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NLRs at the intersection of cell death and immunity
Abstract
Inflammation is a crucial element of the host response to cellular insult. Pathogen-induced inflammation includes a molecular pathway which proceeds through activation of the protease caspase-1 to the release of the inflammatory cytokines interleukin-1 (IL-1) and IL-18. Importantly, pathogens may also induce forms of cell death that have inherently pro-inflammatory features. Here, we review recent evidence demonstrating that NLR (nucleotide-binding domain, leucine-rich repeat containing) family proteins serve as a common component of both caspase-1-activated apoptotic pathways and caspase-independent necrotic pathways. Parallels are drawn between NLR protein function and the activity of structurally similar proteins involved in cell death: the apoptotic mediator APAF1 (apoptotic-protease-activating factor 1) and the plant disease resistance NBS-LRR (nucleotide-binding site leucine-rich repeats) proteins.
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“Polynucleotides and oligonucleotides derived from degrading DNA or RNA can act on TLR3, TLR7, TLR8, or TLR9 as well as on intracellular receptors including RIG1, MDA5, or LGP2, while ATP and its degradation products may activate or inhibit distinct classes of purinergic receptors 45,108,109.”
From Immunogenic and tolerogenic cell death (2009) · cites this paper as [108]
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Cites
Jones, J. D. G., & Dangl, J. L. (2006) · Nature · doi:10.1038/nature05286 · Cited by 13,177
Janeway, C. A., & Medzhitov, R. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.083001.084359 · Cited by 8,394
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
Gout-associated uric acid crystals activate the NALP3 inflammasome
Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., & Tschopp, J. (2006) · Nature · doi:10.1038/nature04516 · Cited by 5,326
Biologic basis for interleukin-1 in disease.
Dinarello, C. (1996) · Blood · doi:10.1182/blood.v87.6.2095.bloodjournal8762095 · Cited by 4,344
The Danger Model: A Renewed Sense of Self
Matzinger, P. (2002) · Science · doi:10.1126/science.1071059 · Cited by 4,205
Toll-like receptor control of the adaptive immune responses
Iwasaki, A., & Medzhitov, R. M. (2004) · Nature Immunology · doi:10.1038/ni1112 · Cited by 4,166
Yoneyama, M., Kikuchi, M., Natsukawa, T., Shinobu, N., Imaizumi, T., Miyagishi, M., Taira, K., Akira, S., & Fujita, T. (2004) · Nature Immunology · doi:10.1038/ni1087 · Cited by 4,022
Editorial Office (1997) · Obesity Surgery · doi:10.1381/096089297765555359 · Cited by 3,941
The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5
Hayashi, F., Smith, K. D., Ozinsky, A., Hawn, T. R., Yi, E. C., Goodlett, D. R., Eng, J. K., Akira, S., Underhill, D. M., & Aderem, A. A. (2001) · Nature · doi:10.1038/35074106 · Cited by 3,605
Seth, R. B., Sun, L., Ea, C.-K., & Chen, Z. J. (2005) · Cell · doi:10.1016/j.cell.2005.08.012 · Cited by 3,329
Apoptosis, oncosis, and necrosis. An overview of cell death.
