis · doi:10.1111/j.1600-0463.2004.t01-1-apm1120602.x · Cited by 74 · see citing works

Atg4D at the interface between autophagy and apoptosis

Betin, V. M. S., & Lane, J. D. (2009) · Autophagy · doi:10.4161/auto.5.7.9684 · Cited by 73 · see citing works

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

Parsons, M. J., McCormick, L. L., Janke, L. J., Howard, A. G. A., Bouchier‐Hayes, L., & Green, D. R. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.38 · Cited by 71 · see citing works

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

Mills, K., Daish, T., Harvey, K. F., Pfleger, C. M., Hariharan, I. K., & Kumar, S. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512126 · Cited by 70 · see citing works

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

Teitz, T., Inoue, M., Valentine, M. B., Zhu, K., Rehg, J. E., Zhao, W. M., Finkelstein, D., Wang, Y., Johnson, M. D., Calabrese, C. R., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-2681 · Cited by 70 · see citing works

Loss of <i>caspase-2</i> augments lymphomagenesis and enhances genomic instability in <i>Atm</i> -deficient mice

Puccini, J., Shalini, S., Voss, A. K., Gatei, M., Wilson, C. H., Hiwase, D. K., Lavin, M. F., Dorstyn, L., & Kumar, S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311947110 · Cited by 69 · see citing works

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

Krajewska, M., Kim, H., Shin, E., Kennedy, S., Duffy, M. J., Wong, Y. F., Marr, D. G., Mikolajczyk, J., Shabaik, A. S., Meinhold-Heerlein, I. M., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-2527 · Cited by 67 · see citing works

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

Olson, N. E., Graves, J. D., Shu, G. L., Ryan, E. J., & Clark, E. A. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.12.6065 · Cited by 66 · see citing works

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

de Haar-Holleman, A., den Boer, M. L., Kazemier, K. M., Beverloo, H. B., von Bergh, A. R. M., Janka-Schaub, G. E., & Pieters, R. (2005) · Blood · doi:10.1182/blood-2004-11-4296 · Cited by 66 · see citing works

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 · see citing works

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

Yoo, N. J., Lee, J. W., Kim, Y. J., Soung, Y. H., Kim, S. Y., Nam, S. W., Park, W. S., Lee, J. Y., & Lee, S. H. (2004) · Apmis · doi:10.1111/j.1600-0463.2004.apm1120602.x · Cited by 63 · see citing works

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 · see citing works

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 · see citing works

The Enigmatic Roles of Caspases in Tumor Development

Jäger, R., & Zwacka, R. M. (2010) · Cancers · doi:10.3390/cancers2041952 · Cited by 58 · see citing works

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

Hsu, S., Dickinson, D. P., Borke, J. L., Walsh, D. S., Wood, J., Qin, H., Winger, J. N., Pearl, H., Schuster, G. S., & Bollag, W. B. (2007) · Experimental Dermatology · doi:10.1111/j.1600-0625.2007.00585.x · Cited by 57 · see citing works

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

Lan, Q., Morton, L. M., Armstrong, B. K., Hartge, P. A., Menashe, I., Zheng, T., Purdue, M. P., Cerhan, J. R., Zhang, Y., Grulich, A. E., et al. (2009) · Blood · doi:10.1182/blood-2009-01-198697 · Cited by 55 · see citing works

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

LeBlanc, A. C. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12250 · Cited by 55 · see citing works

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

Gilot, D., Sérandour, A., Ilyin, G. P., Lagadic‐Gossmann, D., Loyer, P., Corlu, A., Coutant, A., Baffet, G., Peter, M. E., Fardel, O., et al. (2005) · Carcinogenesis · doi:10.1093/carcin/bgi187 · Cited by 55 · see citing works

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

Shimada, K., Crother, T. R., & Arditi, M. (2012) · Microbes and Infection · doi:10.1016/j.micinf.2012.08.004 · Cited by 53 · see citing works

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

Chen, K., Zhao, H., Hu, Z., Wang, L., Zhang, W., Sturgis, E. M., & Wei, Q. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1198 · Cited by 53 · see citing works

Caspase polymorphisms and genetic susceptibility to multiple myeloma

Hosgood, H. D., Baris, D., Zhang, Y., Zhu, Y. L., Zheng, T., Yeager, M., Welch, R. A., Zahm, S. H., Chanock, S. J., Rothman, N., et al. (2008) · Hematological Oncology · doi:10.1002/hon.852 · Cited by 51 · see citing works

Caspase-2 impacts lung tumorigenesis and chemotherapy response in vivo

Terry, M. R., Arya, R. S., Mukhopadhyay, A., Berrett, K., Clair, P. M., Witt, B. L., Salama, M. E., Bhutkar, A. J., & Oliver, T. G. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.159 · Cited by 49 · see citing works

