Cited by 6,887

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Caspases: Enemies Within

Thornberry, Nancy A., Lazebnik, Yuri·1998·Science

Open this paper in CoChat — free account

Abstract

REVIEW Apoptosis, an evolutionarily conserved form of cell suicide, requires specialized machinery. The central component of this machinery is a proteolytic system involving a family of proteases called caspases. These enzymes participate in a cascade that is triggered in response to proapoptotic signals and culminates in cleavage of a set of proteins, resulting in disassembly of the cell. Understanding caspase regulation is intimately linked to the ability to rationally manipulate apoptosis for therapeutic gain.

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

Crossref · 10.1126/science.281.5381.1312

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

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.

Death Receptors: Signaling and Modulation
Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866

Show all 1 references

The hallmarks of cancer
Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219
Death Receptors: Signaling and Modulation
Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866
The biochemistry of apoptosis
Hengartner, M. O. (2000) · Nature · doi:10.1038/35037710 · Cited by 5,779
Cell Death
Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
The Bcl2 family: regulators of the cellular life-or-death switch
Cory, S., & Adams, J. M. (2002) · Nature Reviews Cancer · doi:10.1038/nrc883 · Cited by 4,032
Pathobiology of ischaemic stroke: an integrated view
Dirnagl, U., Iadecola, C., & Moskowitz, M. A. (1999) · Trends in Neurosciences · doi:10.1016/s0166-2236(99)01401-0 · Cited by 3,943
Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP Inhibition
Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000) · Cell · doi:10.1016/s0092-8674(00)00008-8 · Cited by 3,513
Mixed Lineage Kinase Domain-like Protein Mediates Necrosis Signaling Downstream of RIP3 Kinase
Sun, L., Wang, H., Wang, Z., He, S., Chen, S., Liao, D., Wang, L., Yan, J., Liu, W., Lei, X., et al. (2012) · Cell · doi:10.1016/j.cell.2011.11.031 · Cited by 2,698
Receptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-α
He, S., Wang, L., Miao, L., Wang, T., Du, F., Zhao, L., & Wang, X. (2009) · Cell · doi:10.1016/j.cell.2009.05.021 · Cited by 2,214
Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178
Programmed Cell Death in Animal Development and Disease
Fuchs, Y., & Steller, H. (2011) · Cell · doi:10.1016/j.cell.2011.10.033 · Cited by 1,915
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
Proapoptotic Bcl-2 Relative Bim Required for Certain Apoptotic Responses, Leukocyte Homeostasis, and to Preclude Autoimmunity
Bouillet, P., Metcalf, D., Huang, D. C. S., Tarlinton, D. M., Kay, T. W. H., Köntgen, F., Adams, J. M., & Strasser, A. (1999) · Science · doi:10.1126/science.286.5445.1735 · Cited by 1,504
Molecular Imaging
Weissleder, R., & Mahmood, U. (2001) · Radiology · doi:10.1148/radiology.219.2.r01ma19316 · Cited by 1,315
The effect of pain on cognitive function: A review of clinical and preclinical research
Moriarty, O., McGuire, B. E., & Finn, D. P. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.01.002 · Cited by 1,122
Programmed Anuclear Cell Death Delimits Platelet Life Span
Mason, K. D., Carpinelli, M. R., Fletcher, J. I., Collinge, J. E., Hilton, A. A., Ellis, S., Kelly, P. N., Ekert, P. G., Metcalf, D., Roberts, A. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.01.037 · Cited by 1,031
Apo2L/TRAIL-Dependent Recruitment of Endogenous FADD and Caspase-8 to Death Receptors 4 and 5
Kischkel, F. C., Lawrence, D. A., Chuntharapai, A., Schow, P., Kim, K. J., & Ashkenazi, A. (2000) · Immunity · doi:10.1016/s1074-7613(00)80212-5 · Cited by 975