Majno, G., & Joris, I. (1995) · PubMed · Cited by 3,328
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
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
IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
Kawai, T., Takahashi, K., Sato, S., Coban, C., Kumar, H., Kato, H., Ishii, K. J., Takeuchi, O., & Akira, S. (2005) · Nature Immunology · doi:10.1038/ni1243 · Cited by 2,562
High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal
Lotze, M. T., & Tracey, K. J. (2005) · Nature reviews. Immunology · doi:10.1038/nri1594 · Cited by 2,490
Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
Meylan, E., Curran, J., Hofmann, K., Moradpour, D., Binder, M., Bartenschlager, R., & Tschopp, J. (2005) · Nature · doi:10.1038/nature04193 · Cited by 2,401
Apoptosis, Pyroptosis, and Necrosis: Mechanistic Description of Dead and Dying Eukaryotic Cells
Fink, S. L., & Cookson, B. T. (2005) · Infection and Immunity · doi:10.1128/iai.73.4.1907-1916.2005 · Cited by 2,270
Nakai, K., & Horton, P. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01336-x · Cited by 2,181
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 1,864
VISA Is an Adapter Protein Required for Virus-Triggered IFN-β Signaling
Xu, L., Wang, Y., Han, K.-J., Li, L., Zhai, Z., & Shu, H. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.08.014 · Cited by 1,849
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
Host Recognition of Bacterial Muramyl Dipeptide Mediated through NOD2
Inohara, N., Ogura, Y., Fontalba, A., Gutierrez, O., Pons, F., Crespo, J., Fukase, K., Inamura, S., Kusumoto, S., Hashimoto, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200673200 · Cited by 1,694
Triggering the Interferon Antiviral Response Through an IKK-Related Pathway
Sharma, S., tenOever, B. R., Grandvaux, N., Zhou, G., Lin, R., & Hiscott, J. B. (2003) · Science · doi:10.1126/science.1081315 · Cited by 1,685
Molecular identification of a danger signal that alerts the immune system to dying cells
Shi, Y., Evans, J. E., & Rock, K. L. (2003) · Nature · doi:10.1038/nature01991 · Cited by 1,684
Hoffman, H. M., Mueller, J. L., Broide, D. H., Wanderer, A. A., & Kolodner, R. D. (2001) · Nature Genetics · doi:10.1038/ng756 · Cited by 1,679
Nod1 Detects a Unique Muropeptide from Gram-Negative Bacterial Peptidoglycan
Girardin, S. E., Boneca, I. G., Carneiro, L. A. M., Antignac, A., Jéhanno, M., Viala, J., Tedin, K., Taha, M., Labigne-Roussel, A., Zäthringer, U., et al. (2003) · Science · doi:10.1126/science.1084677 · Cited by 1,625
Park, J. S., Svetkauskaite, D., He, Q., Kim, J., Strassheim, D., Ishizaka, A., & Abraham, E. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306793200 · Cited by 1,582
Caspase structure, proteolytic substrates, and function during apoptotic cell death
Nicholson, D. (1999) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400598 · Cited by 1,562
Large-scale analysis of the human and mouse transcriptomes
Su, A. I., Cooke, M. P., Ching, K. A., Hakak, Y., Walker, J. R., Wiltshire, T., Orth, A. P., Vega, R. G., Sapinoso, L. M., Moqrich, A., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012025199 · Cited by 1,466
Death by design: apoptosis, necrosis and autophagy
Edinger, A. L., & Thompson, C. B. (2004) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.09.011 · Cited by 1,362
Nod1 responds to peptidoglycan delivered by the Helicobacter pylori cag pathogenicity island
Viala, J., Chaput, C., Boneca, I. G., Cardona, A., Girardin, S. E., Moran, A. P., Athman, R., Mémet, S., Huerre, M., Coyle, A. J., et al. (2004) · Nature Immunology · doi:10.1038/ni1131 · Cited by 1,221
Gitlin, L., Barchet, W., Gilfillan, S., Cella, M., Beutler, B., Flavell, R. A., Diamond, M., & Colonna, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603082103 · Cited by 1,177
Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3