Caspase-8 as a Regulator of Tumor Cell Motility

Graf, R. P., Keller, N., Barbero, S., & Stupack, D. G. (2014) · Current Molecular Medicine · doi:10.2174/1566524014666140128111951 · Cited by 48 · see citing works

Promoter methylation pattern of caspase-8, P16INK4A, MGMT, TIMP-3, and E-cadherin in medulloblastoma

Ebinger, M., Senf, L., Wachowski, O., & Scheurlen, W. G. (2004) · Pathology & Oncology Research · doi:10.1007/bf02893403 · Cited by 48 · see citing works

Dual role of the caspase enzymes in satellite cells from aged and young subjects

Fulle, S., Sancilio, S., Mancinelli, R., Gatta, V., & Pietro, R. D. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.472 · Cited by 46 · see citing works

Apoptosis regulatory gene NEDD2 maps to human chromosome segment 7q34?35, a region frequently affected in haematological neoplasms

Kumar, S., White, D. L., Takai, S., Turczynowicz, S., Juttner, C. A., & Hughes, T. (1995) · Human Genetics · doi:10.1007/bf00209480 · Cited by 46 · see citing works

Caspase-2 protects against oxidative stress in vivo

Shalini, S., Puccini, J., Wilson, C. H., Finnie, J. W., Dorstyn, L., & Kumar, S. (2014) · Oncogene · doi:10.1038/onc.2014.413 · Cited by 37 · see citing works

Death of p53-defective cells triggered by forced mitotic entry in the presence of DNA damage is not uniquely dependent on Caspase-2 or the PIDDosome

Manzl, C., Fava, L. L., Krumschnabel, G., Peintner, L., Tanzer, M. C., Soratroi, C., Bock, F. J., Schuler, F., Luef, B., Geley, S., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.470 · Cited by 36 · see citing works

Non-apoptotic functions of caspase-7 during osteogenesis

Švandová, E., Lesot, H., Berghe, T. V., Tucker, A. S., Sharpe, P. T., Vandenabeele, P., & Matalová, E. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.330 · Cited by 36 · see citing works

Polymorphisms and Haplotypes in the Caspase-3, Caspase-7, and Caspase-8 Genes and Risk for Endometrial Cancer: A Population-Based, Case-Control Study in a Chinese Population

Xu, H., Xu, W., Cai, Q., Feng, M., Long, J., Zheng, W., Xiang, Y., & Shu, X. (2009) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-09-0152 · Cited by 35 · see citing works

Loss of caspase-8 in hepatocytes accelerates the onset of liver regeneration in mice through premature nuclear factor kappa B activation

Freimuth, J., Bangen, J., Lambertz, D., Hu, W., Nevzorova, Y. A., Sonntag, R., Gaßler, N., Riethmacher, D., Trautwein, C., & Liedtke, C. (2013) · Hepatology · doi:10.1002/hep.26538 · Cited by 34 · see citing works

Caspase‐7 participates in differentiation of cells forming dental hard tissues

Matalová, E., Lesot, H., Švandová, E., Berghe, T. V., Sharpe, P. T., Healy, C., Vandenabeele, P., & Tucker, A. S. (2013) · Development Growth & Differentiation · doi:10.1111/dgd.12066 · Cited by 31 · see citing works

Caspase-1 enhances the apoptotic response of prostate cancer cells to ionizing radiation.

Winter, R., Rhee, J. G., & Kyprianou, N. (2004) · PubMed · Cited by 30 · see citing works

Identification of polymorphisms in the Caspase‐3 gene and their association with lung cancer risk

Jang, J. S., Kim, K. M., Choi, J. E., Ick, S., Kim, C. H., Lee, W. K., Kam, S., Jung, T. H., & Park, J. (2007) · Molecular Carcinogenesis · doi:10.1002/mc.20397 · Cited by 30 · see citing works

Immunohistochemical expression of caspase-1 and -9, uncleaved caspase-3 and -6, cleaved caspase-3 and -6 as well as Bcl-2 in benign epithelium and cancer of the prostate

Ummanni, R., Lehnigk, U., Zimmermann, U., Woenckhaus, C., Walther, R., & Giebel, J. (2009) · Experimental and Therapeutic Medicine · doi:10.3892/etm_00000008 · Cited by 30 · see citing works

Exploitation of a non-apoptotic caspase to regulate the abundance of the cdkI p27KIP1 in transformed lymphoid cells

Frost, V. J., Al-Mehairi, S. S., & Sinclair, A. J. (2001) · Oncogene · doi:10.1038/sj.onc.1204367 · Cited by 29 · see citing works

Polymorphisms in the Caspase7 gene and the risk of lung cancer

Lee, W. K., Kim, J. S., Kang, H., Ick, S., Kim, D. S., Hyun, D.-S., Kam, S., Kim, C. H., Jung, T. H., & Park, J. (2008) · Lung Cancer · doi:10.1016/j.lungcan.2008.10.022 · Cited by 28 · see citing works

