The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Caspases: the executioners of apoptosis
Open accessAbstract
Apoptosis is a major form of cell death, characterized initially by a series of stereotypic morphological changes. In the nematode Caenorhabditis elegans, the gene ced-3 encodes a protein required for developmental cell death. Since the recognition that CED-3 has sequence identity with the mammalian cysteine protease interleukin-1β-converting enzyme (ICE), a family of at least 10 related cysteine proteases has been identified. These proteins are characterized by almost absolute specificity for aspartic acid in the P1 position. All the caspases (ICE-like proteases) contain a conserved QACXG (where X is R, Q or G) pentapeptide active-site motif. Caspases are synthesized as inactive proenzymes comprising an N-terminal peptide (prodomain) together with one large and one small subunit. The crystal structures of both caspase-1 and caspase-3 show that the active enzyme is a heterotetramer, containing two small and two large subunits. Activation of caspases during apoptosis results in the cleavage of critical cellular substrates, including poly(ADP-ribose) polymerase and lamins, so precipitating the dramatic morphological changes of apoptosis. Apoptosis induced by CD95 (Fas/APO-1) and tumour necrosis factor activates caspase-8 (MACH/FLICE/Mch5), which contains an N-terminus with FADD (Fas-associating protein with death domain)-like death effector domains, so providing a direct link between cell death receptors and the caspases. The importance of caspase prodomains in the regulation of apoptosis is further highlighted by the recognition of adapter molecules, such as RAIDD [receptor-interacting protein (RIP)-associated ICH-1/CED-3-homologous protein with a death domain]/CRADD (caspase and RIP adapter with death domain), which binds to the prodomain of caspase-2 and recruits it to the signalling complex. Cells undergoing apoptosis following triggering of death receptors execute the death programme by activating a hierarchy of caspases, with caspase-8 and possibly caspase-10 being at or near the apex of this apoptotic cascade.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Apoptosis in the Pathogenesis and Treatment of Disease
Thompson, C. B. (1995) · Science · doi:10.1126/science.7878464 · Cited by 6,524
Boldin, M. P., Varfolomeev, E. E., Pancer, Z., Mett, I. L., Camonis, J. H., & Wallach, D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.14.7795 · Cited by 993
Cited by
Apoptosis: A Review of Programmed Cell Death
Elmore, S. (2007) · Toxicologic Pathology · doi:10.1080/01926230701320337 · Cited by 13,853
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
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
The Inflammasomes: Guardians of the Body
Martinon, F., Mayor, A., & Tschopp, J. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132715 · Cited by 2,436
Mitochondria and neuronal survival
Nicholls, D. G., & Budd, S. L. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.1.315 · Cited by 1,243
Anoikis molecular pathways and its role in cancer progression
Paoli, P., Giannoni, E., & Chiarugi, P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.026 · Cited by 1,160
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003
Cell death modalities: classification and pathophysiological implications
Galluzzi, L., Maiuri, M. C., Vitale, I., Zischka, H., Castedo, M., Zitvogel, L., & Kroemer, G. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402148 · Cited by 832
TNF receptor subtype signalling: Differences and cellular consequences
MacEwan, D. J. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00262-5 · Cited by 610
Caspase signalling controls microglia activation and neurotoxicity
Burguillos, M. A., Deierborg, T., Kavanagh, E., Persson, A., Hajji, N., Garcia-Quintanilla, A., Cano, J., Brundin, P., Englund, E., Venero, J. L., et al. (2011) · Nature · doi:10.1038/nature09788 · Cited by 585
Bratton, S. B., Walker, G., Srinivasula, S. M., Sun, X., Butterworth, M., Alnemri, E. S., & Cohen, G. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.5.998 · Cited by 406
Self-citationActivation of the caspase-3 apoptotic cascade in traumatic spinal cord injury
Springer, J. E., Azbill, R. D., & Knapp, P. E. (1999) · Nature Medicine · doi:10.1038/11387 · Cited by 371
Cadet, J. L., Jayanthi, S., & Deng, X. (2003) · The FASEB Journal · doi:10.1096/fj.03-0073rev · Cited by 286
Li, D., Ueta, E., Kimura, T., Yamamoto, T., & Osaki, T. (2004) · Cancer Science · doi:10.1111/j.1349-7006.2004.tb03323.x · Cited by 255
Plataki, M., Koutsopoulos, A. V., Darivianaki, K., Delides, G., Siafakas, N. M., & Bouros, D. (2005) · Chest · doi:10.1378/chest.127.1.266 · Cited by 237
Devarajan, P., Mishra, J., Supavekin, S., Patterson, L. T., & Steven Potter, S. (2003) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2003.09.012 · Cited by 229
Tau Cleavage and Dephosphorylation in Cerebellar Granule Neurons Undergoing Apoptosis
Canu, N., Dus, L., Barbato, C., Ciotti, M. T., Brancolini, C., Rinaldi, A. M., Novak, M., Cattaneo, A., Bradbury, A., & Calissano, P. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-18-07061.1998 · Cited by 232
The BCL-2 family of proteins and mitochondrial outer membrane permeabilisation
Birkinshaw, R. W., & Czabotar, P. E. (2017) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2017.04.001 · Cited by 229
Early N-Terminal Changes and Caspase-6 Cleavage of Tau in Alzheimer's Disease
Horowitz, P. M., Patterson, K. R., Guillozet-Bongaarts, A. L., Reynolds, M. R., Carroll, C. A., Weintraub, S. T., Bennett, D. A., Cryns, V. L., Berry, R. W., & Binder, L. I. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1988-04.2004 · Cited by 215
Marissen, W. E., & Lloyd, R. E. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7565 · Cited by 198
CHEN, Q. M., LIU, J., & MERRETT, J. B. (2000) · Biochemical Journal · doi:10.1042/bj3470543 · Cited by 280
Senescent fibroblasts resist apoptosis by downregulating caspase-3.
