Effector functions of NLRs in the intestine: innate sensing, cell death, and disease
Abstract
Nucleotide-binding and oligomerization domain-like receptors (NLRs) are central regulators of pathogen recognition, the induction of innate immune effectors and inflammation with utmost importance in human diseases such as inflammatory bowel diseases. Most NLRs are key mediators of inflammasome complexes that activate caspase-1 and drive proteolytic processing of pro-inflammatory cytokines; however, a few tightly regulate inflammasome-independent activation of nuclear factor-κB and mitogen-activated protein kinase pathways. NLR signaling has evolved in intestinal epithelial cells to avoid overactive inflammatory responses toward the resident microbiota and to preserve epithelial barrier integrity and functions by maintaining homeostasis. In the present review, I examine new insights into the role of the NLRs in antimicrobial defenses. I pay particular attention to the emerging role of these receptors in engaging a complex cross talk between cell death and innate immunity pathways. Furthermore, I discuss the physiological functions of the NLRs in shaping the innate immune response within the intestine, maintaining homeostasis, inducing tissue repair following injury and promoting tumorigenesis.
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NLRs proteins are responsible for maintaining gut barrier integrity by sensing the presence of commensal microbiota and the regulation of intestinal inflammation.
“NLRs proteins are also responsible for maintaining gut barrier integrity by sensing the presence of commensal microbiota and the regulation of intestinal inflammation.172,173”
From Regulation of Intestinal Barrier Function by Microbial Metabolites (2021) · cites this paper as [173]
Cites
Single Lgr5 stem cells build crypt-villus structures in vitro without a mesenchymal niche
Sato, T., Vries, R. G., Snippert, H. J., van de Wetering, M., Barker, N., Stange, D. E., van Es, J. H., Abo, A., Kujala, P., Peters, P. J., et al. (2009) · Nature · doi:10.1038/nature07935 · Cited by 7,204 · see citing works
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066 · see citing works
A role for mitochondria in nlrp3 inflammasome activation
Zhou, R., Yazdi, A. S., Menu, P., & Tschopp, J. (2011) · Nature · doi:10.1038/nature09663 · Cited by 5,602 · see citing works
Schroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475 · see citing works
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 · see citing works
Induction of Intestinal Th17 Cells by Segmented Filamentous Bacteria
Ivanov, I. I., Atarashi, K., Manel, N., Brodie, E. L., Shima, T., Karaoz, U., Wei, D., Goldfarb, K. C., Santee, C. A., Lynch, S. V., et al. (2009) · Cell · doi:10.1016/j.cell.2009.09.033 · Cited by 4,554 · see citing works
Induction of Colonic Regulatory T Cells by Indigenous <i>Clostridium</i> Species
Atarashi, K., Tanoue, T., Shima, T., Imaoka, A., Kuwahara, T., Momose, Y., Cheng, G., Yamasaki, S., Saito, T., Ohba, Y., et al. (2011) · Science · doi:10.1126/science.1198469 · Cited by 3,752 · see citing works
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 · see citing works
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 · see citing works
Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049 · see citing works
An Immunomodulatory Molecule of Symbiotic Bacteria Directs Maturation of the Host Immune System
Mazmanian, S. K., Liu, C. H., Tzianabos, A. O., & Kasper, D. L. (2005) · Cell · doi:10.1016/j.cell.2005.05.007 · Cited by 2,910 · see citing works
Thioredoxin-interacting protein links oxidative stress to inflammasome activation
