Caspases in apoptosis and beyond

The hallmarks of cancer

Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219 · see citing works

Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics

Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,673 · see citing works

Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade

Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289 · see citing works

Cell Death: The Significance of Apoptosis

Wyllie, A. H., Kerr, J. F. R., & Currie, A. R. (1980) · International review of cytology · doi:10.1016/s0074-7696(08)62312-8 · Cited by 7,235 · see citing works

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

Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c

Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167 · 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

The embryonic cell lineage of the nematode Caenorhabditis elegans

Sulston, J. E., Schierenberg, E., White, J. G., & Thomson, J. N. (1983) · Developmental Biology · doi:10.1016/0012-1606(83)90201-4 · Cited by 4,199 · see citing works

Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors

Luo, X., Budihardjo, I., Zou, H., Slaughter, C., & Wang, X. (1998) · Cell · doi:10.1016/s0092-8674(00)81589-5 · Cited by 3,626 · see citing works

BCL-2 family members and the mitochondria in apoptosisPreprint

Gross, A., McDonnell, J. M., & Korsmeyer, S. J. (1999) · Genes & Development · doi:10.1101/gad.13.15.1899 · Cited by 3,623 · see citing works

Post-embryonic cell lineages of the nematode, Caenorhabditis elegans

Sulston, J. E., & Horvitz, H. R. (1977) · Developmental Biology · doi:10.1016/0012-1606(77)90158-0 · Cited by 3,479 · see citing works

Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β

Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A., & Yuan, J. (2000) · Nature · doi:10.1038/47513 · Cited by 3,262 · see citing works

Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis

Watanabe‐Fukunaga, R., Brannan, C., Copeland, N., Jenkins, N., & Nagata, S. (1992) · Nature · doi:10.1038/356314a0 · Cited by 3,153 · see citing works

Apaf-1, a Human Protein Homologous to C. elegans CED-4, Participates in Cytochrome c–Dependent Activation of Caspase-3

Zou, H., Henzel, W. J., Liu, X., Lutschg, A., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80501-2 · Cited by 3,145 · see citing works

Regulation of Cell Death Protease Caspase-9 by Phosphorylation

Cardone, M. H., Roy, N., Stennicke, H. R., Salvesen, G. S., Franke, T. F., Stanbridge, E. J., Frisch, S. M., & Reed, J. C. (1998) · Science · doi:10.1126/science.282.5392.1318 · Cited by 3,118 · 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

Homozygous Defect in HIV-1 Coreceptor Accounts for Resistance of Some Multiply-Exposed Individuals to HIV-1 Infection

Liu, R., Paxton, W. A., Choe, S., Ceradini, D., Martin, S. R., Horuk, R., MacDonald, M. E., Stuhlmann, H., Koup, R. A., & Landau, N. R. (1996) · Cell · doi:10.1016/s0092-8674(00)80110-5 · Cited by 3,074 · see citing works

Two CD95 (APO‐1/Fas) signaling pathways

Scaffidi, C., Fulda, S., Srinivasan, A., Friesen, C., Li, F., Tomaselli, K. J., Debatin, K., Krammer, P. H., & Peter, M. E. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1675 · Cited by 3,000 · see citing works

Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes

Micheau, O., & Tschopp, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00521-x · Cited by 2,738 · see citing works

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

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

A Combinatorial Approach Defines Specificities of Members of the Caspase Family and Granzyme B

Thornberry, N. A., Rano, T. A., Peterson, E. P., Rasper, D., Timkey, T., Garcia-Calvo, M. M., Houtzager, V. M., Nordstrom, P. A., Roy, S., Vaillancourt, J. P., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.29.17907 · Cited by 2,072 · see citing works

Ordering the Cytochrome c–initiated Caspase Cascade: Hierarchical Activation of Caspases-2, -3, -6, -7, -8, and -10 in a Caspase-9–dependent Manner

Slee, E. A., Harte, M. T., Kluck, R. M., Wolf, B. B., Casiano, C. A., Newmeyer, D. D., Wang, H., Reed, J. C., Nicholson, D. W., Alnemri, E. S., et al. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.2.281 · Cited by 1,932 · see citing works