Kanneganti, T., Özören, N., Body–Malapel, M., Amer, A. O., Park, J., Franchi, L., Whitfield, J. R., Barchet, W., Colonna, M., Vandenabeele, P., et al. (2006) · Nature · doi:10.1038/nature04517 · Cited by 1,149
Franchi, L., Amer, A., Body-Malapel, M., Kanneganti, T.-D., Özören, N., Jagirdar, R., Inohara, N., Vandenabeele, P., Bertin, J., Coyle, A., et al. (2006) · Nature Immunology · doi:10.1038/ni1346 · Cited by 1,131
Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf
Miao, E. A., Alpuche-Aranda, C. M., Dors, M., Clark, A. E., Bader, M. W., Miller, S. I., & Aderem, A. (2006) · Nature Immunology · doi:10.1038/ni1344 · Cited by 1,127
Fink, S. L., & Cookson, B. T. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00751.x · Cited by 1,114
The apoptosome: Signalling platform of cell death
Riedl, S. J., & Salvesen, G. S. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2153 · Cited by 1,097
Fernandes-Alnemri, T., Wu, J., Yu, J.-W., Datta, P., Miller, B., Jankowski, W., Rosenberg, S., Zhang, J., & Alnemri, E. S. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402194 · Cited by 1,026
Inhibition of Human Caspases by Peptide-based and Macromolecular Inhibitors
Garcia-Calvo, M. M., Peterson, E. P., Leiting, B., Ruel, R., Nicholson, D. W., & Thornberry, N. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32608 · Cited by 980
Sutterwala, F. S., Ogura, Y., Szczepanik, M., Lara-Tejero, M., Lichtenberger, G. S., Grant, E. P., Bertin, J., Coyle, A. J., Galán, J. E., Askenase, P. W., et al. (2006) · Immunity · doi:10.1016/j.immuni.2006.02.004 · Cited by 980
Martinon, F., & Tschopp, J. (2004) · Cell · doi:10.1016/j.cell.2004.05.004 · Cited by 957
Necrotic death as a cell fatePreprint
Zong, W., & Thompson, C. B. (2006) · Genes & Development · doi:10.1101/gad.1376506 · Cited by 952
Programmed cell death, mitochondria and the plant hypersensitive response
LAM, E. H., Kato, N., & Lawton, M. (2001) · Nature · doi:10.1038/35081184 · Cited by 916
Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
Boyden, E. D., & Dietrich, W. F. (2006) · Nature Genetics · doi:10.1038/ng1724 · Cited by 882
Inflammasome adaptors and sensors: intracellular regulators of infection and inflammation
Mariathasan, S., & Monack, D. M. (2006) · Nature reviews. Immunology · doi:10.1038/nri1997 · Cited by 879
Chen, C.-J., Kono, H., Golenbock, D., Reed, G., Akira, S., & Rock, K. L. (2007) · Nature Medicine · doi:10.1038/nm1603 · Cited by 876
The machinery of programmed cell death
Zimmermann, K. C., Bonzon, C., & Green, D. R. (2001) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(01)00159-0 · Cited by 829
Aksentijevich, I. A., Nowak, M., Mallah, M., Chae, J. J., Watford, W. T., Hofmann, S. R., Stein, L. D., Russo, R. A. G., Goldsmith, D. P., Dent, P. B., et al. (2002) · Arthritis & Rheumatism · doi:10.1002/art.10688 · Cited by 746
Plant NBS-LRR proteins in pathogen sensing and host defense
DeYoung, B. J., & Innes, R. W. (2006) · Nature Immunology · doi:10.1038/ni1410 · Cited by 738
Feldmann, J., Prieur, A., Quartier, P., Berquin, P. C., Dogniaux, S., Cortis, E., Hamel‐Teillac, D., Fischer, A., & Basile, G. D. S. (2002) · The American Journal of Human Genetics · doi:10.1086/341357 · Cited by 737
Conjugative Transfer by the Virulence System of Legionella pneumophila
Vogel, J. P., Andrews, H. L., Wong, S. K., & Isberg, R. R. (1998) · Science · doi:10.1126/science.279.5352.873 · Cited by 721
Reconstituted NALP1 Inflammasome Reveals Two-Step Mechanism of Caspase-1 Activation
Faustin, B., Lartigue, L., Bruey, J., Luciano, F., Sergienko, E. A., Bailly‐Maitre, B., Volkmann, N., Hanein, D., Rouiller, I., & Reed, J. C. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.032 · Cited by 709
Kanneganti, T., Body–Malapel, M., Amer, A. O., Park, J., Whitfield, J. R., Franchi, L., Taraporewala, Z. F., Miller, D. J., Patton, J. T., Inohara, N., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607594200 · Cited by 706