Zhou, R., Tardivel, A., Thorens, B., Choi, I., & Tschopp, J. (2010) · Nature Immunology · doi:10.1038/ni.1831 · Cited by 2,708 · see citing works
Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica
Dostert, C., Pétrilli, V., Van Bruggen, R., Steele, C., Mossman, B. T., & Tschopp, J. (2008) · Science · doi:10.1126/science.1156995 · Cited by 2,658 · see citing works
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 · see citing works
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 · see citing works
Nod2 Is a General Sensor of Peptidoglycan through Muramyl Dipeptide (MDP) Detection
Girardin, S. E., Boneca, I. G., Viala, J., Chamaillard, M., Labigne-Roussel, A., Thomas, G. D., Philpott, D. J., & Sansonetti, P. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200651200 · Cited by 2,397 · see citing works
Integrating cell-signalling pathways with NF-κB and IKK function
Perkins, N. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2083 · Cited by 2,350 · see citing works
A microbial symbiosis factor prevents intestinal inflammatory disease
Mazmanian, S. K., Round, J. L., & Kasper, D. L. (2008) · Nature · doi:10.1038/nature07008 · Cited by 2,340 · see citing works
NLRP6 Inflammasome Regulates Colonic Microbial Ecology and Risk for Colitis
Elinav, E., Strowig, T., Kau, A. L., Henao-Mejia, J., Thaiss, C. A., Booth, C. J., Peaper, D. R., Bertin, J., Eisenbarth, S. C., Gordon, J. I., et al. (2011) · Cell · doi:10.1016/j.cell.2011.04.022 · Cited by 2,024 · see citing works
Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1β production
Saitoh, T., Fujita, N., Jang, M. H., Uematsu, S., Yang, B., Satoh, T., Omori, H., Noda, T., Yamamoto, N., Komatsu, M., et al. (2008) · Nature · doi:10.1038/nature07383 · Cited by 2,020 · see citing works
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 1,822 · see citing works
Kaser, A., Zeissig, S., & Blumberg, R. S. (2010) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101225 · Cited by 1,806 · see citing works
Nod2-Dependent Regulation of Innate and Adaptive Immunity in the Intestinal Tract
Kobayashi, K. S., Chamaillard, M., Ogura, Y., Henegariu, O., Inohara, N., Núñez, G., & Flavell, R. A. (2005) · Science · doi:10.1126/science.1104911 · Cited by 1,776 · see citing works
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 · see citing works
Interactions between commensal intestinal bacteria and the immune system
Macpherson, A. J., & Harris, N. L. (2004) · Nature reviews. Immunology · doi:10.1038/nri1373 · Cited by 1,607 · see citing works
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 1,574 · see citing works
Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants
Eisenbarth, S. C., Colegio, O. R., O’Connor, W., Sutterwala, F. S., & Flavell, R. A. (2008) · Nature · doi:10.1038/nature06939 · Cited by 1,542 · see citing works
Lysosomal membrane permeabilization in cell death
Boya, P., & Kroemer, G. (2008) · Oncogene · doi:10.1038/onc.2008.310 · Cited by 1,425 · see citing works
Chamaillard, M., Hashimoto, M., Horie, Y., Masumoto, J., Qiu, S., Saab, L., Ogura, Y., Kawasaki, A., Fukase, K., Kusumoto, S., et al. (2003) · Nature Immunology · doi:10.1038/ni945 · Cited by 1,323 · see citing works
Travassos, L. H., Carneiro, L. A. M., Ramjeet, M., Hussey, S., Kim, Y.-G., Magalhães, J. G., Yuan, L., Soares, F., Chea, E., Le Bourhis, L., et al. (2010) · Nature Immunology · doi:10.1038/ni.1823 · Cited by 1,306 · see citing works
The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
Zhao, Y., Yang, J., Shi, J., Gong, Y., Lu, Q., Xu, H., Liu, L., & Shao, F. (2011) · Nature · doi:10.1038/nature10510 · Cited by 1,273 · see citing works
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 · see citing works