Marcotte, R., Lacelle, C., & Wang, E. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.07.007 · Cited by 159
Cell-Cell Contacts Prevent Anoikis in Primary Human Colonic Epithelial Cells
Hofmann, C., Obermeier, F., Artinger, M., Hausmann, M., Falk, W., Schoelmerich, J., Rogler, G., & Grossmann, J. (2007) · Gastroenterology · doi:10.1053/j.gastro.2006.11.017 · Cited by 152
Ethanol-Induced Apoptosis in Mouse Liver
Zhou, Z., Sun, X., & Kang, Y. J. (2001) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)61699-9 · Cited by 129
Howard, A. (2003) · Toxicology and Applied Pharmacology · doi:10.1016/s0041-008x(03)00156-x · Cited by 112
ANNAND, R. R., DAHLEN, J. R., SPRECHER, C. A., DREU, P. D., FOSTER, D. C., MANKOVICH, J. A., TALANIAN, R. V., KISIEL, W., & GIEGEL, D. A. (1999) · Biochemical Journal · doi:10.1042/bj3420655 · Cited by 106
Apoptosis: molecular mechanisms and pathogenicity
Rastogi, R. P., R., & Sinha, R. P. (2010) · Technische Universität Dortmund · doi:10.17877/de290r-8930 · Cited by 106
Clementi, M. E., Pezzotti, M., Orsini, F., Sampaolese, B., Mezzogori, D., Grassi, C., Giardina, B., & Misiti, F. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.137 · Cited by 105
Suen, K.-C., Yu, M.-S., So, K.-F., Chang, R. C.-C., & Hugon, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306503200 · Cited by 95
TAS6417, A Novel EGFR Inhibitor Targeting Exon 20 Insertion Mutations
Hasako, S., Terasaka, M., Abe, N., Uno, T., Ohsawa, H., Hashimoto, A., Fujita, R., Tanaka, K., Okayama, T., Wadhwa, R., et al. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-1206 · Cited by 88
Dasari, V. R., Velpula, K. K., Kaur, K., Fassett, D., Klopfenstein, J. D., Dinh, D. H., Gujrati, M., & Rao, J. S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011813 · Cited by 87
RetractedThe X-linked inhibitor of apoptosis (XIAP) prevents cell death in axotomized CNS neurons in vivo
Kügler, S., Straten, G., Kreppel, F., Isenmann, S., Liston, P., & Bähr, M. (2000) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4400712 · Cited by 84
Properties of cell death models calibrated and compared using Bayesian approaches
Eydgahi, H., Chen, W. W., Muhlich, J. L., Vitkup, D., Tsitsiklis, J. N., & Sorger, P. K. (2013) · Molecular Systems Biology · doi:10.1038/msb.2012.69 · Cited by 84
Marrot, L., Belaïdi, J. P., Jones, C., Perez, P., Meunier, J. R., Riou, L., & Sarasin, A. (2003) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2003.12422.x · Cited by 70
Kim, J. Y., Lee, J.-S., Han, Y.-S., Lee, J. H., Bae, I., Yoon, Y. M., Kwon, S. M., & Lee, S. H. (2015) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2015.085 · Cited by 59
Kuo, C.-T., Hsu, M.-J., Chen, B.-C., Chen, C.-C., Teng, C.-M., Pan, S.-L., & Lin, C.-H. (2008) · Toxicology Letters · doi:10.1016/j.toxlet.2007.12.009 · Cited by 62
Moon, A. (2011) · Oncology Reports · doi:10.3892/or.2011.1551 · Cited by 57
Subbiah, V., Chawla, S. P., Conley, A. P., Wilky, B. A., Tolcher, A., Lakhani, N. J., Berz, D., Andrianov, V., Crago, W., Holcomb, M., et al. (2023) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-23-0974 · Cited by 51
Shi, G., Xie, Y., Guo, Y., & Dai, J. (2018) · Aquatic Toxicology · doi:10.1016/j.aquatox.2017.12.002 · Cited by 49
Influenza A virus‐induced caspase‐3 cleaves the histone deacetylase 6 in infected epithelial cells
Husain, M., & Harrod, K. S. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.07.005 · Cited by 42