Salmonella induces macrophage death by caspase‐1‐dependent necrosis
Brennan, M. A., & Cookson, B. T. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02103.x · Cited by 685
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
Evasion of Toll-like receptor 5 by flagellated bacteria
Andersen‐Nissen, E., Smith, K. D., Strobe, K. L., Barrett, S. L. R., Cookson, B. T., Logan, S. M., & Aderem, A. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502040102 · Cited by 657
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
Berger, K. H., & Isberg, R. R. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01092.x · Cited by 646
Hawn, T. R., Verbon, A., Lettinga, K. D., Zhao, L. P., Li, S. S., Laws, R. J., Skerrett, S. J., Beutler, B., Schroeder, L. A., Nachman, A., et al. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20031220 · Cited by 608
The Specific and Essential Role of MAVS in Antiviral Innate Immune Responses
Sun, Q., Sun, L., Liu, H.-H., Chen, X., Seth, R. B., Forman, J., & Chen, Z. J. (2006) · Immunity · doi:10.1016/j.immuni.2006.04.004 · Cited by 604
NLRX1 is a regulator of mitochondrial antiviral immunity
Moore, C. B., Bergstralh, D. T., Duncan, J. A., Lei, Y. L., Morrison, T. E., Zimmermann, A. G., Accavitti-Loper, M. A., Madden, V. J., Sun, L., Ye, Z., et al. (2008) · Nature · doi:10.1038/nature06501 · Cited by 599
Self-citationThe PYRIN-CARD Protein ASC Is an Activating Adaptor for Caspase-1
Srinivasula, S. M., Poyet, J.-L., Razmara, M., Datta, P., Zhang, Z., & Alnemri, E. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200179200 · Cited by 573
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
Suzuki, T., Franchi, L., Toma, C., Ashida, H., Ogawa, M., Yoshikawa, Y., Mimuro, H., Inohara, N., Sasakawa, C., & Núñez, G. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030111 · Cited by 543
Kanneganti, T., Lamkanfi, M., Kim, Y., Chen, G., Park, J., Franchi, L., Vandenabeele, P., & Núñez, G. (2007) · Immunity · doi:10.1016/j.immuni.2007.03.008 · Cited by 537
Flagellin-Deficient Legionella Mutants Evade Caspase-1- and Naip5-Mediated Macrophage Immunity
Ren, T., Zamboni, D. S., Roy, C. R., Dietrich, W. F., & Vance, R. E. (2006) · PLoS Pathogens · doi:10.1371/journal.ppat.0020018 · Cited by 535
Plant disease resistance protein signaling: NBS–LRR proteins and their partners
Belkhadir, Y., Subramaniam, R., & Dangl, J. L. (2004) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2004.05.009 · Cited by 535
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
Duncan, J. A., Bergstralh, D. T., Wang, Y., Willingham, S. B., Ye, Z., Zimmermann, A. G., & Ting, J. P.-Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611496104 · Cited by 503
Self-citationShoham, N. G., Centola, M. B., Mansfield, E. A., Hull, K. M., Wood, G., Wise, C. A., & Kastner, D. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2135380100 · Cited by 497
Cytosolic recognition of flagellin by mouse macrophages restricts Legionella pneumophila infection
Molofsky, A. B., Byrne, B. G., Whitfield, N. N., Madigan, C. A., Fuse, E. T., Tateda, K., & Swanson, M. S. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20051659 · Cited by 490
Cellular autophagy: surrender, avoidance and subversion by microorganisms
Kirkegaard, K., Taylor, M. P., & Jackson, W. T. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro865 · Cited by 444
Genomic Insights into the Immune System of the Sea Urchin
Rast, J. P., Smith, L. C., Loza‐Coll, M., Hibino, T., & Litman, G. W. (2006) · Science · doi:10.1126/science.1134301 · Cited by 440
Means, T. K., Hayashi, F., Smith, K. D., Aderem, A. A., & Luster, A. D. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.10.5165 · Cited by 416
Liu‐Bryan, R., Scott, P., Sydlaske, A., Rose, D. M., & Terkeltaub, R. (2005) · Arthritis & Rheumatism · doi:10.1002/art.21238 · Cited by 414
A bacterial invasin induces macrophage apoptosis by binding directly to ICE.