Rules for Making Human Tumor Cells
Hahn, W. C., & Weinberg, R. A. (2002) · New England Journal of Medicine · doi:10.1056/nejmra021902 · Cited by 951
Prevention of osteocyte and osteoblast apoptosis by bisphosphonates and calcitonin
Plotkin, L. I., Weinstein, R. S., Parfitt, A. M., Roberson, P. K., Manolagas, S. C., & Bellido, T. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6800 · Cited by 890
Structural and biochemical basis of apoptotic activation by Smac/DIABLO
Chai, J., Du, C., Wu, J.-W., Kyin, S., Wang, X., & Shi, Y. (2000) · Nature · doi:10.1038/35022514 · Cited by 864
Apoptosis and interferons: role of interferon-stimulated genes as mediators of apoptosis
Chawla-Sarkar, M., Lindner, D. J., Liu, Y.-F., Williams, B. R., Sen, G. C., Silverman, R. H., & Borden, E. C. (2003) · Apoptosis · doi:10.1023/a:1023668705040 · Cited by 829
Caspases and their substrates
Julien, O., & Wells, J. A. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.44 · Cited by 816
A mechanistic role for cardiac myocyte apoptosis in heart failure
Wencker, D., Chandra, M., Nguyen, K., Miao, W., Garantziotis, S., Factor, S. M., Shirani, J., Armstrong, R. C., & Kitsis, R. N. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17664 · Cited by 765
Chemotherapy-Associated Oxidative Stress: Impact on Chemotherapeutic Effectiveness
Conklin, K. A. (2004) · Integrative Cancer Therapies · doi:10.1177/1534735404270335 · Cited by 752
Oxidative stress and apoptosis: Impact on cancer therapy
Ozben, T. (2007) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.20874 · Cited by 751
Wired for Reproduction: Organization and Development of Sexually Dimorphic Circuits in the Mammalian Forebrain
Simerly, R. B. (2002) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.25.112701.142745 · Cited by 723
Inhibition of JNK activation through NF-κB target genes
Tang, G., Minemoto, Y., Dibling, B., Purcell, N. H., Li, Z., Karin, M., & Lin, A. (2001) · Nature · doi:10.1038/35104568 · Cited by 721
The transcription factor NFIA controls the onset of gliogenesis in the developing spinal cord
Deneen, B., Ho, R., Lukaszewicz, A., Hochstim, C. J., Gronostajski, R. M., & Anderson, D. J. (2006) · Neuron · doi:10.1016/j.neuron.2006.11.019 · Cited by 514
On the role of Hsp27 in regulating apoptosis
Concannon, C. G., Gorman, A. M., & Samali, A. (2003) · Apoptosis · doi:10.1023/a:1021601103096 · Cited by 513
Cytochrome c Deficiency Causes Embryonic Lethality and Attenuates Stress-Induced Apoptosis
Li, K., Li, Y., Shelton, J. M., Richardson, J. A., Spencer, E., Chen, Z. J., Wang, X., & Williams, R. S. (2000) · Cell · doi:10.1016/s0092-8674(00)80849-1 · Cited by 509
Caspase-9 Can Be Activated without Proteolytic Processing
Stennicke, H. R., Deveraux, Q. L., Humke, E. W., Reed, J. C., Dixit, V. M., & Salvesen, G. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8359 · Cited by 497
The Long Form of FLIP Is an Activator of Caspase-8 at the Fas Death-inducing Signaling Complex
Micheau, O., Thome, M., Schneider, P., Holler, N., Tschopp, J., Nicholson, D. W., Briand, C., & Grütter, M. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206882200 · Cited by 482
Apoptosis is an innate defense function of macrophages against Mycobacterium tuberculosis
Behar, S. M., Martin, C. J., Booty, M. G., Nishimura, T., Zhao, X., Gan, H.-X., Divangahi, M., & Remold, H. G. (2011) · Mucosal Immunology · doi:10.1038/mi.2011.3 · Cited by 447
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
Self-citation
Distinct mechanisms underlie neurotoxin-mediated cell death in cultured dopaminergic neurons
Lotharius, J., Dugan, L. L., & O’Malley, K. L. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-04-01284.1999 · Cited by 403
Metformin induces unique biological and molecular responses in triple negative breast cancer cells
