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Caspase-1: is IL-1 just the tip of the ICEberg?
Open accessAbstract
Caspase-1, formerly known as interleukin (IL)-1-converting enzyme is best established as the protease responsible for the processing of the key pro-inflammatory cytokine IL-1β from an inactive precursor to an active, secreted molecule. Thus, caspase-1 is regarded as a key mediator of inflammatory processes, and has become synonymous with inflammation. In addition to the processing of IL-1β, caspase-1 also executes a rapid programme of cell death, termed pyroptosis, in macrophages in response to intracellular bacteria. Pyroptosis is also regarded as a host response to remove the niche of the bacteria and to hasten their demise. These processes are generally accepted as the main roles of caspase-1. However, there is also a wealth of literature supporting a direct role for caspase-1 in non-infectious cell death processes. This is true in mammals, but also in non-mammalian vertebrates where caspase-1-dependent processing of IL-1β is absent because of the lack of appropriate caspase-1 cleavage sites. This literature is most prevalent in the brain where caspase-1 may directly regulate neuronal cell death in response to diverse insults. We attempt here to summarise the evidence for caspase-1 as a cell death enzyme and propose that, in addition to the processing of IL-1β, caspase-1 has an important and a conserved role as a cell death protease.
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Cites
Pattern Recognition Receptors and Inflammation
Takeuchi, O., & Akira, S. (2010) · Cell · doi:10.1016/j.cell.2010.01.022 · Cited by 8,895
Schroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475
NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals
Duewell, P., Kono, H., Rayner, K. J., Sirois, C. M., Vladimer, G., Bauernfeind, F. G., Abela, G. S., Franchi, L., Nuñez, G., Schnurr, M., et al. (2010) · Nature · doi:10.1038/nature08938 · Cited by 4,026
Pyroptosis: host cell death and inflammation
Bergsbaken, T., Fink, S. L., & Cookson, B. T. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2070 · Cited by 3,183
Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A., & Latz, E. (2008) · Nature Immunology · doi:10.1038/ni.1631 · Cited by 3,065
Sterile inflammation: sensing and reacting to damage
Chen, G. Y., & Nuñez, G. (2010) · Nature Reviews Immunology · doi:10.1038/nri2873 · Cited by 3,051
A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,572
Yuan, J. (1993) · Cell · doi:10.1016/0092-8674(93)90485-9 · Cited by 2,483
The NALP3 inflammasome is involved in the innate immune response to amyloid-β
Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T. (2008) · Nature Immunology · doi:10.1038/ni.1636 · Cited by 2,441
Human ICE/CED-3 Protease Nomenclature
Alnemri, E. S., Livingston, D. J., Nicholson, D. W., Salvesen, G., Thornberry, N. A., Wong, W. W., & Yuan, J. (1996) · Cell · doi:10.1016/s0092-8674(00)81334-3 · Cited by 2,372
Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
Shimada, K., Crother, T. R., Karlin, J., Dagvadorj, J., Chiba, N., Chen, S., Ramanujan, V. K., Wolf, A. J., Vergnes, L., Ojcius, D. M., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.009 · Cited by 2,282
Interleukin-1 in the pathogenesis and treatment of inflammatory diseases
Dinarello, C. A. (2011) · Blood · doi:10.1182/blood-2010-07-273417 · Cited by 2,248
Inflammasomes in health and disease
Strowig, T., Henao-Mejia, J., Elinav, E., & Flavell, R. (2012) · Nature · doi:10.1038/nature10759 · Cited by 2,230
AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
Fernandes-Alnemri, T., Yu, J.-W., Datta, P., Wu, J., & Alnemri, E. S. (2009) · Nature · doi:10.1038/nature07710 · Cited by 1,831
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 1,616
Understanding the mechanism of IL-1β secretion
Lopez-Castejon, G., & Brough, D. (2011) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2011.10.001 · Cited by 1,519
Li, P., Allen, H., Banerjee, S., Franklin, S., Herzog, L., Johnston, C., McDowell, J., Paskind, M., Rodman, L., Salfeld, J., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90490-5 · Cited by 1,417