Chen, Y., Smith, M. R., Thirumalai, K., & Zychlinsky, A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00759.x · Cited by 413
Chae, J. J., Komarow, H. D., Cheng, J., Wood, G., Raben, N., Liu, P. P., & Kastner, D. L. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00056-x · Cited by 412
Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis
Mariathasan, S., Weiss, D. S., Dixit, V. M., & Monack, D. M. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050977 · Cited by 402
Bishop, D. K., & Hinrichs, D. J. (1987) · The Journal of Immunology · doi:10.4049/jimmunol.139.6.2005 · Cited by 384
Aganna, E., Martinon, F., Hawkins, P. N., Ross, J. B., Swan, D., Booth, D. R., Lachmann, H. J., Gaudet, R., Woo, P. M., Feighery, C., et al. (2002) · Arthritis & Rheumatism · doi:10.1002/art.10509 · Cited by 367
Expression of Legionella pneumophila Virulence Traits in Response to Growth Conditions
Byrne, B. G., & Swanson, M. S. (1998) · Infection and Immunity · doi:10.1128/iai.66.7.3029-3034.1998 · Cited by 364
Cryopyrin and pyrin activate caspase-1, but not NF-κB, via ASC oligomerization
Yu, J., Wu, J., Zhang, Z., Datta, P., Ibrahimi, I., Taniguchi, S., Sagara, J., Fernandes‐Alnemri, T., & Alnemri, E. S. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401734 · Cited by 350
Familial autoinflammatory diseases: genetics, pathogenesis and treatment
STOJANOV, S., & Kastner, D. L. (2005) · Current Opinion in Rheumatology · doi:10.1097/bor.0000174210.78449.6b · Cited by 348
CATERPILLERs, pyrin and hereditary immunological disorders
Ting, J. P. ‐., Kastner, D. L., & Hoffman, H. M. (2006) · Nature reviews. Immunology · doi:10.1038/nri1788 · Cited by 342
Self-citationDifferentiate to thrive: lessons from the Legionella pneumophila life cycle
Molofsky, A. B., & Swanson, M. S. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04129.x · Cited by 338
Bcl-2 and Bcl-XL Regulate Proinflammatory Caspase-1 Activation by Interaction with NALP1
Bruey, J., Bruey-Sédano, N., Luciano, F., Zhai, D., Balpai, R., Xu, C., Kress, C. L., Bailly‐Maitre, B., Li, X., Osterman, A. L., et al. (2007) · Cell · doi:10.1016/j.cell.2007.01.045 · Cited by 319
Willingham, S. B., Bergstralh, D. T., O'Connor, W., Morrison, A. C., Taxman, D. J., Duncan, J. A., Barnoy, S., Venkatesan, M. M., Flavell, R. A., Deshmukh, M., et al. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2007.07.009 · Cited by 299
Self-citationNagai, H., Cambronne, E. D., Kagan, J. C., Amor, J. C., Kahn, R., & Roy, C. R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406239101 · Cited by 284
Birc1e is the gene within the Lgn1 locus associated with resistance to Legionella pneumophila
Diez, E., Lee, S. H., Gauthier, S., Yaraghi, Z., Tremblay, M. L., Vidal, S. M., & Gros, P. (2002) · Nature Genetics · doi:10.1038/ng1065 · Cited by 282
Autophagy is an immediate macrophage response to Legionella pneumophila
Amer, A. O., & Swanson, M. S. (2005) · Cellular Microbiology · doi:10.1111/j.1462-5822.2005.00509.x · Cited by 279
Naip5 Affects Host Susceptibility to the Intracellular Pathogen Legionella pneumophila
Wright, E. K., Goodart, S. A., Growney, J. D., Hadinoto, V., Endrizzi, M. G., Long, E. M., Sadigh, K., Abney, A. L., Bernstein-Hanley, I., & Dietrich, W. F. (2003) · Current Biology · doi:10.1016/s0960-9822(02)01359-3 · Cited by 260
Co‐ordination of Legionella pneumophila virulence with entry into stationary phase by ppGpp
Hammer, B. K., & Swanson, M. S. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01519.x · Cited by 259
Jones, S., & Portnoy, D. A. (1994) · Infection and Immunity · doi:10.1128/iai.62.12.5608-5613.1994 · Cited by 249
The Apoptosome: Physiological, Developmental, and Pathological Modes of Regulation
Schafer, Z. T., & Kornbluth, S. A. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.04.008 · Cited by 247