HuGE systematic review and meta-analysis demonstrate association of CASP-3 and CASP-7 genetic polymorphisms with cancer risk

Yan, S., Li, Y. Z., Zhu, X., Liu, C. L., Wang, P., & Liu, Y. L. (2013) · Genetics and Molecular Research · doi:10.4238/2013.may.13.10 · Cited by 28 · see citing works

An unexpected role for caspase-2 in neuroblastoma

Dorstyn, L., Puccini, J., Nikolic, A., Shalini, S., Wilson, C. H., Norris, M. D., Haber, M., & Kumar, S. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.342 · Cited by 23 · see citing works

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

Oh, J. E., Kim, M. S., Ahn, C. H., Kim, S. S., Han, J. Y., Lee, S. H., & Yoo, N. J. (2009) · Pathology · doi:10.3109/00313020903434371 · Cited by 21 · see citing works

Loss of caspase-2 accelerates age-dependent alterations in mitochondrial production of reactive oxygen species

Lopez‐Cruzan, M., & Herman, B. A. (2013) · Biogerontology · doi:10.1007/s10522-013-9415-x · Cited by 15 · see citing works

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.

Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death &amp; Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works

Activation of apoptosis signalling pathways by reactive oxygen species

Redza-Dutordoir, M., & Averill-Bates, D. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.012 · Cited by 3,731 · see citing works

Apoptosis as anticancer mechanism: function and dysfunction of its modulators and targeted therapeutic strategies

Pistritto, G., Trisciuoglio, D., Ceci, C., Garufi, A., & D’Orazi, G. (2016) · Aging · doi:10.18632/aging.100934 · Cited by 1,670 · see citing works

Guidelines for the use of flow cytometry and cell sorting in immunological studies (second edition)

Cossarizza, A., Chang, H., Radbruch, A., Acs, A., Adam, D., Adam‐Klages, S., Agace, W. W., Aghaeepour, N., Akdiş, M., Allez, M., et al. (2019) · European Journal of Immunology · doi:10.1002/eji.201970107 · Cited by 982 · see citing works

Autophagy-dependent cell death

Denton, D., & Kumar, S. (2019) · Cell Death &amp; Differentiation · doi:10.1038/s41418-018-0252-y · Cited by 777 · see citing works

Apoptosis: A Comprehensive Overview of Signaling Pathways, Morphological Changes, and Physiological Significance and Therapeutic Implications

Mustafa, M., Ahmad, R., Tantry, I. Q., Ahmad, W., Siddiqui, S., Alam, M., Abbas, K., Moinuddin, Hassan, M. I., Habib, S., et al. (2024) · Cells · doi:10.3390/cells13221838 · Cited by 595 · see citing works

Interleukin-18 in Health and Disease

Yasuda, K., Nakanishi, K., & Tsutsui, H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030649 · Cited by 564 · see citing works

Guidelines for the use of flow cytometry and cell sorting in immunological studies *

Cossarizza, A., Chang, H., Radbruch, A., Akdiş, M., Andrä, I., Annunziato, F., Bächer, P., Barnaba, V., Battistini, L., Bauer, W. M., et al. (2017) · European Journal of Immunology · doi:10.1002/eji.201646632 · Cited by 572 · see citing works

Caspase‐3: Structure, function, and biotechnological aspects

Asadi, M., Taghizadeh, S., Kaviani, E., Vakili, O., Taheri‐Anganeh, M., Tahamtan, M., & Savardashtaki, A. (2021) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2233 · Cited by 537 · see citing works

Caspase-1 initiates apoptosis in the absence of gasdermin D

Tsuchiya, K., Nakajima, S., Hosojima, S., Nguyen, D. T., Hattori, T., Le, T. M., Hori, O., Mahib, M. R., Yamaguchi, Y., Miura, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09753-2 · Cited by 502 · see citing works

Programmed cell death in aging

Tower, J. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.04.002 · Cited by 426 · see citing works

Recent Insights into the Molecular Mechanisms Underlying Pyroptosis and Gasdermin Family Functions

Aglietti, R. A., & Dueber, E. C. (2017) · Trends in Immunology · doi:10.1016/j.it.2017.01.003 · Cited by 409 · see citing works

A Review on Caspases: Key Regulators of Biological Activities and Apoptosis

Sahoo, G., Samal, D., Khandayataray, P., & Murthy, M. K. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03433-5 · Cited by 406 · see citing works

Microglia: Agents of the CNS Pro-Inflammatory Response

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

Apoptotic cell death in disease—Current understanding of the NCCD 2023

Vitale, I., Pietrocola, F., Guilbaud, E., Aaronson, S. A., Abrams, J., Adam, D., Agostini, M., Agostinis, P., Alnemri, E. S., Altucci, L., et al. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01153-w · Cited by 359 · see citing works