Liu, B., Fan, Z., Edgerton, S. M., Deng, X.-S., Alimova, I. N., Lind, S. E., & Thor, A. D. (2009) · Cell Cycle · doi:10.4161/cc.8.13.8814 · Cited by 392
Peroxiredoxin III, a Mitochondrion-specific Peroxidase, Regulates Apoptotic Signaling by Mitochondria
Chang, T.-S., Cho, C.-S., Park, S., Yu, S., Kang, S. W., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407707200 · Cited by 388
Inhibition of constitutively active Stat3 suppresses proliferation and induces apoptosis in glioblastoma multiforme cells
Rahaman, S. O., Harbor, P. C., Chernova, O., Barnett, G. H., Vogelbaum, M. A., & Haque, S. J. (2002) · Oncogene · doi:10.1038/sj.onc.1206047 · Cited by 377
Molecular control of bacterial death and lysis
Rice, K. C., & Bayles, K. W. (2008) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00030-07 · Cited by 362
Glucocorticoid-induced osteoporosis: an update
Mazziotti, G., Angeli, A., Bilezikian, J. P., Canalis, E., & Giustina, A. (2006) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2006.03.009 · Cited by 362
Neuroprotective effect of cannabidiol, a non‐psychoactive component from Cannabis sativa, on β‐amyloid‐induced toxicity in PC12 cells
Iuvone, T., Esposito, G., Esposito, R., Santamaria, R., Di Rosa, M., & Izzo, A. A. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2003.02327.x · Cited by 361
Bacterial programmed cell death: making sense of a paradox
Bayles, K. W. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3136 · Cited by 315
Uncoupling Protein-2 Overexpression Inhibits Mitochondrial Death Pathway in Cardiomyocytes
Teshima, Y., Akao, M., Jones, S. P., & Marbán, E. (2003) · Circulation Research · doi:10.1161/01.res.0000085581.60197.4d · Cited by 318
Oncogenic protein interfaces: small molecules, big challenges
Nero, T. L., Morton, C. J., Holien, J. K., Wielens, J., & Parker, M. W. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3690 · Cited by 312
Heme Oxygenase-1-derived Carbon Monoxide Requires the Activation of Transcription Factor NF-κB to Protect Endothelial Cells from Tumor Necrosis Factor-α-mediated Apoptosis
Brouard, S., Berberat, P. O., Tobiasch, E., Seldon, M. P., Bach, F. H., & Soares, M. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108317200 · Cited by 306
Carbon monoxide inhibition of apoptosis during ischemia-reperfusion lung injury is dependent on the p38 mitogen-activated protein kinase pathway and involves caspase 3
Zhang, X., Shan, P., Otterbein, L. E., Alam, J., Flavell, R. A., Davis, R. J., Choi, A. M. K., & Lee, P. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208419200 · Cited by 288
The lighter side of BDNF
Noble, E. E., Billington, C. J., Kotz, C. M., & Wang, C. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00776.2010 · Cited by 284
Nitric oxide in gastrointestinal epithelial cell carcinogenesis: linking inflammation to oncogenesis
Jaiswal, M., LaRusso, N. F., & Gores, G. J. (2001) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2001.281.3.g626 · Cited by 278
Oxidative Stress in COPD: Sources, Markers, and Potential Mechanisms
McGuinness, A., & Sapey, E. (2017) · Journal of Clinical Medicine · doi:10.3390/jcm6020021 · Cited by 243
“This has been linked to oxidation of an essential part of the caspase apoptosis pathway [86], caspase 3, which is inactivated in oxidative”
Background
Gene expression in early ischemic renal injury: clues towards pathogenesis, biomarker discovery, and novel therapeutics
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
Ultraviolet radiation-induced apoptosis in keratinocytes: On the role of cytosolic factors
Assefa, Z., Van Laethem, A., Garmyn, M., & Agostinis, P. (2005) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2005.04.001 · Cited by 212
Resveratrol: Anti-Obesity Mechanisms of Action