Recognition of peptidoglycan from the microbiota by Nod1 enhances systemic innate immunity
Clarke, T. B., Davis, K. M., Lysenko, E. S., Zhou, A. Y., Yu, Y., & Weiser, J. N. (2010) · Nature Medicine · doi:10.1038/nm.2087 · Cited by 1,154 · see citing works
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 · see citing works
Allen, I. C., Scull, M. A., Moore, C. B., Holl, E. K., McElvania-TeKippe, E., Taxman, D. J., Guthrie, E. H., Pickles, R. J., & Ting, J. P.-Y. (2009) · Immunity · doi:10.1016/j.immuni.2009.02.005 · Cited by 1,113 · see citing works
Lymphoid tissue genesis induced by commensals through NOD1 regulates intestinal homeostasis
Bouskra, D., Brézillon, C., Bérard, M., Werts, C., Varona, R., Boneca, I. G., & Eberl, G. (2008) · Nature · doi:10.1038/nature07450 · Cited by 1,107 · see citing works
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 · see citing works
Cooney, R. M., BAKER, J. T., Brain, O., Danis, B., Pichulik, T., Allan, P., Ferguson, D. J. P., Campbell, B. J., Jewell, D. P., & Simmons, A. (2009) · Nature Medicine · doi:10.1038/nm.2069 · Cited by 1,046 · see citing works
Zaki, M. H., Boyd, K. L., Vogel, P., Kastan, M. B., Lamkanfi, M., & Kanneganti, T.-D. (2010) · Immunity · doi:10.1016/j.immuni.2010.03.003 · Cited by 989 · see citing works
The NLR Gene Family: A Standard Nomenclature
Ting, J. P. ‐., Lovering, R. C., Alnemri, E. S., Bertin, J., Boss, J. M., Davis, B. K., Flavell, R. A., Girardin, S. E., Godzik, A., Harton, J. A., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.02.005 · Cited by 958 · see citing works
Martinon, F., & Tschopp, J. (2004) · Cell · doi:10.1016/j.cell.2004.05.004 · Cited by 940 · see citing works
The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response
Muruve, D. A., Pétrilli, V., Zaiss, A. K., White, L. R., Clark, S. A., Ross, P. J., Parks, R. J., & Tschopp, J. (2008) · Nature · doi:10.1038/nature06664 · Cited by 936 · see citing works
Syk kinase signalling couples to the Nlrp3 inflammasome for anti-fungal host defence
Groß, O., Poeck, H., Bscheider, M., Dostert, C., Hannesschläger, N., Endres, S., Hartmann, G., Tardivel, A., Schweighoffer, E., Tybulewicz, V. L. J., et al. (2009) · Nature · doi:10.1038/nature07965 · Cited by 922 · see citing works
Colitis induced in mice with dextran sulfate sodium (DSS) is mediated by the NLRP3 inflammasome
Bauer, C. A., Duewell, P., Mayer, C., Lehr, H. A., Fitzgerald, K. A., Dauer, M., Tschopp, J., Endres, S., Latz, E., & Schnurr, M. M. (2010) · Gut · doi:10.1136/gut.2009.197822 · Cited by 918 · see citing works
The Nalp3 inflammasome is essential for the development of silicosis
Cassel, S. L., Eisenbarth, S. C., Iyer, S. S., Sadler, J. J., Colegio, O. R., Tephly, L. A., Carter, A. B., Rothman, P. B., Flavell, R. A., & Sutterwala, F. S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803933105 · Cited by 907 · see citing works
Regulation of MHC Class II Expression by Interferon-γ Mediated by the Transactivator Gene CIITA
Steimle, V., Siegrist, C.-A., Mottet, A., Lisowska-Grospierre, B., & Mach, B. (1994) · Science · doi:10.1126/science.8016643 · Cited by 898 · see citing works
Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
Kofoed, E. M., & Vance, R. E. (2011) · Nature · doi:10.1038/nature10394 · Cited by 894 · see citing works
Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
Boyden, E. D., & Dietrich, W. F. (2006) · Nature Genetics · doi:10.1038/ng1724 · Cited by 860 · see citing works
Xu, J., & Gordon, J. I. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1734063100 · Cited by 856 · see citing works
Reversible Microbial Colonization of Germ-Free Mice Reveals the Dynamics of IgA Immune Responses