Caspases Connect Cell-Death Signaling to Organismal Homeostasis

Galluzzi, L., López-Soto, A., Kumar, S., & Kroemer, G. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.020 · Cited by 350 · see citing works

An eco-friendly synthesis of Enterococcus sp.–mediated gold nanoparticle induces cytotoxicity in human colorectal cancer cells

Vairavel, M., Ezhilarasan, D., & Rajeshkumar, S. (2020) · Environmental Science and Pollution Research · doi:10.1007/s11356-019-07511-x · Cited by 340 · see citing works

Proteomic and interactomic insights into the molecular basis of cell functional diversity

Bludau, I., & Aebersold, R. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0231-2 · Cited by 297 · see citing works

The Ageing Brain: Molecular and Cellular Basis of Neurodegeneration

Azam, S., Haque, M. E., Balakrishnan, R., Kim, I., & Choi, D. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.683459 · Cited by 257 · see citing works

Switching from Apoptosis to Pyroptosis: Gasdermin-Elicited Inflammation and Antitumor Immunity

Tsuchiya, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22010426 · Cited by 256 · see citing works

H19 lncRNA alters DNA methylation genome wide by regulating S-adenosylhomocysteine hydrolase

Zhou, J., Yang, L., Zhong, T., Mueller, M., Men, Y., Zhang, N., Xie, J., Giang, K., Chung, H., Sun, X., et al. (2015) · Nature Communications · doi:10.1038/ncomms10221 · Cited by 254 · see citing works

The Roles of Neutrophil-Derived Myeloperoxidase (MPO) in Diseases: The New Progress

Lin, W. C., Chen, H., Chen, X., & Guo, C. (2024) · Antioxidants · doi:10.3390/antiox13010132 · Cited by 274 · see citing works

Intracellular regulation of TNF activity in health and disease

Varfolomeev, E. E., & Vucic, D. (2016) · Cytokine · doi:10.1016/j.cyto.2016.08.035 · Cited by 247 · see citing works

Chemical Design of Activatable Photoacoustic Probes for Precise Biomedical Applications

Liu, Y., Teng, L., Yin, B., Meng, H., Yin, X., Huan, S., Song, G., & Zhang, X. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00875 · Cited by 249 · see citing works

Inflammasome‐associated cell death: Pyroptosis, apoptosis, and physiological implications

Tsuchiya, K. (2020) · Microbiology and Immunology · doi:10.1111/1348-0421.12771 · Cited by 238 · see citing works

Shining New Light on Biological Systems: Luminescent Transition Metal Complexes for Bioimaging and Biosensing Applications

Lee, L. C., & Lo, K. K. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00629 · Cited by 248 · see citing works

Killers creating new life: caspases drive apoptosis-induced proliferation in tissue repair and disease

Fogarty, C. E., & Bergmann, A. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.47 · Cited by 235 · see citing works

Proteolytic Cleavage—Mechanisms, Function, and “Omic” Approaches for a Near-Ubiquitous Posttranslational Modification

Klein, T., Eckhard, U., Dufour, A., Solis, N., & Overall, C. M. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00120 · Cited by 229 · see citing works

A Cell’s Fate: An Overview of the Molecular Biology and Genetics of Apoptosis

Cavalcante, G. C., Schaan, A. P., Cabral, G. F., Santana-da-Silva, M. N., Pinto, P., Vidal, A. F., & Ribeiro‐dos‐Santos, Â. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174133 · Cited by 222 · see citing works

Mechanisms of apoptosis

Savitskaya, M. A., & Онищенко, Г. Е. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915110012 · Cited by 214 · see citing works

NLRP3 Inflammasome as a Molecular Marker in Diabetic Cardiomyopathy

Luo, B., Huang, F., Liu, Y., Liang, Y., Wei, Z., Ke, H., Zeng, Z., Huang, W., & He, Y. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00519 · Cited by 213 · see citing works

Mechanistic insights from inflammasome structures

Fu, J., Schroder, K., & Wu, H. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-00995-w · Cited by 215 · see citing works

Apoptosis Regulators Bcl-2 and Caspase-3

Hussar, P. (2022) · Encyclopedia · doi:10.3390/encyclopedia2040111 · Cited by 210 · see citing works

The interplay between inflammation and metabolism in rheumatoid arthritis

Chimenti, M. S., Triggianese, P., Conigliaro, P., Candi, E., Melino, G., & Perricone, R. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.246 · Cited by 208 · see citing works

Dietary and Physiological Effects of Zinc on the Immune System

Weßels, I., Fischer, H. J., & Rink, L. (2021) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-122019-120635 · Cited by 207 · see citing works

Mechanisms for the transition from physiological to pathological cardiac hypertrophy

Oldfield, C. J., Duhamel, T. A., & Dhalla, N. S. (2019) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2019-0566 · Cited by 206 · see citing works