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
Activation of Interferon-γ Inducing Factor Mediated by Interleukin-1β Converting Enzyme
Gu, Y., Kuida, K., Tsutsui, H., Ku, G., Hsiao, K., Fleming, M. A., Hayashi, N., Higashino, K., Okamura, H., Nakanishi, K., et al. (1997) · Science · doi:10.1126/science.275.5297.206 · Cited by 1,155
Interleukin-1 and neuronal injury
Allan, S. M., Tyrrell, P. J., & Rothwell, N. J. (2005) · Nature Reviews Immunology · doi:10.1038/nri1664 · Cited by 992
Ray, C. A., Black, R. A., Kronheim, S. R., Greenstreet, T. A., Sleath, P. R., Salvesen, G. S., & Pickup, D. J. (1992) · Cell · doi:10.1016/0092-8674(92)90223-y · Cited by 978
The Sterile Inflammatory Response
Rock, K. L., Latz, E., Ontiveros, F., & Kono, H. (2010) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101311 · Cited by 865
Hara, H., Friedlander, R. M., Gagliardini, V., Ayata, C., Fink, K., Huang, Z., Shimizu-Sasamata, M., Yuan, J., & Moskowitz, M. A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.5.2007 · Cited by 834
Perregaux, D., & Gabel, C. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36591-2 · Cited by 758
Involvement of an ICE-like protease in Fas-mediated apoptosis
Enari, M., Hug, H., & Nagata, S. (1995) · Nature · doi:10.1038/375078a0 · Cited by 734
Functional Role of Caspase-1 and Caspase-3 in an ALS Transgenic Mouse Model
Li, M., Ona, V. O., Guégan, C., Chen, M., Jackson-Lewis, V., Andrews, L. J., Olszewski, A. J., Stieg, P. E., Lee, J.-P., Przedborski, S., et al. (2000) · Science · doi:10.1126/science.288.5464.335 · Cited by 716
The IL-1-like cytokine IL-33 is inactivated after maturation by caspase-1
Cayrol, C., & Girard, J.-P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812690106 · Cited by 707
Prevention of Vertebrate Neuronal Death by the crmA Gene
Gagliardini, V., Fernandez, P.-A., Lee, R. K. K., Drexler, H. C. A., Rotello, R. J., Fishman, M. C., & Yuan, J. (1994) · Science · doi:10.1126/science.8303301 · Cited by 612
Requirement of an ICE/CED-3 protease for Fas/APO-1-mediated apoptosis
Los, M., Craen, M. V. D., Penning, L. C., Schenk, H., Westendorp, M., Baeuerle, P. A., Dröge, W., Krammer, P. H., Fiers, W., & Schulze-Osthoff, K. (1995) · Nature · doi:10.1038/375081a0 · Cited by 607
Interleukin-1 as a Pathogenetic Mediator of Ischemic Brain Damage in Rats
Yamasaki, Y., Matsuura, N., Shozuhara, H., Onodera, H., Itoyama, Y., & Kogure, K. (1995) · Stroke · doi:10.1161/01.str.26.4.676 · Cited by 572
IL-1α and IL-1β Recruit Different Myeloid Cells and Promote Different Stages of Sterile Inflammation
Rider, P., Carmi, Y., Guttman, O., Braiman, A., Cohen, I., Voronov, E., White, M. R., Dinarello, C. A., & Apte, R. N. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1102048 · Cited by 522
Poeck, H., Bscheider, M., Gross, O., Finger, K., Roth, S., Rebsamen, M., Hannesschläger, N., Schlee, M., Rothenfusser, S., Barchet, W., et al. (2010) · Nature Immunology · doi:10.1038/ni.1824 · Cited by 521
Identification of a monocyte specific pre-interleukin 1 beta convertase activity.
Kostura, M. J., Tocci, M. J., Limjuco, G., Chin, J., Cameron, P., Hillman, A. G., Chartrain, N. A., & Schmidt, J. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.14.5227 · Cited by 518
Caspase-8 and Bid: Caught in the act between death receptors and mitochondria
Kantari, C., & Walczak, H. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.01.026 · Cited by 502
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
Role of IL-1α and IL-1β in Ischemic Brain Damage
Boutin, H., LeFeuvre, R. A., Horai, R., Asano, M., Iwakura, Y., & Rothwell, N. J. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-15-05528.2001 · Cited by 477
Impaired IL-18 processing protects caspase-1–deficient mice from ischemic acute renal failure
Melnikov, V. Y., Ecder, T., Fantuzzi, G., Siegmund, B., Lucia, M. S., Dinarello, C. A., Schrier, R. W., & Edelstein, C. L. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12089 · Cited by 476
Interleukin 1 is processed and released during apoptosis.