Hapfelmeier, S., Lawson, M. A. E., Slack, E., Kirundi, J. K., Stoel, M., Heikenwalder, M., Cahenzli, J., Velykoredko, Y., Balmer, M. L., Endt, K., et al. (2010) · Science · doi:10.1126/science.1188454 · Cited by 835 · see citing works
Allen, I. C., TeKippe, E. M., Woodford, R.-M. T., Uronis, J. M., Holl, E. K., Rogers, A. B., Herfarth, H. H., Jobin, C., & Ting, J. P.-Y. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20100050 · Cited by 826 · see citing works
Cruz, C. M., Rinna, A., Forman, H. J., Ventura, A. L. M., Persechini, P. M., & Ojcius, D. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608083200 · Cited by 786 · see citing works
Homeostasis and Inflammation in the Intestine
Garrett, W. S., Gordon, J. I., & Glimcher, L. H. (2010) · Cell · doi:10.1016/j.cell.2010.01.023 · Cited by 784 · see citing works
NOD-Like Receptors: Role in Innate Immunity and Inflammatory Disease
Chen, G., Shaw, M. H., Kim, Y., & Núñez, G. (2008) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092239 · Cited by 770 · see citing works
Thomas, P. G., Dash, P., Aldridge, J. R., Ellebedy, A. H., Reynolds, C., Funk, A. J., Martin, W. J., Lamkanfi, M., Webby, R. J., Boyd, K. L., et al. (2009) · Immunity · doi:10.1016/j.immuni.2009.02.006 · Cited by 749 · see citing works
Nod1, an Apaf-1-like Activator of Caspase-9 and Nuclear Factor-κB
Inohara, N., Koseki, T., del Peso, L., Hu, Y., Yee, C., Chen, S., Carrio, R., Merino, J., Liu, D., Ni, J., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.14560 · Cited by 742 · see citing works
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 · see citing works
The inflammasome: a danger sensing complex triggering innate immunity
Pétrilli, V., Dostert, C., Muruve, D. A., & Tschopp, J. (2007) · Current Opinion in Immunology · doi:10.1016/j.coi.2007.09.002 · Cited by 700 · see citing works
Inflammasome recognition of influenza virus is essential for adaptive immune responses
Ichinohe, T., Lee, H. K., Ogura, Y., Flavell, R. A., & Iwasaki, A. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20081667 · Cited by 682 · see citing works
War and peace at mucosal surfaces
Sansonetti, P. J. (2004) · Nature reviews. Immunology · doi:10.1038/nri1499 · Cited by 680 · see citing works
Influenza virus activates inflammasomes via its intracellular M2 ion channel
Ichinohe, T., Pang, I. K., & Iwasaki, A. (2010) · Nature Immunology · doi:10.1038/ni.1861 · Cited by 632 · see citing works
NALP1 in Vitiligo-Associated Multiple Autoimmune Disease
Jin, Y., Mailloux, C. M., Gowan, K., Riccardi, S. L., LaBerge, G. S., Bennett, D. C., Fain, P. R., & Spritz, R. A. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa061592 · Cited by 626 · see citing works
Bauernfeind, F., Bartok, E., Rieger, A., Franchi, L., Núñez, G., & Hornung, V. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100613 · Cited by 617 · see citing works
Greten, F. R., Arkan, M. C., Bollrath, J., Hsu, L.-C., Goode, J., Miething, C., Göktuna, S. I., Neuenhahn, M., Fierer, J., Paxian, S., et al. (2007) · Cell · doi:10.1016/j.cell.2007.07.009 · Cited by 616 · see citing works
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 586 · see citing works
Hise, A. G., Tomalka, J. A., Ganesan, S., Patel, K., Hall, B. A., Brown, G. D., & Fitzgerald, K. A. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.05.002 · Cited by 568 · see citing works
Nod2 is required for the regulation of commensal microbiota in the intestine
Petnicki-Ocwieja, T., Hrncir, T., Liu, Y.-J., Biswas, A., Hudcovic, T., Tlaskalova-Hogenova, H., & Kobayashi, K. S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907722106 · Cited by 564 · see citing works
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 · see citing works