Molecular mechanisms of caspase regulation during apoptosis

Riedl, S. J., & Shi, Y. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1496 · Cited by 1,893 · see citing works

Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice

Kuida, K., Zheng, T. S., Na, S., Kuan, C.-Y., Yang, D., Karasuyama, H., RAKIC, P. T., & Flavell, R. A. (1996) · Nature · doi:10.1038/384368a0 · Cited by 1,881 · 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

Mechanisms of Caspase Activation and Inhibition during Apoptosis

Shi, Y. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00482-3 · Cited by 1,824 · see citing works

Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf

Mariathasan, S., Newton, K., Monack, D. M., Vucic, D., French, D. M., Lee, W. P., Roose-Girma, M., Erickson, S. L., & Dixit, V. M. (2004) · Nature · doi:10.1038/nature02664 · Cited by 1,822 · see citing works

Reduced Apoptosis and Cytochrome c–Mediated Caspase Activation in Mice Lacking Caspase 9

Kuida, K., Haydar, T. F., Kuan, C.-Y., Gu, Y., Taya, C., Karasuyama, H., Su, M. S.-S., Rakic, P., & Flavell, R. A. (1998) · Cell · doi:10.1016/s0092-8674(00)81476-2 · Cited by 1,643 · 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

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

Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3

Miura, M. (1993) · Cell · doi:10.1016/0092-8674(93)90486-a · Cited by 1,382 · see citing works

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

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

Differential Requirement for Caspase 9 in Apoptotic Pathways In Vivo

Hakem, R., Hakem, A., Duncan, G. S., Henderson, J. T., Woo, M., Soengas, M. S., Elia, A., de la Pompa, J. L., Kägi, D., Khoo, W., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81477-4 · Cited by 1,284 · 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

Caspases 3 and 7: Key Mediators of Mitochondrial Events of Apoptosis

Lakhani, S. A., Masud, A. J., Kuida, K., Porter, G. A., Jr., Booth, C. J., Mehal, W. Z., Inayat, I., & Flavell, R. A. (2006) · Science · doi:10.1126/science.1115035 · Cited by 1,175 · see citing works

C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2

Hengartner, M. O., & Horvitz, H. R. (1994) · Cell · doi:10.1016/0092-8674(94)90506-1 · Cited by 1,167 · see citing works

Molecular Cloning of the Interleukin-1β Converting Enzyme

Cerretti, D. P., Kozlosky, C. J., Mosley, B., Nelson, N. C., Ness, K. V., Greenstreet, T. A., March, C. J., Kronheim, S. R., Druck, T., Cannizzaro, L. A., et al. (1992) · Science · doi:10.1126/science.1373520 · Cited by 1,147 · see citing works

A decade of caspases

Degterev, A., Boyce, M., & Yuan, J. (2003) · Oncogene · doi:10.1038/sj.onc.1207107 · Cited by 1,118 · see citing works

How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?

Chipuk, J. E., & Green, D. R. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.01.007 · Cited by 982 · see citing works

A Unified Model for Apical Caspase Activation

Boatright, K. M., Renatus, M., Scott, F. L., Sperandio, S., Shin, H., Pedersen, I. M., Ricci, J., Edris, W. A., Sutherlin, D. P., Green, D. R., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00051-0 · Cited by 963 · see citing works

Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase

Gottlob, K., Majewski, N., Kennedy, S., Kandel, E., Robey, R. B., & Hay, N. (2001) · Genes & Development · doi:10.1101/gad.889901 · Cited by 961 · see citing works

Inflammatory Caspases

Martinon, F., & Tschopp, J. (2004) · Cell · doi:10.1016/j.cell.2004.05.004 · Cited by 940 · see citing works

Caspase activation: The induced-proximity model

Salvesen, G. S., & Dixit, V. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.10964 · Cited by 932 · see citing works

Three-Dimensional Structure of the Apoptosome

Acehan, D., Jiang, X., Morgan, D. G., Heuser, J. E., Wang, X., & Akey, C. W. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00442-2 · Cited by 912 · see citing works