Cell Death and Inflammation: The Role of Mitochondria in Health and Disease

Picca, A., Calvani, R., Coelho‐Júnior, H. J., & Marzetti, E. (2021) · Cells · doi:10.3390/cells10030537 · Cited by 203 · see citing works

Neutrophil pyroptosis: new perspectives on sepsis

Liu, L., & Sun, B. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03060-1 · Cited by 197 · see citing works

Caspase-2 cleavage of tau reversibly impairs memory

Zhao, X., Kotilinek, L. A., Smith, B., Hlynialuk, C., Zahs, K., Ramsden, M., Cleary, J., & Ashe, K. H. (2016) · Nature Medicine · doi:10.1038/nm.4199 · Cited by 187 · see citing works

Advances in mechanism and regulation of PANoptosis: Prospects in disease treatment

Zhu, P., Ke, Z.-R., Chen, J.-X., Li, S., Ma, T., & Fan, X.-L. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1120034 · Cited by 194 · see citing works

Caspase involvement in autophagy

Tsapras, P., & Nezis, I. P. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.43 · Cited by 191 · see citing works

Endoplasmic Reticulum Stress and Unfolded Protein Response in Breast Cancer: The Balance between Apoptosis and Autophagy and Its Role in Drug Resistance

Sisinni, L., Pietrafesa, M., Lepore, S., Maddalena, F., Condelli, V., Esposito, F., & Landriscina, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040857 · Cited by 185 · see citing works

Antidepressant active ingredients from herbs and nutraceuticals used in TCM: pharmacological mechanisms and prospects for drug discovery

Wang, Y.-S., Shen, C., & Jiang, J. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104520 · Cited by 183 · see citing works

Cell death regulation: A new way for natural products to treat osteoporosis

Li, Z., Li, D., Chen, R., Gao, S., Xu, Z., & Li, N. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106635 · Cited by 180 · see citing works

Crosstalk between cGAS–STING signaling and cell death

Murthy, A. M. V., Robinson, N., & Kumar, S. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00624-8 · Cited by 170 · see citing works

PANoptosis: bridging apoptosis, pyroptosis, and necroptosis in cancer progression and treatment

Gao, J., Xiong, A., Liu, J., Li, X., Wang, J., Zhang, L., Liu, Y., Xiong, Y., Li, G., & He, X. (2024) · Cancer Gene Therapy · doi:10.1038/s41417-024-00765-9 · Cited by 172 · see citing works

Inhibiting the inhibitors: Targeting anti-apoptotic proteins in cancer and therapy resistance

Shahar, N., & Larisch, S. (2020) · Drug Resistance Updates · doi:10.1016/j.drup.2020.100712 · Cited by 170 · see citing works

A delicate balance – The BCL-2 family and its role in apoptosis, oncogenesis, and cancer therapeutics

Knight, T. E., Luedtke, D. A., Edwards, H. J., Taub, J. W., & Ge, Y. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.01.015 · Cited by 166 · see citing works

The Life and Death of a Plant Cell

Kabbage, M., Kessens, R., Bartholomay, L. C., & Williams, B. (2017) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-043015-111655 · Cited by 157 · see citing works

An unexpected friend − ROS in apoptosis-induced compensatory proliferation: Implications for regeneration and cancer

Diwanji, N., & Bergmann, A. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.07.004 · Cited by 154 · see citing works

Caspases as master regulators of programmed cell death: apoptosis, pyroptosis and beyond

Dho, S. H., Cho, M., Woo, W., Jeong, S., & Kim, L. K. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01470-9 · Cited by 155 · see citing works

Targeted contrast agents and activatable probes for photoacoustic imaging of cancer

Zhao, Z., Swartchick, C. B., & Chan, J. (2022) · Chemical Society Reviews · doi:10.1039/d0cs00771d · Cited by 154 · see citing works

Hesperidin from Citrus seed induces human hepatocellular carcinoma HepG2 cell apoptosis via both mitochondrial and death receptor pathways

Banjerdpongchai, R., Wudtiwai, B., Khaw-on, P., Rachakhom, W., Duangnil, N., & Kongtawelert, P. (2015) · Tumor Biology · doi:10.1007/s13277-015-3774-7 · Cited by 150 · see citing works

Caspase-9: A Multimodal Therapeutic Target With Diverse Cellular Expression in Human Disease

Avrutsky, M. I., & Troy, C. M. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.701301 · Cited by 151 · see citing works

Antitumor Effects of Carvacrol and Thymol: A Systematic Review

Sampaio, L. A., Pina, L. T. S., Serafini, M. R., Tavares, D. D. S., & Guimarães, A. G. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.702487 · Cited by 148 · see citing works

Spontaneous preterm birth: advances toward the discovery of genetic predisposition

Strauss, J. F., Romero, R. J., Gomez‐Lopez, N., Haymond‐Thornburg, H., Modi, B. P., Teves, M. E., Pearson, L. N., York, T. P., & Schenkein, H. A. (2017) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2017.12.009 · Cited by 147 · see citing works