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 532 · see citing works
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 526 · see citing works
Common variants in the NLRP3 region contribute to Crohn's disease susceptibility
Villani, A., Lemire, M., Fortin, G., Louis, E. J., Silverberg, M. S., Collette, C., Baba, N., Libioulle, C., Bélaïche, J., Bitton, A., et al. (2008) · Nature Genetics · doi:10.1038/ng.285 · Cited by 526 · see citing works
A critical role of RICK/RIP2 polyubiquitination in Nod‐induced NF‐κB activation
Hasegawa, M., Fujimoto, Y., Lucas, P. C., Nakano, H., Fukase, K., Núñez, G., & Inohara, N. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601962 · Cited by 520 · see citing works
Dupaul-Chicoine, J., Yeretssian, G., Doiron, K., Bergstrom, K. S. B., McIntire, C. R., LeBlanc, P. M., Meunier, C., Turbide, C., Gros, P., Beauchemin, N., et al. (2010) · Immunity · doi:10.1016/j.immuni.2010.02.012 · Cited by 517 · see citing works
Self-citationZamboni, 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 · see citing works
Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome
Sutterwala, F. S., Mijares, L. A., Li, L., Ogura, Y., Kazmierczak, B. I., & Flavell, R. A. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20071239 · Cited by 509 · see citing works
Toll‐like receptor 2‐dependent bacterial sensing does not occur via peptidoglycan recognition
Travassos, L. H., Girardin, S. E., Philpott, D. J., Blanot, D., Nahori, M., Werts, C., & Boneca, I. G. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400248 · Cited by 504 · see citing works
Diversification of T-helper-cell lineages: finding the family root of IL-17-producing cells
Dong, C. (2006) · Nature reviews. Immunology · doi:10.1038/nri1807 · Cited by 487 · see citing works
Lightfield, K. L., Persson, J., Brubaker, S. W., Witte, C. E., von Moltke, J., Dunipace, E. A., Henry, T., Sun, Y., Cado, D., Dietrich, W. F., et al. (2008) · Nature Immunology · doi:10.1038/ni.1646 · Cited by 487 · see citing works
Identification of Ipaf, a Human Caspase-1-activating Protein Related to Apaf-1
Poyet, J., Srinivasula, S. M., Tnani, M., Razmara, M., Fernandes‐Alnemri, T., & Alnemri, E. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100250200 · Cited by 456 · see citing works
Regulation of Legionella Phagosome Maturation and Infection through Flagellin and Host Ipaf
Amer, A., Franchi, L., Kanneganti, T.-D., Body-Malapel, M., Özören, N., Brady, G., Meshinchi, S., Jagirdar, R., Gewirtz, A., Akira, S., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604933200 · Cited by 453 · see citing works
Inflammation-induced tumorigenesis in the colon is regulated by caspase-1 and NLRC4
Hu, B., Elinav, E., Huber, S., Booth, C. J., Strowig, T., Jin, C., Eisenbarth, S. C., & Flavell, R. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016814108 · Cited by 452 · see citing works
NLRC5 Negatively Regulates the NF-κB and Type I Interferon Signaling Pathways
Cui, J., Zhu, L., Xia, X., Wang, H. Y., Legras, X. D., Hong, J. K., Ji, J., Shen, P., Zheng, S. S., Chen, Z. J., et al. (2010) · Cell · doi:10.1016/j.cell.2010.03.040 · Cited by 449 · see citing works
A functional role for NLRP6 in intestinal inflammation and tumorigenesis
Chen, G. Y., Liu, M., Wang, F., Bertin, J., & Núñez, G. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100412 · Cited by 436 · see citing works
NLRP3 inflammasome plays a key role in the regulation of intestinal homeostasis
Hirota, S. A., Ng, J., Lueng, A., Khajah, M. A., Parhar, K. K. S., Li, Y., Lam, V. L., Potentier, M. S., Ng, K., Bawa, M., et al. (2010) · Inflammatory Bowel Diseases · doi:10.1002/ibd.21478 · Cited by 434 · see citing works