Legionella pneumophila Replication Vacuoles Mature into Acidic, Endocytic Organelles
Sturgill-Koszycki, S., & Swanson, M. S. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.9.1261 · Cited by 243
Gründling, A., Burrack, L. S., Bouwer, H. G. A., & Higgins, D. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404924101 · Cited by 240
Hammer, B. K., Tateda, E. S., & Swanson, M. S. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02884.x · Cited by 240
Bardill, J. P., Miller, J. L., & Vogel, J. P. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04539.x · Cited by 223
Tateda, K., Moore, T. A., Deng, J. C., Newstead, M. W., Zeng, X., Matsukawa, A., Swanson, M. S., Yamaguchi, K., & Standiford, T. J. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.5.3355 · Cited by 214
Update on colchicine and its mechanism of action
Molad, Y. (2002) · Current Rheumatology Reports · doi:10.1007/s11926-002-0073-2 · Cited by 213
Molofsky, A. B., & Swanson, M. S. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03706.x · Cited by 207
Navarre, W. W., & Zychlinsky, A. (2000) · Cellular Microbiology · doi:10.1046/j.1462-5822.2000.00056.x · Cited by 196
Stack, J. H., Beaumont, K. C., Larsen, P. D., Straley, K. S., Henkel, G., Randle, J. C. R., & Hoffman, H. M. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.4.2630 · Cited by 191
Hentze, H., Lin, X. Y., Choi, M. S. K., & Porter, A. G. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401264 · Cited by 187
The Neuronal Apoptosis Inhibitory Protein Is a Direct Inhibitor of Caspases 3 and 7
Maier, J. K. X., Lahoua, Z., Gendron, N. H., Fetni, R., Johnston, A., Davoodi, J., Rasper, D., Roy, S., Slack, R. S., Nicholson, D. W., et al. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-06-02035.2002 · Cited by 185
Yamamoto, M., Yaginuma, K., Tsutsui, H., Sagara, J., Guan, X., Seki, E., Yasuda, K., Yamamoto, M., Akira, S., Nakanishi, K., et al. (2004) · Genes to Cells · doi:10.1111/j.1365-2443.2004.00789.x · Cited by 184
Type IVB Secretion by Intracellular Pathogens
Sexton, J. A., & Vogel, J. P. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.030303.x · Cited by 181
Heterotypic interactions among NACHT domains: implications for regulation of innate immune responses
Damiano, J. S., Oliveira, V. A., Welsh, K., & Reed, J. C. (2004) · Biochemical Journal · doi:10.1042/bj20031506 · Cited by 165
Saito, M. K., Nishikomori, R., Kambe, N., Fujisawa, A., Tanizaki, H., Takeichi, K., Imagawa, T., Iehara, T., Takada, H., Matsubayashi, T., et al. (2007) · Blood · doi:10.1182/blood-2007-06-094201 · Cited by 151
RIG-I family RNA helicases: Cytoplasmic sensor for antiviral innate immunity
Yoneyama, M., & Fujita, T. (2007) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2007.06.023 · Cited by 144
New insights into the mechanism of IL-1β maturation
Burns, K., Martinon, F., & Tschopp, J. (2003) · Current Opinion in Immunology · doi:10.1016/s0952-7915(02)00017-1 · Cited by 143
Perregaux, D. G., Barberia, J. T., Lanzetti, A. J., Geoghegan, K. F., Carty, T. J., & Gabel, C. A. (1992) · The Journal of Immunology · doi:10.4049/jimmunol.149.4.1294 · Cited by 135
Brieland, J. K., Freeman, P., Kunkel, R., Chrisp, C. E., Hurley, M. C., Fantone, J. C., & Engleberg, C. (1994) · PubMed Central · Cited by 134
Alli, O. A. T., Gao, L., Pedersen, L. L., Zink, S. D., Radulic, M., Dorić, M., & Kwaik, Y. A. (2000) · Infection and Immunity · doi:10.1128/iai.68.11.6431-6440.2000 · Cited by 130
Zink, S. D., Pedersen, L., Cianciotto, N. P., & Kwaik, Y. A. (2002) · Infection and Immunity · doi:10.1128/iai.70.3.1657-1663.2002 · Cited by 123
Activation of Caspase 3 duringLegionella pneumophila-Induced Apoptosis
Gao, L., & Kwaik, Y. A. (1999) · Infection and Immunity · doi:10.1128/iai.67.9.4886-4894.1999 · Cited by 111