Hogquist, K. A., Nett, M. A., Unanue, E. R., & Chaplin, D. D. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8485 · Cited by 456
Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death
Vucic, D., Dixit, V. M., & Wertz, I. E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3143 · Cited by 444
Fink, S. L., Bergsbaken, T., & Cookson, B. T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707370105 · Cited by 403
Stein, C., Caccamo, M., Laird, G., & Leptin, M. (2007) · Genome Biology · doi:10.1186/gb-2007-8-11-r251 · Cited by 374
Friedlander, R. M., Gagliardini, V., Hara, H., Fink, K. B., Li, W., MacDonald, G., Fishman, M. C., Greenberg, A. H., Moskowitz, M. A., & Yuan, J. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.5.933 · Cited by 348
Targeted Peptidecentric Proteomics Reveals Caspase-7 as a Substrate of the Caspase-1 Inflammasomes
Lamkanfi, M., Kanneganti, T.-D., Van Damme, P., Vanden Berghe, T., Vanoverberghe, I., Vandekerckhove, J., Vandenabeele, P., Gevaert, K., & Nuénñez, G. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800132-mcp200 · Cited by 341
An NLRP7-Containing Inflammasome Mediates Recognition of Microbial Lipopeptides in Human Macrophages
Khare, S., Dorfleutner, A., Bryan, N. B., Yun, C., Radian, A. D., de Almeida, L., Rojanasakul, Y., & Stehlik, C. (2012) · Immunity · doi:10.1016/j.immuni.2012.02.001 · Cited by 339
Muñoz-Planillo, R., Franchi, L., Miller, L. S., & Núñez, G. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900729 · Cited by 336
A Molecular Platform in Neurons Regulates Inflammation after Spinal Cord Injury
de Rivero Vaccari, J. P., Lotocki, G., Marcillo, A. E., Dietrich, W. D., & Keane, R. W. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.0157-08.2008 · Cited by 332
Inhibition of ICE slows ALS in mice
Friedlander, R. M., Brown, R. H., Gagliardini, V., Wang, J., & Yuan, J. (1997) · Nature · doi:10.1038/40299 · Cited by 332
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
Howard, A. D., Kostura, M. J., Thornberry, N., Ding, G. J., Limjuco, G., Weidner, J., Salley, J. P., Hogquist, K. A., Chaplin, D. D., & Mumford, R. A. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.147.9.2964 · Cited by 323
Shao, W., Yeretssian, G., Doiron, K., Hussain, S. N., & Saleh, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708182200 · Cited by 322
Abulafia, D. P., de Rivero Vaccari, J. P., Lozano, J. D., Lotocki, G., Keane, R. W., & Dietrich, W. D. (2009) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2008.143 · Cited by 322
Bcl-2 and Bcl-XL Regulate Proinflammatory Caspase-1 Activation by Interaction with NALP1
Bruey, J.-M., Bruey-Sedano, N., Luciano, F., Zhai, D., Balpai, R., Xu, C., Kress, C. L., Bailly-Maitre, B., Li, X., Osterman, A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.01.045 · Cited by 319
Mutant superoxide dismutase 1-induced IL-1β accelerates ALS pathogenesis
Meissner, F., Molawi, K., & Zychlinsky, A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002396107 · Cited by 318
Milligan, C. E., Prevette, D., Yaginuma, H., Homma, S., Cardwellt, C., Fritz, L. C., Tomaselli, K. J., Oppenheim, R. W., & Schwartz, L. M. (1995) · Neuron · doi:10.1016/0896-6273(95)90042-x · Cited by 313
Pomerantz, B. J., Reznikov, L. L., Harken, A. H., & Dinarello, C. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041611398 · Cited by 310
Caspases at the crossroads of immune-cell life and death
Siegel, R. M. (2006) · Nature Reviews Immunology · doi:10.1038/nri1809 · Cited by 305
Caspase 1–independent activation of interleukin‐1β in neutrophil‐predominant inflammation
Guma, M., Ronacher, L., Liu‐Bryan, R., Takai, S., Karin, M., & Corr, M. (2009) · Arthritis & Rheumatism · doi:10.1002/art.24959 · Cited by 304
Caspase Inhibition Reduces Myocyte Cell Death Induced by Myocardial Ischemia and Reperfusion In Vivo