Nod-like proteins in immunity, inflammation and disease

Fritz, J. H., Ferrero, R. L., Philpott, D. J., & Girardin, S. E. (2006) · Nature Immunology · doi:10.1038/ni1412 · Cited by 889 · see citing works

Caenorhabditis elegans gene ced-9 protects cells from programmed cell death

Hengartner, M. O., Ellis, R. E., & Horvitz, H. R. (1992) · Nature · doi:10.1038/356494a0 · Cited by 889 · see citing works

The protein structures that shape caspase activity, specificity, activation and inhibition

Fuentes‐Prior, P., & Salvesen, G. S. (2004) · Biochemical Journal · doi:10.1042/bj20041142 · Cited by 877 · see citing works

Inflammatory caspases and inflammasomes: master switches of inflammation

Martinon, F., & Tschopp, J. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402038 · Cited by 821 · see citing works

Apoptosis and caspases regulate death and inflammation in sepsis

Hotchkiss, R. S., & Nicholson, D. W. (2006) · Nature reviews. Immunology · doi:10.1038/nri1943 · Cited by 796 · see citing works

Requirement for Caspase-2 in Stress-Induced Apoptosis Before Mitochondrial Permeabilization

Lassus, P., Opitz-Araya, X., & Lazebnik, Y. A. (2002) · Science · doi:10.1126/science.1074721 · Cited by 719 · 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

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

Defects in regulation of apoptosis in caspase-2-deficient micePreprint

Bergeron, L., Perez, G. I., MacDonald, G., Shi, L., Sun, Y., Jurisicova, A., Varmuza, S., Latham, K. E., Flaws, J. A., Salter, J. C. M., et al. (1998) · Genes & Development · doi:10.1101/gad.12.9.1304 · Cited by 681 · see citing works

NLRs join TLRs as innate sensors of pathogens

Martinon, F., & Tschopp, J. (2005) · Trends in Immunology · doi:10.1016/j.it.2005.06.004 · Cited by 673 · 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

Anti-inflammatory therapies to treat sepsis and septic shock

Zéni, F., Freeman, B. D., & Natanson, C. (1997) · Critical Care Medicine · doi:10.1097/00003246-199707000-00001 · Cited by 656 · see citing works

Interleukin-1–Receptor Antagonist in the Muckle–Wells Syndrome

Hawkins, P. N., Lachmann, H. J., & McDermott, M. F. (2003) · New England Journal of Medicine · doi:10.1056/nejm200306193482523 · Cited by 654 · see citing works

Inherited Human Caspase 10 Mutations Underlie Defective Lymphocyte and Dendritic Cell Apoptosis in Autoimmune Lymphoproliferative Syndrome Type II

Wang, J., Zheng, L., Lobito, A. A., Chan, F. K.-M., Dale, J. K., Sneller, M. C., Xu, Y., Puck, J. M., Straus, S. E., & Lenardo, M. J. (1999) · Cell · doi:10.1016/s0092-8674(00)80605-4 · Cited by 639 · see citing works

Akt-Directed Glucose Metabolism Can Prevent Bax Conformation Change and Promote Growth Factor-Independent Survival

Rathmell, J. C., Fox, C. J., Plas, D. R., Hammerman, P. S., Cinalli, R. M., & Thompson, C. B. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7315-7328.2003 · Cited by 572 · see citing works

Prevention of cold-associated acute inflammation in familial cold autoinflammatory syndrome by interleukin-1 receptor antagonist

Hoffman, H. M., Rosengren, S., Boyle, D. L., Cho, J. Y., Nayar, J., Mueller, J. L., Anderson, J. P., Wanderer, A. A., & Firestein, G. S. (2004) · The Lancet · doi:10.1016/s0140-6736(04)17401-1 · 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

Targeting programmed cell death in neurodegenerative diseases

Vila, M., & Przedborski, S. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1100 · Cited by 545 · see citing works

Caspase inhibitors improve survival in sepsis: a critical role of the lymphocyte

Hotchkiss, R. S., Chang, K., Swanson, P. E., Tinsley, K. W., Hui, J. J., Klender, P. M., Xanthoudakis, S., Roy, S., Black, C. A., Grimm, E. L., et al. (2000) · Nature Immunology · doi:10.1038/82741 · Cited by 526 · see citing works