Aguirre, L., Fernández-Quintela, A., Arias, N., & Portillo, M. (2014) · Molecules · doi:10.3390/molecules191118632 · Cited by 205
Role of the anion nitrite in ischemia-reperfusion cytoprotection and therapeutics
DEZFULIAN, C., RAAT, N., SHIVA, S., & GLADWIN, M. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.05.001 · Cited by 198
Autophagy within the antigen donor cell facilitates efficient antigen cross-priming of virus-specific CD8+ T cells
Uhl, M., Kepp, O., Jusforgues-Saklani, H., Vicencio, J.-M., Kroemer, G., & Albert, M. L. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2009.8 · Cited by 196
IV. Determinants of nitric oxide protection and toxicity in liver
Li, J., & Billiar, T. R. (1999) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1999.276.5.g1069 · Cited by 195
Spatial Distribution of Bax and Bcl-2 in Osteocytes After Bone Fatigue: Complementary Roles in Bone Remodeling Regulation?
Verborgt, O., Tatton, N. A., Majeska, R. J., & Schaffler, M. B. (2002) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2002.17.5.907 · Cited by 192
Accelerated metabolism and exclusion of 4-hydroxynonenal through induction of RLIP76 and hGST5.8 is an early adaptive response of cells to heat and oxidative stress
Cheng, J.-Z., Sharma, R., Yang, Y., Singhal, S. S., Sharma, A., Saini, M. K., Singh, S. V., Zimniak, P., Awasthi, S., & Awasthi, Y. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106838200 · Cited by 185
Apoptosis or Senescence-like Growth Arrest: Influence of Cell-Cycle Position, P53, P21 and Bax in H2O2 Response of Normal Human FIbroblasts
CHEN, Q. M., LIU, J., & MERRETT, J. B. (2000) · Biochemical Journal · doi:10.1042/bj3470543 · Cited by 280
Apolipoprotein E4 Potentiates Amyloid β Peptide-induced Lysosomal Leakage and Apoptosis in Neuronal Cells
Ji, Z.-S., Miranda, R. D., Newhouse, Y. M., Weisgraber, K. H., Huang, Y., & Mahley, R. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112109200 · Cited by 177
Dependence receptors: a new paradigm in cell signaling and cancer therapy
Goldschneider, D., & Mehlen, P. (2010) · Oncogene · doi:10.1038/onc.2010.13 · Cited by 169
Cell Death and Survival Assays
Kabakov, A. E., & Gabai, V. L. (2018) · Methods in Molecular Biology · doi:10.1007/978-1-4939-7477-1_9 · Cited by 156
Prostaglandin E 2 induces fibroblast apoptosis by modulating multiple survival pathways
Huang, S. K., White, E. S., Wettlaufer, S. H., Grifka, H., Hogaboam, C. M., Thannickal, V. J., Horowitz, J. C., & Peters-Golden, M. (2009) · The FASEB Journal · doi:10.1096/fj.08-128801 · Cited by 147
Mitomycin C induces apoptosis and caspase-8 and -9 processing through a caspase-3 and Fas-independent pathway
Pirnia, F., Schneider, E., Betticher, D. C., & Borner, M. M. (2002) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401062 · Cited by 151
Structural and functional analysis of the interaction between the agonistic monoclonal antibody Apomab and the proapoptotic receptor DR5
Adams, C., Totpal, K., Lawrence, D., Marsters, S., Pitti, R., Yee, S., Ross, S., Deforge, L., Koeppen, H., Sagolla, M., et al. (2008) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402306 · Cited by 148
Gold from the sea: Marine compounds as inhibitors of the hallmarks of cancer
Schumacher, M., Kelkel, M., Dicato, M., & Diederich, M. (2011) · Biotechnology Advances · doi:10.1016/j.biotechadv.2011.02.002 · Cited by 138
Presenilin-1 P264L Knock-In Mutation: Differential Effects on Aβ Production, Amyloid Deposition, and Neuronal Vulnerability
Siman, R., Reaume, A. G., Savage, M. J., Trusko, S., Lin, Y.-G., Scott, R. W., & Flood, D. G. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-23-08717.2000 · Cited by 133
Nuclear Factor-κB-inducible Death Effector Domain-containing Protein Suppresses Tumor Necrosis Factor-mediated Apoptosis by Inhibiting Caspase-8 Activity