Quercetin modulates signaling pathways and induces apoptosis in cervical cancer cells

Sundaram, M. K., Raina, R., Afroze, N., Bajbouj, K., Hamad, M. A., Haque, S., & Hussain, A. (2019) · Bioscience Reports · doi:10.1042/bsr20190720 · Cited by 150 · see citing works

A Photoacoustic Probe for the Imaging of Tumor Apoptosis by Caspase‐Mediated Macrocyclization and Self‐Assembly

Wang, Y., Hu, X., Weng, J., Li, J., Fan, Q., Zhang, Y., & Ye, D. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201813748 · Cited by 144 · see citing works

Activatable Multimodal Probes for In Vivo Imaging and Theranostics

Wang, Y., Hu, Y., & Ye, D. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202209512 · Cited by 142 · see citing works

Different types of cell death and their shift in shaping disease

Shen, S., Shao, Y., & Li, C. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01581-0 · Cited by 146 · see citing works

Probing the correlation of neuronal loss, neurofibrillary tangles, and cell death markers across the Alzheimer's disease Braak stages: a quantitative study in humans

Theofilas, P., Ehrenberg, A. J., Nguy, A. K., Thackrey, J. M., Dunlop, S. R., Mejia, M. B., Alho, A. T. D. L., Leite, R. E. P., Rodriguez, R. D., Suemoto, C. K., et al. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.09.007 · Cited by 131 · see citing works

Peptide‐Based Multifunctional Nanomaterials for Tumor Imaging and Therapy

Zhang, C., Wu, W. H., Li, R., Qiu, W., Zhuang, Z., Cheng, S., & Zhang, X. (2018) · Advanced Functional Materials · doi:10.1002/adfm.201804492 · Cited by 135 · see citing works

Gasdermin D mediates the maturation and release of IL-1α downstream of inflammasomes

Tsuchiya, K., Hosojima, S., Hara, H., Kushiyama, H., Mahib, M. R., Kinoshita, T., & Suda, T. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108887 · Cited by 135 · see citing works

A natural products solution to diabetic nephropathy therapy

Hu, Q., Jiang, L., Qi, Y., Zeng, J., Ma, X., & Zhao, Y. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108314 · Cited by 133 · see citing works

Evolution of caspase-mediated cell death and differentiation: twins separated at birth

Bell, R. A. V., & Megeney, L. A. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.37 · Cited by 131 · see citing works

The changing 50% inhibitory concentration (IC50) of cisplatin: a pilot study on the artifacts of the MTT assay and the precise measurement of density-dependent chemoresistance in ovarian cancer

He, Y., Zhu, Q., Chen, M., Huang, Q., Wang, W., Li, Q., Huang, Y., & Di, W. J. (2016) · Oncotarget · doi:10.18632/oncotarget.12223 · Cited by 136 · see citing works

Metabolic and Homeostatic Changes in Seizures and Acquired Epilepsy—Mitochondria, Calcium Dynamics and Reactive Oxygen Species

Kovac, S., Dinkova‐Kostova, A. T., Herrmann, A. M., Melzer, N., Meuth, S. G., & Gorji, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091935 · Cited by 129 · see citing works

Mechanisms of Cadmium-Induced Testicular Injury: A Risk to Male Fertility

Ali, W., Ma, Y., Zhu, J., Zou, H., & Liu, Z. (2022) · Cells · doi:10.3390/cells11223601 · Cited by 127 · see citing works

Genome-wide association and transcriptome studies identify target genes and risk loci for breast cancer

Ferreira, M. A. R., Gamazon, E. R., Al‐Ejeh, F., Aittomäki, K., Andrulis, I. L., Anton‐Culver, H., Arason, A., Arndt, V., Aronson, K. J., Arun, B., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-08053-5 · Cited by 122 · see citing works

Pathway network of pyroptosis and its potential inhibitors in acute kidney injury

Li, N., Wang, Y., Wang, X., Sun, N., & Gong, Y.-H. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.106033 · Cited by 123 · see citing works

Omega-3 PUFA Loaded in Resveratrol-Based Solid Lipid Nanoparticles: Physicochemical Properties and Antineoplastic Activities in Human Colorectal Cancer Cells In Vitro

Serini, S., Cassano, R., Corsetto, P. A., Rizzo, A. M., Calviello, G., & Trombino, S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020586 · Cited by 123 · see citing works

Storage lipid studies in tuberculosis reveal that foam cell biogenesis is disease-specific

Guerrini, V., Prideaux, B., Blanc, L., Bruiners, N., Arrigucci, R., Singh, S., Liang, H.-P. H., Salamon, H., Chen, P., Lakehal, K., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007223 · Cited by 119 · see citing works

A Novel Circular RNA Mediates Pyroptosis of Diabetic Cardiomyopathy by Functioning as a Competing Endogenous RNA