Essential requirement for caspase-8/FLICE in the initiation of the Fas-induced apoptotic cascade

Juo, P., Kuo, C. J., Yuan, J., & Blenis, J. (1998) · Current Biology · doi:10.1016/s0960-9822(07)00420-4 · Cited by 524 · see citing works

Caspase-2 Induces Apoptosis by Releasing Proapoptotic Proteins from Mitochondria

Guo, Y., Srinivasula, S. M., Druilhe, A., Fernandes‐Alnemri, T., & Alnemri, E. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108029200 · Cited by 521 · 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

The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection

Zamboni, D. S., Kobayashi, K. S., Kohlsdorf, T., Ogura, Y., Long, E. M., Vance, R. E., Kuida, K., Mariathasan, S., Dixit, V. M., Flavell, R. A., et al. (2006) · Nature Immunology · doi:10.1038/ni1305 · Cited by 515 · see citing works

Death receptor signaling

Lavrik, I. N., Golks, A., & Krammer, P. H. (2005) · Journal of Cell Science · doi:10.1242/jcs.01610 · Cited by 494 · see citing works

Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK

Allan, L. A., MORRICE, N. A., Brady, S. C., Magee, G. J., Pathak, S., & Clarke, P. R. (2003) · Nature Cell Biology · doi:10.1038/ncb1005 · Cited by 474 · see citing works

Identification of Ipaf, a Human Caspase-1-activating Protein Related to Apaf-1

Poyet, J., Srinivasula, S. M., Tnani, M., Razmara, M., Fernandes‐Alnemri, T., & Alnemri, E. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100250200 · Cited by 456 · see citing works

Prevention of lymphocyte cell death in sepsis improves survival in mice

Hotchkiss, R. S., Tinsley, K. W., Swanson, P. E., Chang, K. C., Cobb, J. P., Buchman, T. G., Korsmeyer, S. J., & Karl, I. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.25.14541 · Cited by 454 · see citing works

The CASBAH: a searchable database of caspase substrates

Lüthi, A. U., & Martin, S. J. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402103 · Cited by 434 · see citing works

Requirement for Caspase-8 in NF-κB Activation by Antigen Receptor

Su, H. C., Bidère, N., Zheng, L., Cubre, A., Sakai, K., Dale, J. K., Salmena, L., Hakem, R., Straus, S. E., & Lenardo, M. J. (2005) · Science · doi:10.1126/science.1104765 · Cited by 427 · 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

Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1

Qin, H., Srinivasula, S. M., Wu, G., Fernandes‐Alnemri, T., Alnemri, E. S., & Shi, Y. (1999) · Nature · doi:10.1038/21124 · Cited by 421 · see citing works

Direct coupling of the cell cycle and cell death machinery by E2F

Nahle, Z., Polakoff, J., Davuluri, R. V., McCurrach, M. E., Jacobson, M. D., Narita, M., Zhang, M. Q., Lazebnik, Y., Bar-Sagi, D., & Lowe, S. W. (2002) · Nature Cell Biology · doi:10.1038/ncb868 · Cited by 421 · see citing works

Caspase-2 Acts Upstream of Mitochondria to Promote Cytochromec Release during Etoposide-induced Apoptosis

Robertson, J. D., Enoksson, M., Suomela, M., Zhivotovsky, B., & Orrenius, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204185200 · Cited by 409 · see citing works

The Caenorhabditis elegans cell death gene ced-4 encodes a novel protein and is expressed during the period of extensive programmed cell death

Yuan, J., & Horvitz, H. R. (1992) · Development · doi:10.1242/dev.116.2.309 · Cited by 403 · 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

Caspase-2 Mediates Neuronal Cell Death Induced by β-Amyloid

Troy, C. M., Rabacchi, S. A., Friedman, W., Frappier, T. F., Brown, K. R., & Shelanski, M. L. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-04-01386.2000 · Cited by 354 · see citing works

Pidd, a new death-domain–containing protein, is induced by p53 and promotes apoptosis