You, Z., Ouyang, H., Lopatin, D., Polver, P. J., & Wang, C.-Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102464200 · Cited by 127
Systemically Administered Brain-Targeted Nanoparticles Transport Peptides across the Blood—Brain Barrier and Provide Neuroprotection
Yemisci, M., Caban, S., Gursoy-Ozdemir, Y., Lule, S., Novoa-Carballal, R., Riguera, R., Fernandez-Megia, E., Andrieux, K., Couvreur, P., Capan, Y., et al. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2014.220 · Cited by 118
Regulation of Apoptosis in Myeloid Cells by Interferon Consensus Sequence–Binding Protein
Gabriele, L., Phung, J., Fukumoto, J., Segal, D., Wang, I.-M., Giannakakou, P., Giese, N. A., Ozato, K., & Morse, H. C. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.3.411 · Cited by 114
An Overview of Acute Stroke Therapy: Past, Present, and Future
Fisher, M., & Schaebitz, W. (2000) · Archives of Internal Medicine · doi:10.1001/archinte.160.21.3196 · Cited by 112
Caspase-9 is activated in a cytochrome c-independent manner early during TNFα-induced apoptosis in murine cells
McDonnell, M. A., Wang, D., Khan, S. M., Vander Heiden, M. G., & Kelekar, A. (2003) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401271 · Cited by 109
Delphinidin, an active compound of red wine, inhibits endothelial cell apoptosis via nitric oxide pathway and regulation of calcium homeostasis
Martin, S., Giannone, G., Andriantsitohaina, R., & Carmen Martinez, M. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705347 · Cited by 107
From proteases to proteomics
Neurath, H. (2001) · Protein Science · doi:10.1110/ps.40101 · Cited by 98
Upstream Signaling Pathways Leading to the Activation of Double-stranded RNA-dependent Serine/Threonine Protein Kinase in β-Amyloid Peptide Neurotoxicity
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
Asbestos causes apoptosis in alveolar epithelial cells: Role of iron-induced free radicals
Aljandali, A., Pollack, H., Yeldandi, A., LI, Y., Weitzman, S. A., & Kamp, D. W. (2001) · Journal of Laboratory and Clinical Medicine · doi:10.1067/mlc.2001.114826 · Cited by 92
Epidermal langerhans cell depletion after artificial ultraviolet B irradiation of human skin in vivo: Apoptosis versus migration
Kölgen, W., Both, H., van Weelden, H., Guikers, K. L. H., Bruijnzeel-Koomen, C. A. F. M., Knol, E. F., van Vloten, W. A., & de Gruijl, F. R. (2002) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2002.01742.x · Cited by 88
Apoptosis in myocardial infarction
Rodríguez, M., Lucchesi, B. R., & Schaper, J. (2002) · Annals of Medicine · doi:10.1080/078538902321012414 · Cited by 81
Tethering of Apoptotic Cells to Phagocytes through Binding of CD47 to Src Homology 2 Domain-Bearing Protein Tyrosine Phosphatase Substrate-1
Tada, K., Tanaka, M., Hanayama, R., Miwa, K., Shinohara, A., Iwamatsu, A., & Nagata, S. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.11.5718 · Cited by 70
Impact of Tau on Neurovascular Pathology in Alzheimer's Disease
Canepa, E., & Fossati, S. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.573324 · Cited by 67
The novel caspase-3 substrate Gap43 is involved in AMPA receptor endocytosis and long-term depression
Han, M.-H., Jiao, S., Jia, J.-M., Chen, Y., Chen, C. Y., Gucek, M., Markey, S. P., & Li, Z. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.030676 · Cited by 62
A Mapping Study of Caspase-3 Activation Following Acute Spinal Cord Contusion in Rats
McEwen, M. L., & Springer, J. E. (2005) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.4a6467.2005 · Cited by 48
Altered signal transduction pathways and induction of autophagy in human myotonic dystrophy type 1 myoblasts
Beffy, P., Del Carratore, R., Masini, M., Furling, D., Puymirat, J., Masiello, P., & Simili, M. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.08.010 · Cited by 42