Holly, T. A., Drincic, A., Byun, Y., Nakamura, S., Harris, K., Klocke, F. J., & Cryns, V. L. (1999) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1999.1006 · Cited by 303
Reduced Ischemic Brain Injury in Interleukin-1β Converting Enzyme—Deficient Mice
Schielke, G. P., Yang, G.-Y., Shivers, B. D., & Betz, A. L. (1998) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199802000-00009 · Cited by 302
Joosten, L. A. B., Netea, M. G., Fantuzzi, G., Koenders, M. I., Helsen, M. M. A., Sparrer, H., Pham, C. T., van der Meer, J. W. M., Dinarello, C. A., & van den Berg, W. B. (2009) · Arthritis & Rheumatism · doi:10.1002/art.25006 · Cited by 296
Interleukin-18 Involvement in Hypoxic–Ischemic Brain Injury
Hedtjärn, M., Leverin, A.-L., Eriksson, K., Blomgren, K., Mallard, C., & Hagberg, H. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-14-05910.2002 · Cited by 290
Bird, S., Zou, J., Wang, T., Munday, B., Cunningham, C., & Secombes, C. J. (2002) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(02)00028-x · Cited by 266
Specific Caspase Pathways Are Activated in the Two Stages of Cerebral Infarction
Benchoua, A., Guégan, C., Couriaud, C., Hosseini, H., Sampaı̈o, N., Morin, D., & Onténiente, B. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-18-07127.2001 · Cited by 246
Tsutsui, H., Kayagaki, N., Kuida, K., Nakano, H., Hayashi, N., Takeda, K., Matsui, K., Kashiwamura, S.-I., Hada, T., Akira, S., et al. (1999) · Immunity · doi:10.1016/s1074-7613(00)80111-9 · Cited by 243
Response to local inflammation of IL-1 beta-converting enzyme- deficient mice
Fantuzzi, G., Ku, G., Harding, M. W., Livingston, D. J., Sipe, J. D., Kuida, K., Flavell, R. A., & Dinarello, C. A. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.4.1818 · Cited by 232
An Inflammasome-Independent Role for Epithelial-Expressed Nlrp3 in Renal Ischemia-Reperfusion Injury
Shigeoka, A. A., Mueller, J. L., Kambo, A., Mathison, J. C., King, A. J., Hall, W. F., Correia, J. D. S., Ulevitch, R. J., Hoffman, H. M., & McKay, D. B. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1002330 · Cited by 229
Pasinelli, P., Borchelt, D. R., Houseweart, M. K., Cleveland, D. W., & Brown, R. H. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15763 · Cited by 221
Inflammatory Stimuli Regulate Caspase Substrate Profiles
Agard, N. J., Maltby, D., & Wells, J. A. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900528-mcp200 · Cited by 216
Fundamental role of the Rip2/caspase-1 pathway in hypoxia and ischemia-induced neuronal cell death
Zhang, W.-H., Wang, X., Narayanan, M., Zhang, Y., Huo, C., Reed, J. C., & Friedlander, R. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2534856100 · Cited by 211
Rabuffetti, M., Sciorati, C., Tarozzo, G., Clementi, E., Manfredi, A. A., & Beltramo, M. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-12-04398.2000 · Cited by 196
Caspase-7 Activation by the Nlrc4/Ipaf Inflammasome Restricts Legionella pneumophila Infection
Akhter, A., Gavrilin, M. A., Frantz, L., Washington, S., Ditty, C., Limoli, D., Day, C., Sarkar, A., Newland, C., Butchar, J., et al. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000361 · Cited by 193
Le Feuvre, R. A., Brough, D., Iwakura, Y., Takeda, K., & Rothwell, N. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m104388200 · Cited by 192
Self-citationEffect of endotoxin in IL-1 β-deficient mice
Fantuzzi, G., Zheng, H., Faggioni, R., Benigni, F., Ghezzi, P., Sipe, J. D., Shaw, A. R., & Dinarello, C. A. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.157.1.291 · Cited by 190
Troy, C. M., Stefanis, L., Prochiantz, A., Greene, L. A., & Shelanski, M. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5635 · Cited by 190
Mulcahy, N. J., Ross, J., Rothwell, N. J., & Loddick, S. A. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705462 · Cited by 185
Functional role of interleukin 1 beta (IL-1 beta) in IL-1 beta-converting enzyme-mediated apoptosis.