Lin, Y., Ma, W., & Benchimol, S. (2000) · Nature Genetics · doi:10.1038/79102 · Cited by 353 · see citing works

Caspase Activation

Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.06.007 · Cited by 349 · see citing works

The mouse fas-ligand gene is mutated in gld mice and is part of a TNF family gene cluster

Lynch, D. H., Watson, M. L., Alderson, M. R., Baum, P. R., Miller, R. E., Tough, T. W., Gibson, M., Davis-Smyth, T., Smiths, C. A., Hunter, K. W., et al. (1994) · Immunity · doi:10.1016/1074-7613(94)90106-6 · Cited by 331 · see citing works

Dual Role of Caspase-11 in Mediating Activation of Caspase-1 and Caspase-3 under Pathological Conditions

Kang, S.-J., Wang, S., Hara, H., Peterson, E. P., Namura, S., Amin‐Hanjani, S., Huang, Z., Srinivasan, A. N., Tomaselli, K. J., Thornberry, N. A., et al. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.3.613 · Cited by 326 · 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

PIDD Mediates NF-κB Activation in Response to DNA Damage

Janssens, S., Tinel, A., Lippens, S., & Tschopp, J. (2005) · Cell · doi:10.1016/j.cell.2005.09.036 · Cited by 319 · see citing works

Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8

Stennicke, H. R., Renatus, M., Meldal, M., & Salvesen, G. S. (2000) · Biochemical Journal · doi:10.1042/bj3500563 · Cited by 316 · 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

An Inherited Disorder of Lymphocyte Apoptosis: The Autoimmune Lymphoproliferative Syndrome

Straus, S. E., Sneller, M., Lenardo, M. J., Puck, J. M., & Strober, W. (1999) · Annals of Internal Medicine · doi:10.7326/0003-4819-130-7-199904060-00020 · Cited by 290 · 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

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

Caspase-14 reveals its secrets

Denecker, G., Ovaere, P., Vandenabeele, P., & Declercq, W. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709098 · Cited by 252 · see citing works

Metabolic Regulation of Oocyte Cell Death through the CaMKII-Mediated Phosphorylation of Caspase-2

Nutt, L. K., Margolis, S. S., Jensen, M. V., Herman, C. E., Dunphy, W. G., Rathmell, J. C., & Kornbluth, S. A. (2005) · Cell · doi:10.1016/j.cell.2005.07.032 · Cited by 249 · see citing works

Crystal Structure of a Procaspase-7 Zymogen

Chai, J., Wu, Q. Y., Shiozaki, E. N., Srinivasula, S. M., Alnemri, E. S., & Shi, Y. (2001) · Cell · doi:10.1016/s0092-8674(01)00544-x · Cited by 246 · 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

Phosphorylation of Caspase-9 by CDK1/Cyclin B1 Protects Mitotic Cells against Apoptosis

Allan, L. A., & Clarke, P. R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.019 · Cited by 237 · see citing works

Identification and Characterization of Ich-3, a Member of the Interleukin-1β Converting Enzyme (ICE)/Ced-3 Family and an Upstream Regulator of ICE

Wang, S., Miura, M., Jung, Y., Zhu, H., Gagliardini, V., Shi, L. F., Greenberg, A. H., & Yuan, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20580 · Cited by 236 · see citing works

Structural basis for the activation of human procaspase-7

Riedl, S. J., Fuentes‐Prior, P., Renatus, M., Kairies, N., Krapp, S., Huber, R., Salvesen, G. S., & Bode, W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221580098 · Cited by 220 · see citing works

Expression Analysis of the Human Caspase-1 Subfamily Reveals Specific Regulation of the CASP5 Gene by Lipopolysaccharide and Interferon-γ

Lin, X. Y., Choi, M. S. K., & Porter, A. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007255200 · Cited by 194 · 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

In vivo delivery of caspase-8 or Fas siRNA improves the survival of septic mice

Szollosi, D. E., Chung, C., Lomas‐Neira, J., Doughty, L., Gregory, S. H., & Ayala, A. (2005) · Blood · doi:10.1182/blood-2004-10-4086 · Cited by 177 · see citing works