Regulation of neutrophil apoptosis
Edwards, S. W., Moulding, D. A., Derouet, M., & Moots, R. J. (2003) · Chemical Immunology and Allergy · doi:10.1159/000071562 · Cited by 41
Anti-mitotic chemotherapeutics promote apoptosis through TL1A-activated death receptor 3 in cancer cells
Qi, C., Wang, X., Shen, Z., Chen, S., Yu, H., Williams, N., & Wang, G. (2018) · Cell Research · doi:10.1038/s41422-018-0018-6 · 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
Robust neuroinflammation and perivascular pathology in rTg-DI rats, a novel model of microvascular cerebral amyloid angiopathy
Zhu, X., Hatfield, J., Sullivan, J. K., Xu, F., & Van Nostrand, W. E. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01755-y · Cited by 33
Apoptosis in primary lymphoid organs with aging
Sainz, R. M., Mayo, J. C., Reiter, R. J., Tan, D. X., & Rodriguez, C. (2003) · Microscopy Research and Technique · doi:10.1002/jemt.10414 · Cited by 32
Cell death assays for neurodegenerative disease drug discovery
Linsley, J. W., Reisine, T., & Finkbeiner, S. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2019.1623784 · Cited by 32
Specific inhibition of caspase-8 and −9 in CHO cells enhances cell viability in batch and fed-batch cultures
Yun, C. Y., Liu, S., Lim, S. F., Wang, T., Chung, B. Y. F., Jiat Teo, J., Chuan, K. H., Soon, A. S. C., Goh, K. S., & Song, Z. (2007) · Metabolic Engineering · doi:10.1016/j.ymben.2007.06.001 · Cited by 30
Executing cell senescence
Narita, M., & Lowe, S. W. (2004) · Cell Cycle · doi:10.4161/cc.3.3.699 · Cited by 29
Absence of Caspase-3 Protects Pancreatic β-Cells from c-Myc-induced Apoptosis without Leading to Tumor Formation
Radziszewska, A., Schroer, S. A., Choi, D., Tajmir, P., Radulovich, N., Ho, J. C., Wang, L., Liadis, N., Hakem, R., Tsao, M.-S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806960200 · Cited by 22
In vivo analysis reveals different apoptotic pathways in pre‐ and postmigratory cerebellar granule cells of rabbit
Lossi, L., Gambino, G., Mioletti, S., & Merighi, A. (2004) · Journal of Neurobiology · doi:10.1002/neu.20032 · Cited by 18
Antioxidant dietary supplementation in mice exposed to proton radiation attenuates expression of programmed cell death-associated genes
Sanzari, J. K., Wambi, C., Lewis-Wambi, J. S., & Kennedy, A. R. (2011) · Radiation Research · doi:10.1667/rr2330.1 · Cited by 16
Expression of FADD and cFLIPL balances mitochondrial integrity and redox signaling to substantiate apoptotic cell death
Ranjan, K., & Pathak, C. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2813-z · Cited by 16
Long-term functional maintenance of primary hepatocytes in vitro using macroporous hydrogels engineered through liquid-liquid phase separation
Sun, Y., Yin, S., Cui, J., Wang, Z., Han, Y., Ma, D., Wang, S., Wu, J., Cao, Y., Jiang, C., et al. (2024) · Nano Research · doi:10.1007/s12274-023-5940-3 · Cited by 13
Caspase Inhibition Attenuates Contractile Dysfunction Following Cardioplegic Arrest and Rewarming in the Setting of Left Ventricular Failure
Yarbrough, W. M., Mukherjee, R., Squires, C. E., Reese, E. S., Leiser, J. S., Stroud, R. E., Sample, J. A., Hendrick, J. W., Mingoia, J. T., McLean, J. E., et al. (2004) · Journal of Cardiovascular Pharmacology · doi:10.1097/00005344-200412000-00004 · Cited by 4

Authors: Thornberry, N. A., & Lazebnik, Y.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1998-08-28
Volume: 281
Issue: 5381
Pages: 1312-1316
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.281.5381.1312
OpenAlex: W2061497413
Cited by: 6,887
References: 1
FWCI: 177.05
Type: journal article
Language: en
Open access: closed

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.

Caspases: Enemies Within

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources