The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity
Open accessAbstract
Defects in death receptor-mediated apoptosis have been linked to cancer and autoimmune disease in humans. The in vivo role of caspase 8, a component of this pathway, has eluded analysis in postnatal tissues because of the lack of an appropriate animal model. Targeted disruption of caspase 8 is lethal in utero. We generated mice with a targeted caspase 8 mutation that is restricted to the T-cell lineage. Despite normal thymocyte development in the absence of caspase 8, we observed a marked decrease in the number of peripheral T-cells and impaired T-cell response ex vivo to activation stimuli.caspase 8 ablation protected thymocytes and activated T-cells from CD95 ligand but not anti-CD3-induced apoptosis, or apoptosis activated by agents that are known to act through the mitochondria.caspase 8 mutant mice were unable to mount an immune response to viral infection, indicating that caspase 8 deletion in T-cells leads to immunodeficiency. These findings identify an essential, cell-stage-specific role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity. This is consistent with the recent identification of caspase 8 mutations in human immunodeficiency.
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
NF-κB regulation in the immune system
Li, Q., & Verma, I. M. (2002) · Nature Reviews Immunology · doi:10.1038/nri910 · Cited by 4,007
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837
BH3-only Bcl-2 family member Bim is required for apoptosis of autoreactive thymocytes
Bouillet, P., Purton, J. F., Godfrey, D. I., Zhang, L.-C., Coultas, L., Puthalakath, H., Pellegrini, M., Cory, S., Adams, J. M., & Strasser, A. (2002) · Nature · doi:10.1038/415922a · Cited by 782
Cited by
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593
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
Necroptosis: The Release of Damage-Associated Molecular Patterns and Its Physiological Relevance
Kaczmarek, A., Vandenabeele, P., & Krysko, D. V. (2013) · Immunity · doi:10.1016/j.immuni.2013.02.003 · Cited by 1,411
Old, new and emerging functions of caspases
Shalini, S., Dorstyn, L., Dawar, S., & Kumar, S. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.216 · Cited by 1,267
Catalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosis
Oberst, A., Dillon, C. P., Weinlich, R., McCormick, L. L., Fitzgerald, P., Pop, C., Hakem, R., Salvesen, G. S., & Green, D. R. (2011) · Nature · doi:10.1038/nature09852 · Cited by 1,278
Self-citationCaspases in apoptosis and beyond
Li, J., & Yuan, J. (2008) · Oncogene · doi:10.1038/onc.2008.297 · Cited by 1,090
RIP3 mediates the embryonic lethality of caspase-8-deficient mice
Kaiser, W. J., Upton, J. W., Long, A. B., Livingston-Rosanoff, D., Daley-Bauer, L. P., Hakem, R., Caspary, T., & Mocarski, E. S. (2011) · Nature · doi:10.1038/nature09857 · Cited by 1,057
Self-citationNecroptosis in development, inflammation and disease
Weinlich, R., Oberst, A., Beere, H. M., & Green, D. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.149 · Cited by 1,016
The many roles of FAS receptor signaling in the immune system
Strasser, A., Jost, P. J., & Nagata, S. (2009) · Immunity · doi:10.1016/j.immuni.2009.01.001 · Cited by 968
Toll-like Receptor 3-mediated Necrosis via TRIF, RIP3, and MLKL
Kaiser, W. J., Sridharan, H., Huang, C., Mandal, P., Upton, J. W., Gough, P. J., Sehon, C. A., Marquis, R. W., Bertin, J., & Mocarski, E. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.462341 · Cited by 959
Activity of Protein Kinase RIPK3 Determines Whether Cells Die by Necroptosis or Apoptosis
Newton, K., Dugger, D. L., Wickliffe, K. E., Kapoor, N., de Almagro, M. C., Vucic, D., Komuves, L., Ferrando, R. E., French, D. M., Webster, J., et al. (2014) · Science · doi:10.1126/science.1249361 · Cited by 687
Survival Function of the FADD-CASPASE-8-cFLIPL Complex
Dillon, C. P., Oberst, A., Weinlich, R., Janke, L. J., Kang, T.-B., Ben-Moshe, T., Mak, T. W., Wallach, D., & Green, D. R. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.03.010 · Cited by 331
“Mice, treatments, and timed matings Mice with a deleted allele of caspase-8 were generated by germ line deletion of a caspase-8flox allele described previously (Salmena et al., 2003).”
MethodDietary modulation of the microbiome affects autoinflammatory disease
Lukens, J. R., Gurung, P., Vogel, P., Johnson, G. R., Carter, R. A., McGoldrick, D. J., Bandi, S. R., Calabrese, C. R., Walle, L. V., Lamkanfi, M., et al. (2014) · Nature · doi:10.1038/nature13788 · Cited by 314
A positive feedback loop between RIP3 and JNK controls non‐alcoholic steatohepatitis
Gautheron, J., Vucur, M., Reisinger, F., Cardenas, D. V., Roderburg, C., Koppe, C., Kreggenwinkel, K., Schneider, A. T., Bartneck, M., Neumann, U. P., et al. (2014) · EMBO Molecular Medicine · doi:10.15252/emmm.201403856 · Cited by 314
Hughes, M. A., Powley, I. R., Jukes-Jones, R., Horn, S., Feoktistova, M., Fairall, L., Schwabe, J. W. R., Leverkus, M., Cain, K., & MacFarlane, M. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.023 · Cited by 257
Alvarez-Diaz, S., Dillon, C. P., Lalaoui, N., Tanzer, M. C., Rodriguez, D. A., Lin, A., Lebois, M., Hakem, R., Josefsson, E. C., O’Reilly, L. A., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.07.016 · Cited by 242
Self-citationEssential Role for Caspase-8 in Toll-like Receptors and NFκB Signaling
Lemmers, B., Salmena, L., Bidère, N., Su, H., Matysiak-Zablocki, E., Murakami, K., Ohashi, P. S., Jurisicova, A., Lenardo, M., Hakem, R., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m606721200 · Cited by 181
Self-citationLee, E., Song, C.-H., Bae, S.-J., Ha, K.-T., & Karki, R. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01069-y · Cited by 164
Protective Roles for Caspase-8 and cFLIP in Adult Homeostasis
Weinlich, R., Oberst, A., Dillon, C. P., Janke, L. J., Milasta, S., Lukens, J. R., Rodriguez, D. A., Gurung, P., Savage, C., Kanneganti, T. D., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.045 · Cited by 157
RIPK1 Suppresses a TRAF2-Dependent Pathway to Liver Cancer
Schneider, A. T., Gautheron, J., Feoktistova, M., Roderburg, C., Loosen, S. H., Roy, S., Benz, F., Schemmer, P., Büchler, M. W., Nachbur, U., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2016.11.009 · Cited by 155
Aziz, M., Jacob, A., & Wang, P. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.488 · Cited by 125
Jones, R. G., Bui, T., White, C., Madesh, M., Krawczyk, C. M., Lindsten, T., Hawkins, B. J., Kubek, S., Frauwirth, K. A., Wang, Y. L., et al. (2007) · Immunity · doi:10.1016/j.immuni.2007.05.023 · Cited by 109
Essential role for Bclaf1 in lung development and immune system function
McPherson, J. P., Sarras, H., Lemmers, B., Tamblyn, L., Migon, E., Matysiak-Zablocki, E., Hakem, A., Azami, S. A., Cardoso, R., Fish, J., et al. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2008.167 · Cited by 86
Self-citationZhang, X., Fan, C., Zhang, H., Zhao, Q., Liu, Y., Xu, C., Xie, Q., Wu, X., Yu, X., Zhang, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.06.103 · Cited by 93
NF-κB and Extrinsic Cell Death Pathways – Entwined Do-or-Die Decisions for T cells
Blanchett, S., Boal-Carvalho, I., Layzell, S., & Seddon, B. (2021) · Trends in Immunology · doi:10.1016/j.it.2020.10.013 · Cited by 58
Koenig, A., Buskiewicz, I. A., Fortner, K. A., Russell, J. Q., Asaoka, T., He, Y.-W., Hakem, R., Eriksson, J. E., & Budd, R. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.506428 · Cited by 42
Self-citationSyk mediates BCR- and CD40-signaling integration during B cell activation
Ying, H., Li, Z., Yang, L., & Zhang, J. (2011) · Immunobiology · doi:10.1016/j.imbio.2010.09.016 · Cited by 40
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
Self-citationMartin, P., Palmer, G., Rodriguez, E., Palomo, J., Lemeille, S., Goldstein, J., & Gabay, C. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.1901074 · Cited by 19
Interactions of DNR1 with the apoptotic machinery of Drosophila melanogaster
Primrose, D. A., Chaudhry, S., Johnson, A. G. D., Hrdlicka, A., Schindler, A., Tran, D., & Foley, E. (2007) · Journal of Cell Science · doi:10.1242/jcs.03417 · Cited by 15
Metadata
- Authors
- Salmena, L., Lemmers, B., Hakem, A., Matysiak-Zablocki, E., Murakami, K., Au, P. Y. B., Berry, D. M., Tamblyn, L., Shehabeldin, A., Migon, E., Wakeham, A., Bouchard, D., Yeh, W. C., McGlade, J. C., Ohashi, P. S., & Hakem, R.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2003-03-21
- Volume
- 17
- Issue
- 7
- Pages
- 883-895
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2121842388
- Cited by
- 485
- References
- 3
- Type
- posted content
- Language
- en
- Open access
- diamond
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.