Friedlander, R. M., Gagliardini, V, Rotello, R. J., & Yuan, J. (1996) · The Journal of experimental medicine · doi:10.1084/jem.184.2.717 · Cited by 183
Encyclopedia of Molecular Pharmacology
Offermanns, S., & Rakush, V. (2008) · Springer eBooks · doi:10.1007/978-3-540-38918-7 · Cited by 171
Labbé, K., McIntire, C. R., Doiron, K., Leblanc, P. M., & Saleh, M. (2011) · Immunity · doi:10.1016/j.immuni.2011.10.016 · Cited by 170
Erener, S., Pétrilli, V., Kassner, I., Minotti, R., Castillo, R., Santoro, R., Hassa, P. O., Tschopp, J., & Hottiger, M. O. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.02.016 · Cited by 158
Frantz, S. (2003) · Journal of Molecular and Cellular Cardiology · doi:10.1016/s0022-2828(03)00113-5 · Cited by 154
Sarkar, A., Hall, M. W., Exline, M. C., Hart, J., Knatz, N. L., Gatson, N. T., & Wewers, M. D. (2006) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200604-546oc · Cited by 150
Role of IL-1 in renal ischemic reperfusion injury.
Haq, M., Norman, J., Saba, S. R., Ramírez, G., & Rabb, H. (1998) · Journal of the American Society of Nephrology · doi:10.1681/asn.v94614 · Cited by 149
Blocking interleukin-1β in acute and chronic autoinflammatory diseases
Dinarello, C. A. (2010) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2010.02313.x · Cited by 146
Malireddi, R. K. S., Ippagunta, S. K., Lamkanfi, M., & Kanneganti, T. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1001512 · Cited by 141
Luheshi, N., Kovács, K., López‐Castejón, G., Brough, D., & Dénes, Á. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-186 · Cited by 141
Self-citationMonack, D. M., Detweiler, C. S., & Falkow, S. (2001) · Cellular Microbiology · doi:10.1046/j.1462-5822.2001.00162.x · Cited by 137
Nguyen, M. D., Julien, J., & Rivest, S. (2001) · Annals of Neurology · doi:10.1002/ana.1256 · Cited by 132
Miggin, S. M., Pålsson‐McDermott, E. M., Dunne, A., Jefferies, C. A., Pinteaux, E., Banahan, K., Murphy, C., Moynagh, P. N., Yamamoto, M., Akira, S., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608100104 · Cited by 129
Ikegami, R., Hunter, P., & Yager, T. D. (1999) · Developmental Biology · doi:10.1006/dbio.1999.9243 · Cited by 113
A Role for Caspase-1 in Heart Failure
Merkle, S., Frantz, S., Schön, M. P., Bauersachs, J. K., Buitrago, M. A. B., Frost, R. J., Schmitteckert, E. M., Lohse, M. J., & Engelhardt, S. H. (2007) · Circulation Research · doi:10.1161/01.res.0000260203.55077.61 · Cited by 112
Masumoto, J., Zhou, W., Chen, F. F., Su, F., Kuwada, J. Y., Hidaka, E., Katsuyama, T., Sagara, J., Taniguchi, S., Ngo-Hazelett, P., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m203944200 · Cited by 108
Instrumental Activation of Bid by Caspase-1 in a Transgenic Mouse Model of ALS
Guégan, C. (2002) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2002.1136 · Cited by 104
Kono, H., Karmarkar, D., Iwakura, Y., & Rock, K. L. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902485 · Cited by 101
Caspase-1 Promiscuity Is Counterbalanced by Rapid Inactivation of Processed Enzyme
Walsh, J. G., Logue, S. E., Lüthi, A. U., & Martin, S. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225862 · Cited by 96
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Wang, W., Faubel, S. G., Ljubanović, D. G., Mitra, A., Falk, S. A., Kim, J., Tao, Y., Soloviev, A., Reznikov, L. L., Dinarello, C. A., et al. (2005) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00130.2004 · Cited by 96
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Rouquet, N., Pagès, J., Molina, T. J., Briand, P., & Joulin, V. (1996) · Current Biology · doi:10.1016/s0960-9822(02)70688-x · Cited by 95