Cervantes, J., Nagata, T., Uchijima, M., Shibata, K., & Koide, Y. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.01012.x · Cited by 109
Molofsky, A. B., Shetron‐Rama, L. M., & Swanson, M. S. (2005) · Infection and Immunity · doi:10.1128/iai.73.9.5720-5734.2005 · Cited by 107
Fujisawa, A., Kambe, N., Saito, M. K., Nishikomori, R., Tanizaki, H., Kanazawa, N., Adachi, S., Heike, T., Sagara, J., Suda, T., et al. (2006) · Blood · doi:10.1182/blood-2006-07-033597 · Cited by 102
Chapman, P. T., Yarwood, H., Harrison, A. A., Stocker, C. J., Jamar, F., Gundel, R. H., Peters, A. M., & Haskard, D. O. (1997) · Arthritis & Rheumatism · doi:10.1002/art.1780400525 · Cited by 99
McCall, S. H., Sahraei, M., Young, A. B., Worley, C. S., Duncan, J. A., Ting, J. P.-Y., & Marriott, I. (2007) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.071002 · Cited by 92
Self-citationMolmeret, M., Zink, S. D., Han, L., Abu-Zant, A., Asari, R., Bitar, D. M., & Kwaik, Y. A. (2003) · Cellular Microbiology · doi:10.1046/j.1462-5822.2003.00335.x · Cited by 91
Getting, S. J., Flower, R. J., Parente, L., de Médicis, R., Lussier, A., Woliztky, B. A., Martins, M. A., & Perretti, M. (1997) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)37005-3 · Cited by 90
Abu-Zant, A., Šantić, M., Molmeret, M., Jones, S. C., Helbig, J. H., & Kwaik, Y. A. (2005) · Infection and Immunity · doi:10.1128/iai.73.9.5339-5349.2005 · Cited by 88
Mandal, M., & Lee, K. (2002) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(02)00368-1 · Cited by 82
Neuronal Apoptosis-inhibitory Protein Does Not Interact with Smac and Requires ATP to Bind Caspase-9
Davoodi, J., Lin, L., Kelly, J., Liston, P., & MacKenzie, A. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405963200 · Cited by 81
Fernandez-Prada, C. M., Hoover, D. L., Tall, B. D., & Venkatesan, M. M. (1997) · Infection and Immunity · doi:10.1128/iai.65.4.1486-1496.1997 · Cited by 80
Derré, I., & Isberg, R. R. (2004) · Infection and Immunity · doi:10.1128/iai.72.11.6221-6229.2004 · Cited by 77
Legionnaires' disease. Pathological and historical aspects of a 'new' disease.
Blackmon, J. A., Hicklin, M. D., & Chandler, F. W. (1978) · PubMed · Cited by 76
The role of high mobility group box-1 protein in severe sepsis
Sundén‐Cullberg, J., Norrby‐Teglund, A., & Treutiger, C. J. (2006) · Current Opinion in Infectious Diseases · doi:10.1097/01.qco.0000224816.96986.67 · Cited by 70
Janssen, R., Verhard, E. M., Lankester, A. C., Cate, R. T., & van Dissel, J. T. (2004) · Arthritis & Rheumatism · doi:10.1002/art.20494 · Cited by 67
Zhao, X., Pike, B. R., Newcomb, J. K., Wang, K., Posmantur, R. M., & Hayes, R. L. (1999) · Neurochemical Research · doi:10.1023/a:1020933616351 · Cited by 60
Bergman, M. A., Cummings, L. A., Barrett, S. L. R., Smith, K. D., Lara, J. C., Aderem, A. A., & Cookson, B. T. (2005) · Infection and Immunity · doi:10.1128/iai.73.3.1350-1356.2005 · Cited by 60
Suzuki, T., Nakanishi, K., Tsutsui, H., Iwai, H., Akira, S., Inohara, N., Chamaillard, M., Núñez, G., & Sasakawa, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414671200 · Cited by 59
Suppression of metabolic accompaniments of phagocytosis by colchicine
Goldfinger, S. E., Howell, R. R., & Seegmiller, J. E. (1965) · Arthritis & Rheumatism · doi:10.1002/art.1780080610 · Cited by 57
Naip5/Birc1e and susceptibility to Legionella pneumophila
Fortier, A. H., Diez, E., & Gros, P. (2005) · Trends in Microbiology · doi:10.1016/j.tim.2005.05.007 · Cited by 55
Hägele, S., Hacker, J., & Brand, B. C. (1998) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1998.tb13298.x · Cited by 53
Koterski, J. F., Nahvi, M., Venkatesan, M. M., & Haimovich, B. (2005) · Infection and Immunity · doi:10.1128/iai.73.1.504-513.2005 · Cited by 52
ELISA kits based on monoclonal antibodies do not measure total IL-1β synthesis
Dinarello, C. A. (1992) · Journal of Immunological Methods · doi:10.1016/0022-1759(92)90179-w · Cited by 51
Meng, Z. H., Hudson, A. P., Schumacher, H. R., Baker, J. F., & Baker, D. G. (1997) · PubMed · Cited by 47
Maitotoxin Induces Biphasic Interleukin-1β Secretion and Membrane Blebbing in Murine Macrophages
Verhoef, P. A., Kertesy, S. B., Estación, M., Schilling, W. P., & Dubyak, G. (2004) · Molecular Pharmacology · doi:10.1124/mol.66.4.909 · Cited by 47
Damiano, J. S., Newman, R. M., & Reed, J. C. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.10.6338 · Cited by 45
Legionella pneumophila induces apoptosis via the mitochondrial death pathway
Neumeister, B., Faigle, M., Lauber, K., Northoff, H., & Wesselborg, S. (2002) · Microbiology · doi:10.1099/00221287-148-11-3639 · Cited by 44
Shen, D., Liang, X., Gawinowicz, M. A., & Gottesman, M. M. (2004) · PubMed · doi:10.1124/mol.66.4 · Cited by 31
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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
“It remains to be determined whether RIP1 is implicated in pyronecrosis, as well as whether pyroptosis and pyronecrosis play any role outside of the innate immune system.(84,85)”
Caspase Functions in Cell Death and DiseasePreprint
McIlwain, D. R., Berger, T., & Mak, T. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008656 · Cited by 2,702
“Activated caspase-1 in turn cleaves pro-IL-1b and pro-IL-18, which facilitates the secretion of these proinflammatory cytokines (Ting et al. 2008b).”
BackgroundInfluentialFatty acid–induced NLRP3-ASC inflammasome activation interferes with insulin signaling
Wen, H., Gris, D., Lei, Y., Jha, S., Zhang, L., Huang, M. T.-H., Brickey, W. J., & Ting, J. P.-Y. (2011) · Nature Immunology · doi:10.1038/ni.2022 · Cited by 1,698
“Several NLR molecules including NLRP3, along with the adaptor protein ASC (apoptotic speck protein containing a caspase recruitment domain; also called PYCARD) and procaspase-1, form molecular platforms called the inflammasome, which mediates the catalytic activation of caspase-1, followed by the cleavage and release…”
Self-citationImmunogenic and tolerogenic cell death
Green, D. R., Ferguson, T., Zitvogel, L., & Kroemer, G. (2009) · Nature Reviews Immunology · doi:10.1038/nri2545 · Cited by 1,176
How do plants achieve immunity? Defence without specialized immune cells
Spoel, S. H., & Dong, X. (2012) · Nature reviews. Immunology · doi:10.1038/nri3141 · Cited by 1,166
“However, unlike NLRs in animals, which are known to trigger cell apoptosis through the activity of caspases that activate pro-inflammatory cytokine”
Background
Metadata
- Authors
- Ting, J. P.-Y., Willingham, S. B., & Bergstralh, D. T.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Ting, Jenny P.-Y.
- ORCID
- Ting, Jenny P.-Y.
- Venue
- Nature Reviews Immunology
- Published
- 2008-05
- Volume
- 8
- Issue
- 5
- Pages
- 372-379
- ISSN
- 1474-1733 (ISSN-L)
- 1474-1741
- OpenAlex
- W2050870561
- Cited by
- 371
- References
- 145
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 7 · 2023: 8 · 2022: 10 · 2021: 14 · 2020: 10 · 2019: 19 · 2018: 18 · 2017: 18 · 2016: 17 · 2015: 19 · 2014: 22 · 2013: 27 · 2012: 36
- FWCI
- 3.40
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Immunology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- NLR proteins, cell death, pyroptosis, caspase-1, apoptosis, necrosis, inflammation, interleukin-1, IL-18, Apaf-1, NBS-LRR proteins, plant disease resistance, host-pathogen interaction
- MeSH terms
- NLR Proteins, Leucine-Rich Repeat Proteins, Animals, Communicable Diseases, Humans, Interleukin-1, Necrosis, Proteins, Tumor Necrosis Factor-alpha, Apoptosis, Caspase 1, HMGB1 Protein, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Apoptosis Regulatory Proteins, Apoptotic Protease-Activating Factor 1
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