Yang, F., Li, A., Qin, Y., Che, H., Wang, Y., Lv, J., Li, Y., Li, H., Yue, E., Ding, X., et al. (2019) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.06.026 · Cited by 119 · see citing works

Ovulation and ovarian wound healing are impaired with advanced reproductive age

Mara, J. N., Zhou, L. T., Larmore, M. J., Johnson, B., Ayiku, R., Amargant, F., Pritchard, M. T., & Duncan, F. E. (2020) · Aging · doi:10.18632/aging.103237 · Cited by 117 · see citing works

Microglial Corpse Clearance: Lessons From Macrophages

Márquez-Ropero, M., Benito, E., Plaza‐Zabala, A., & Sierra, A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00506 · Cited by 112 · see citing works

Bortezomib in cancer therapy: Mechanisms, side effects, and future proteasome inhibitors

Sogbein, O., Paul, P., Umar, M., Châari, A., Batuman, V., & Upadhyay, R. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.123125 · Cited by 114 · see citing works

Reassessing apoptosis in plants

Dickman, M. B., Williams, B., Li, Y., de Figueiredo, P., & Wolpert, T. (2017) · Nature Plants · doi:10.1038/s41477-017-0020-x · Cited by 112 · see citing works

Guizhi-Shaoyao-Zhimu decoction possesses anti-arthritic effects on type II collagen-induced arthritis in rats via suppression of inflammatory reactions, inhibition of invasion & migration and induction of apoptosis in synovial fibroblasts

Zhang, Q., Peng, W., Wei, S., Wei, D., Li, R., Liu, J., Peng, L., Yang, S., Gao, Y., Wu, C., et al. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109367 · Cited by 111 · see citing works

Relevance of the Pyroptosis-Related Inflammasome Pathway in the Pathogenesis of Diabetic Kidney Disease

Liu, P., Zhang, Z., & Yao, L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.603416 · Cited by 110 · see citing works

NLRP3 inflammasome: The rising star in cardiovascular diseases

Zheng, Y., Li, X., Dong, N., & Li, F. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.927061 · Cited by 109 · see citing works

A Role for the Inflammasome in Spontaneous Preterm Labor With Acute Histologic Chorioamnionitis

Gomez‐Lopez, N., Romero, R. J., Xu, Y., Plazyo, O., Unkel, R., Leng, Y., Than, N. G., Chaiworapongsa, T., Panaitescu, B., Dong, Z., et al. (2017) · Reproductive Sciences · doi:10.1177/1933719116687656 · Cited by 107 · see citing works

Interplay between Cell Death and Cell Proliferation Reveals New Strategies for Cancer Therapy

Loftus, L. V., Amend, S. R., & Pienta, K. J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094723 · Cited by 112 · see citing works

A Role for the Inflammasome in Spontaneous Labor at Term

Romero, R. J., Xu, Y., Plazyo, O., Chaemsaithong, P., Chaiworapongsa, T., Unkel, R., Than, N. G., Chiang, P. J., Dong, Z., Xu, Z., et al. (2016) · American Journal of Reproductive Immunology · doi:10.1111/aji.12440 · Cited by 106 · see citing works

Potentiation of in Vivo Anticancer Efficacy of Selenium Nanoparticles by Mushroom Polysaccharides Surface Decoration

Zeng, D., Zhao, J., Luk, K.-H., Cheung, S.-T., Wong, K., & Chen, T. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b00193 · Cited by 104 · see citing works

Procaspase-3 Overexpression in Cancer: A Paradoxical Observation with Therapeutic Potential

Boudreau, M. W., Peh, J., & Hergenrother, P. J. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00338 · Cited by 104 · see citing works

Tumor-promoting function of apoptotic caspases by an amplification loop involving ROS, macrophages and JNK in Drosophila

Pérez, E., Lindblad, J. L., & Bergmann, A. (2017) · eLife · doi:10.7554/elife.26747 · Cited by 101 · see citing works

Vascular ageing: Underlying mechanisms and clinical implications

Laina, A., Stellos, K., & Stamatelopoulos, K. S. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.06.007 · Cited by 103 · see citing works

Caspases and their role in inflammation and ischemic neuronal death. Focus on caspase-12

de la Cadena, S. G., & Massieu, L. (2016) · APOPTOSIS · doi:10.1007/s10495-016-1247-0 · Cited by 101 · see citing works

MSC-derived exosomes ameliorate erectile dysfunction by alleviation of corpus cavernosum smooth muscle apoptosis in a rat model of cavernous nerve injury

Ouyang, X., Han, X., Chen, Z., Fang, J., Huang, X., & Wei, H. (2018) · Stem Cell Research & Therapy · doi:10.1186/s13287-018-1003-1 · Cited by 100 · see citing works

Caspases in the Developing Central Nervous System: Apoptosis and Beyond

Nguyen, T. T. M., Gillet, G., & Popgeorgiev, N. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.702404 · Cited by 104 · see citing works

Inflammasome activation during spontaneous preterm labor with intra‐amniotic infection or sterile intra‐amniotic inflammation

Gomez‐Lopez, N., Romero, R. J., Panaitescu, B., Leng, Y., Xu, Y., Tarca, A. L., Faro, J. P., Pacora, P., Hassan, S. S., & Hsu, C. (2018) · American Journal of Reproductive Immunology · doi:10.1111/aji.13049 · Cited by 95 · see citing works

Morphological and Phagocytic Profile of Microglia in the Developing Rat Cerebellum

Perez‐Pouchoulen, M., VanRyzin, J. W., & McCarthy, M. M. (2015) · eNeuro · doi:10.1523/eneuro.0036-15.2015 · Cited by 100 · see citing works

Long non-coding RNA Malat1 activated autophagy, hence promoting cell proliferation and inhibiting apoptosis by sponging miR-101 in colorectal cancer

Si, Y., Yang, Z., Ge, Q.-X., Yu, L., Yao, M., Sun, X.-F., Ren, Z., & Ding, C. (2019) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-019-0175-8 · Cited by 94 · see citing works

Seizure-Induced Oxidative Stress in Status Epilepticus: Is Antioxidant Beneficial?

Lin, T., Chen, S., Lin, K.-J., & Chuang, Y. (2020) · Antioxidants · doi:10.3390/antiox9111029 · Cited by 94 · see citing works

Inflammatory Caspases Drive Pyroptosis in Acute Lung Injury

Liu, B., He, R., Zhang, L., Hao, B., Jiang, W., Wang, W., & Geng, Q. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.631256 · Cited by 94 · see citing works

Cardiomyopathy Associated with Diabetes: The Central Role of the Cardiomyocyte

Filardi, T., Ghinassi, B., Baldassarre, A. D., Tanzilli, G., Morano, S., Lenzi, A., Basili, S., & Crescioli, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133299 · Cited by 93 · see citing works

In-vitro evaluation of apoptotic effect of OEO and thymol in 2D and 3D cell cultures and the study of their interaction mode with DNA

Jamali, T., Kavoosi, G., Safavi, M., & Ardestani, S. K. (2018) · Scientific Reports · doi:10.1038/s41598-018-34055-w · Cited by 92 · see citing works

Crosstalk of the Wnt/β-Catenin Signaling Pathway in the Induction of Apoptosis on Cancer Cells

Trejo‐Solís, C., Escamilla-Ramírez, Á., Jiménez‐Farfán, D., Castillo‐Rodríguez, R. A., Flores‐Nájera, A., & Cruz-Salgado, A. (2021) · Pharmaceuticals · doi:10.3390/ph14090871 · Cited by 90 · see citing works

Distinct modes of TNF signaling through its two receptors in health and disease

Atretkhany, K. N., Gogoleva, V. S., Drutskaya, M. S., & Nedospasov, S. A. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.2mr0120-510r · Cited by 89 · see citing works

The Apaf-1 apoptosome induces formation of caspase-9 homo- and heterodimers with distinct activities

Wu, C.-C., Lee, S. H., Malladi, S., Chen, M.-D., Mastrandrea, N. J., Zhang, Z., & Bratton, S. B. (2016) · Nature Communications · doi:10.1038/ncomms13565 · Cited by 89 · see citing works

A matter of regeneration and repair: caspases as the key molecules

Bolkent, Ş., Öztay, F., Gezginci-Oktayoğlu, S., BAŞ, S. S., & Kaçar, A. K. (2016) · TURKISH JOURNAL OF BIOLOGY · doi:10.3906/biy-1507-18 · Cited by 12 · see citing works

Novel roles of apoptotic caspases in tumor repopulation, epigenetic reprogramming, carcinogenesis, and beyond

Zhao, R., Kaakati, R. N., Lee, A. K., Liu, X., Li, F., & Li, C. (2018) · Cancer and Metastasis Reviews · doi:10.1007/s10555-018-9736-y · Cited by 63 · see citing works

When dying is not the end: Apoptotic caspases as drivers of proliferation

Pérez-Garijo, A. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.11.036 · Cited by 59 · see citing works

Non-apoptotic Roles of Caspases in Stem Cell Biology, Carcinogenesis, and Radiotherapy

Kaakati, R. N., Zhao, R., Bao, X., Lee, A. K., Liu, X., Li, F., & Li, C. (2019) · Current Stem Cell Reports · doi:10.1007/s40778-019-0151-2 · Cited by 2 · see citing works

Vital functions for lethal caspases

Launay, S., Hermine, O., Fontenay, M., Kroemer, G., Solary, É., & Garrido, C. (2005) · Oncogene · doi:10.1038/sj.onc.1208524 · Cited by 226 · see citing works