Role of Caspase in a Subset of Human Platelet Activation Responses

Shcherbina, A. Y., & Remold‐O’Donnell, E. (1999) · Blood · doi:10.1182/blood.v93.12.4222 · Cited by 159 · see citing works

A Structure of the Human Apoptosome at 12.8 Å Resolution Provides Insights into This Cell Death Platform

Yu, X., Acehan, D., Ménétret, J., et al. (2005) · Structure · doi:10.1016/j.str.2005.09.006 · Cited by 149 · see citing works

Caspase-11 regulates cell migration by promoting Aip1–Cofilin-mediated actin depolymerization

Li, J., Brieher, W. M., Scimone, M. L., Kang, S. J., Zhu, H., Yin, H. L., von Andrian, U. H., Mitchison, T. J., & Yuan, J. (2007) · Nature Cell Biology · doi:10.1038/ncb1541 · Cited by 134 · see citing works

Caspase-8 Promotes Cell Motility and Calpain Activity under Nonapoptotic Conditions

Helfer, B. M., Boswell, B. C., Finlay, D., Ciprés, A., Vuori, K., Kang, T., Wallach, D., Dorfleutner, A., Lahti, J. M., Flynn, D. C., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4183 · Cited by 129 · 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

NAIP and Ipaf Control Legionella pneumophila Replication in Human Cells

Vinzing, M., Eitel, J., Lippmann, J., Hocke, A. C., Zahlten, J., Slevogt, H., N’Guessan, P. D., Günther, S., Schmeck, B., Hippenstiel, S., et al. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.10.6808 · Cited by 124 · see citing works

Beginnings of a signal-transduction pathway for bioenergetic control of cell survival

Hammerman, P. S., Fox, C. J., & Thompson, C. B. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.09.008 · Cited by 115 · see citing works

Lens Fibre Cell Differentiation – A Link with Apoptosis?

Dahm, R. (1999) · Ophthalmic Research · doi:10.1159/000055530 · Cited by 110 · see citing works

Crystal Structure of Caspase-2, Apical Initiator of the Intrinsic Apoptotic Pathway

Schweizer, A., Briand, C., & Grütter, M. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304895200 · Cited by 106 · see citing works

Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD

Berube, C., Boucher, L.-M., Ma, W., Wakeham, A. C., Salmena, L., Hakem, R., Yeh, W., Mak, T. W., & Benchimol, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506475102 · Cited by 105 · see citing works

Is caspase‐dependent apoptosis only cell differentiation taken to the extreme?

Fernando, P., & Megeney, L. A. (2006) · The FASEB Journal · doi:10.1096/fj.06-5912hyp · Cited by 104 · see citing works

Caspase-14: Analysis of Gene Structure and mRNA Expression during Keratinocyte Differentiation

Eckhart, L., Ban, J., Fischer, H., et al. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3698 · Cited by 88 · see citing works

A genome-wide RNAi screen reveals multiple regulators of caspase activation

Yi, C. H., Sogah, D. K., Boyce, M., Degterev, A., Christofferson, D. E., & Yuan, J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200708090 · Cited by 80 · see citing works

Regulation of Caspase 9 through Phosphorylation by Protein Kinase C Zeta in Response to Hyperosmotic Stress

Brady, S. C., Allan, L. A., & Clarke, P. R. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.23.10543-10555.2005 · Cited by 79 · see citing works

Caspases as therapeutic targets

Howley, B. A., & Fearnhead, H. O. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00292.x · Cited by 72 · see citing works

Apoptosis in the treatment of cancer: a promise kept?

Meng, X. W., Lee, S. H., & Kaufmann, S. H. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.10.008 · Cited by 65 · see citing works

p53-induced protein with a death domain (PIDD) isoforms differentially activate nuclear factor-kappaB and caspase-2 in response to genotoxic stress

Cuenin, S., Tinel, A., Janssens, S., & Tschopp, J. (2007) · Oncogene · doi:10.1038/sj.onc.1210635 · Cited by 58 · see citing works