Functional characteristics of photochemically treated platelets
Jansen, G. A. J., Van Vliet, H. H. D. M., Vermeij, H., Beckers, E. A. M., Leebeek, F. W. G., Sonneveld, P., & Van Rhenen, D. J. (2004) · Transfusion · doi:10.1111/j.1537-2995.2003.00588.x · Cited by 41
Involvement of caspase 3- and 8-like proteases in ceramide-induced apoptosis of cardiomyocytes
Wang, J., Zhen, L., Klug, M. G., Wood, D., Wu, X., & Mizrahi, J. (2000) · Journal of Cardiac Failure · doi:10.1054/jcaf.2000.9502 · Cited by 40
Caspase activation pathways induced by staurosporine and low potassium: Role of caspase‐2
Caballero‐Benítez, A., & Morán, J. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10493 · Cited by 40
MATSUU, M., SHICHIJO, K., OKAICHI, K., WEN, C. Y., FUKUDA, E., NAKASHIMA, M., NAKAYAMA, T., SHIRAHATA, S., TOKUMARU, S., & SEKINE, I. (2003) · Journal of Radiation Research · doi:10.1269/jrr.44.111 · Cited by 38
QUINN, C. M., KÅGEDAL, K., TERMAN, A., STROIKIN, U., BRUNK, U. T., JESSUP, W., & GARNER, B. (2004) · Biochemical Journal · doi:10.1042/bj20031352 · Cited by 36
Caspase 3 Deficiency Rescues Peripheral Nervous System Defect in Retinoblastoma Nullizygous Mice
Simpson, M. T. W., MacLaurin, J. G., Xu, D., Ferguson, K. L., Vanderluit, J. L., Davoli, M. A., Roy, S., Nicholson, D. W., Robertson, G. S., Park, D. S., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-18-07089.2001 · Cited by 35
Are dietary fish oil supplements appropriate for dyslipidemia management? A review of the evidence
Sherratt, S. C. R., Lero, M., & Mason, R. P. (2020) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000665 · Cited by 33
Trapani, L., Melli, L., Segatto, M., Trezza, V., Campolongo, P., Jozwiak, A., Swiezewska, E., Pucillo, L. P., Moreno, S., Fanelli, F., et al. (2011) · The FASEB Journal · doi:10.1096/fj.11-184218 · Cited by 25
Pereira, C. P. M., Francis-Oliveira, J., Singulani, M. P., Ferreira, A. F. F., & Britto, L. R. G. (2023) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2023.578019 · Cited by 22
The novel phospholipase C activator, m-3M3FBS, induces monocytic leukemia cell apoptosis
Lee, Y.-N., Lee, H.-Y., Kim, J.-S., Park, C., Choi, Y. H., Lee, T. G., Ryu, S. H., Kwak, J.-Y., & Bae, Y.-S. (2005) · Cancer Letters · doi:10.1016/j.canlet.2004.09.017 · Cited by 18
Blockage of the JAK/STAT3 signaling pathway in multiple myeloma by leelamine
Jung, Y. Y., Um, J.-Y., Nasif, O., Alharbi, S. A., Sethi, G., & Ahn, K. S. (2021) · Phytomedicine · doi:10.1016/j.phymed.2021.153574 · Cited by 19
Makav, M., & Eroğlu, H. A. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-020-11985-5 · Cited by 16
Apoptosis and Related Proteins during Parturition in Prostaglandin F Receptor-Deficient Mice
Mu, J., Kanzaki, T., Si, X., Tomimatsu, T., Fukuda, H., Fujii, E., Hosono, T., Murata, Y., Sugimoto, Y., & Ichikawa, A. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6698 · Cited by 8
Metadata
- Authors
- COHEN, G. M.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1997-08-15
- Volume
- 326
- Issue
- 1
- Pages
- 1-16
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1942214720
- Cited by
- 4,719
- References
- 2
- FWCI
- 82.91
- Type
- journal article
- Language
- en
- Open access
- bronze
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 ›
Are you an author, or do you see a problem with this page? Request a review
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.