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Kahns, S., Kalai, M., Jakobsen, L. D., Clark, B. F. C., Vandenabeele, P., & Jensen, P. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300495200 · Cited by 95
Angosto-Bazarra, D., López‐Castejón, G., López‐Muñoz, A., Sepulcre, M. P., Arizcún, M., Meseguer, J., & Mulero, V. (2012) · Innate Immunity · doi:10.1177/1753425912441956 · Cited by 90
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Weigert, A., Cremer, S., Schmidt, M. V., von Knethen, A., Angioni, C., Geißlinger, G., & Brüne, B. (2010) · Blood · doi:10.1182/blood-2009-10-243444 · Cited by 88
Multiple interleukin‐1β–converting enzymes contribute to inflammatory arthritis
Stehlik, C. (2009) · Arthritis & Rheumatism · doi:10.1002/art.24961 · Cited by 82
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Hoffman, H. M., & Brydges, S. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.135491 · Cited by 80
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Brough, D., Tyrrell, P. J., & Allan, S. M. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.06.002 · Cited by 78
Self-citationProapoptotic Effects of Caspase-1/Interleukin-Converting Enzyme Dominate in Myocardial Ischemia
Syed, F. M., Hahn, H. S., Odley, A. M., Guo, Y., Vallejo, J. G., Lynch, R. A., Mann, D. L., Bolli, R., & Dorn, G. W. (2005) · Circulation Research · doi:10.1161/01.res.0000166925.45995.ed · Cited by 77
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Benchoua, A., Braudeau, J., Reis, A., Couriaud, C., & Onténiente, B. (2004) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/01.wcb.0000140272.54583.fb · Cited by 76
Ray, A. M., OWEN, D. E., Evans, M. L., Davis, J. B., & Benham, C. D. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02230-7 · Cited by 69
López‐Castejón, G., Sepulcre, M. P., Mulero, I., Pelegrín, P., Meseguer, J., & Mulero, V. (2007) · Molecular Immunology · doi:10.1016/j.molimm.2007.05.015 · Cited by 69
ROSS, J., Brough, D., GIBSON, R., et al. (2007) · Neuropharmacology · doi:10.1016/j.neuropharm.2007.07.015 · Cited by 62
Self-citationMenzel, C. L., Sun, Q., Loughran, P., Pape, H., Billiar, T. R., & Scott, M. J. (2011) · Molecular Medicine · doi:10.2119/molmed.2011.00015 · Cited by 58
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Brodsky, I. E., & Medzhitov, R. M. (2011) · Current Biology · doi:10.1016/j.cub.2010.12.008 · Cited by 47
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Wheeler, R. D., Boutin, H., Touzani, O., Luheshi, G. N., Takeda, K., & Rothwell, N. J. (2003) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/01.wcb.0000059587.71206.ba · Cited by 47
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Johnson, A. L., Bridgham, J. T., Munks, M. W., & Witty, J. P. (1998) · Gene · doi:10.1016/s0378-1119(98)00373-4 · Cited by 36
Russo, R., Siviglia, E., Gliozzi, M., Amantea, D., M, P. A., Berliocchi, L., Bagetta, G., & Corasaniti, M. T. (2007) · International review of neurobiology · doi:10.1016/s0074-7742(07)82023-x · Cited by 22
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Metadata
- Authors
- Denes, A., Lopez-Castejon, G., & Brough, D.
- Venue
- Cell Death & Disease
- Published
- 2012-07-05
- Volume
- 3
- Issue
- 7
- Pages
- e338-e338
- ISSN
- 2041-4889 (ISSN-L)
- OpenAlex
- W2152174954
- Cited by
- 265
- References
- 113
- FWCI
- 7.43
- Type
- journal article
- Language
- en
- Open access
- gold
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.