CASPASES -2, -3, -6, AND -9, BUT NOT CASPASE-1, ARE ACTIVATED IN SEPSIS-INDUCED THYMOCYTE APOPTOSIS

Tinsley, K. W., Cheng, S. L., Buchman, T. G., et al. (2000) · Shock · doi:10.1097/00024382-200013010-00001 · Cited by 45 · 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

Brown seaweed fucoidan: Biological activity and apoptosis, growth signaling mechanism in cancer

Senthilkumar, K., Manivasagan, P., Venkatesan, J., & Kim, S.-K. (2013) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2013.06.030 · Cited by 340 · see citing works

An overview of apoptosis assays detecting DNA fragmentation

Majtnerová, P., & Roušar, T. (2018) · Molecular Biology Reports · doi:10.1007/s11033-018-4258-9 · Cited by 330 · see citing works

Fucoidan extract induces apoptosis in MCF-7 cells via a mechanism involving the ROS-dependent JNK activation and mitochondria-mediated pathways

Zhang, Z., Teruya, K., Eto, H., & Shirahata, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027441 · Cited by 167 · see citing works

Caspase 3 Inactivation Protects Against Hepatic Cell Death and Ameliorates Fibrogenesis in a Diet-Induced NASH Model

Thapaliya, S., Wree, A., Povero, D., Inzaugarat, M. E., Berk, M., Dixon, L., Papouchado, B. G., & Feldstein, A. E. (2014) · Digestive Diseases and Sciences · doi:10.1007/s10620-014-3167-6 · Cited by 162 · see citing works

Following Cytochrome <i>c</i> Release, Autophagy Is Inhibited during Chemotherapy-Induced Apoptosis by Caspase 8–Mediated Cleavage of Beclin 1

Li, H., Wang, P., Sun, Q., Ding, W.-X., Yin, X.-M., Sobol, R. W., Stolz, D. B., Yu, J., & Zhang, L. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-4475 · Cited by 150 · see citing works

Regulation of muscle atrophy in aging and disease

Vinciguerra, M., Musaro, A., & Rosenthal, N. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_15 · Cited by 149 · see citing works

Fas-Mediated Apoptosis Is Regulated by the Extracellular Matrix Protein CCN1 (CYR61) In Vitro and In Vivo

Juric, V., Chen, C.-C., & Lau, L. F. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00064-09 · Cited by 70 · see citing works

Matrix Protein CCN1 Is Critical for Prostate Carcinoma Cell Proliferation and TRAIL-Induced Apoptosis

Franzen, C. A., Chen, C.-C., Todorović, V., Juric, V., Monzon, R. I., & Lau, L. F. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0017 · Cited by 66 · see citing works

Globular adiponectin as a complete mesoangioblast regulator: Role in proliferation, survival, motility, and skeletal muscle differentiation

Fiaschi, T., Tedesco, F. S., Giannoni, E., Diaz-Manera, J., Parri, M., Cossu, G., & Chiarugi, P. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-04-0310 · Cited by 35 · see citing works

Bioprophylactic potential of novel human colostrum probiotics via apoptotic induction of colon cancer cells and cell immune activation

Srikham, K., & Thirabunyanon, M. (2022) · Biomedicine &amp; Pharmacotherapy · doi:10.1016/j.biopha.2022.112871 · Cited by 24 · see citing works

Caspases and programmed cell death in the hypersensitive response of plants to pathogens

del Pozo, O., & Lam, E. W. ‐. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70469-5 · Cited by 425 · see citing works

Caspase-independent programmed cell death with necrotic morphology

Kitanaka, C., & Kuchino, Y. (1999) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400526 · Cited by 376 · see citing works

[Caspase-independent programmed cell death with necrotic morphology].

Kitanaka, C., & Kuchino, Y. (1999) · PubMed · Cited by 3 · see citing works

Programmed cell death and its clinical implications.

Katoch, B., Sebastian, S., Sahdev, S., Padh, H., Hasnain, S. E., & Begum, R. (2002) · PubMed · Cited by 25 · see citing works

Roles of Caspases in the Programmed Cell Death of Motoneurons in vivo.

Yaginuma, H., Sato, N., Homma, S., et al. (2001) · Archivum histologicum japonicum · doi:10.1679/aohc.64.461 · Cited by 18 · see citing works