Craven, R. R., Gao, X., Allen, I. C., Gris, D., Wardenburg, J. B., McElvania, E., Ting, J. P. ‐., & Duncan, J. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007446 · Cited by 433 · see citing works
Salcedo, R., Worschech, A., Cardone, M., Jones, Y., Gyulai, Z., Dai, R.-M., Wang, E., Ma, W., Haines, D., O'hUigin, C., et al. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20100199 · Cited by 429 · see citing works
Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms
Saleh, M., Vaillancourt, J. P., Graham, R. K., Huyck, M., Srinivasula, S. M., Alnemri, E. S., Steinberg, M. H., Nolan, V., Baldwin, C. T., Hotchkiss, R. S., et al. (2004) · Nature · doi:10.1038/nature02451 · Cited by 423 · see citing works
The adaptor protein CARD9 is required for innate immune responses to intracellular pathogens
Hsu, Y.-M. S., Zhang, Y., You, Y., Wang, D., Li, H., Duramad, O., Qin, F. X.-F., Dong, C., & Lin, X. (2006) · Nature Immunology · doi:10.1038/ni1426 · Cited by 420 · see citing works
Zaki, M. H., Vogel, P., Body-Malapel, M., Lamkanfi, M., & Kanneganti, T.-D. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1002046 · Cited by 411 · see citing works
The NOD-Like Receptor NLRP12 Attenuates Colon Inflammation and Tumorigenesis
Zaki, H., Vogel, P., Malireddi, R. K. S., Body–Malapel, M., Anand, P., Bertin, J., Green, D. R., Lamkanfi, M., & Kanneganti, T. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.10.022 · Cited by 410 · see citing works
Gastrointestinal microbiology enters the metagenomics era
Frank, D. N., & Pace, N. R. (2008) · Current Opinion in Gastroenterology · doi:10.1097/mog.0b013e3282f2b0e8 · Cited by 405 · see citing works
Innate immune mechanisms of colitis and colitis-associated colorectal cancer
Saleh, M., & Trinchieri, G. (2010) · Nature reviews. Immunology · doi:10.1038/nri2891 · Cited by 402 · see citing works
Hsu, L.-C., Ali, S. R., McGillivray, S. M., Tseng, P., Mariathasan, S., Humke, E. W., Eckmann, L., Powell, J. J., Nizet, V., Dixit, V. M., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802726105 · Cited by 388 · see citing works
Boneca, I. G., Dussurget, O., Cabanes, D., Nahori, M., Sousa, S., Lecuit, M., Psylinakis, E., Bouriotis, V., Hugot, J., Giovannini, M., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609672104 · Cited by 378 · see citing works
Abbott, D. W., Wilkins, A., Asara, J. M., & Cantley, L. C. (2004) · Current Biology · doi:10.1016/j.cub.2004.12.032 · Cited by 374 · see citing works
Wang, L., Manji, G. A., Grenier, J. M., Al-Garawi, A. A., Merriam, S., Lora, J. M., Geddes, B. J., Briskin, M., DiStefano, P. S., & Bertin, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203915200 · Cited by 371 · see citing works
Allen, I. C., Moore, C. B., Schneider, M., Lei, Y. L., Davis, B. K., Scull, M. A., Gris, D., Roney, K. E., Zimmermann, A. G., Bowzard, J. B., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.03.026 · Cited by 365 · see citing works
Normand, S., Delanoye, A., Bressenot, A., Huot, L., Grandjean, T., Peyrin‐Biroulet, L., Lemoine, Y., Hot, D., & Chamaillard, M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100981108 · Cited by 358 · see citing works
Fritz, J. H., Girardin, S. E., Fitting, C., Werts, C., Mengin‐Lecreulx, D., Caroff, M., Cavaillon, J., Philpott, D. J., & Adib‐Conquy, M. (2005) · European Journal of Immunology · doi:10.1002/eji.200526286 · Cited by 355 · see citing works
McNeela, E. A., Burke, Á., Neill, D. R., Baxter, C., Fernandes, V. E., Ferreira, D. M., Smeaton, S., El-Rachkidy, R. G., McLoughlin, R. M., Mori, A., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001191 · Cited by 354 · see citing works
Human caspase 12 has acquired deleterious mutations
Fischer, H., Koenig, U., Eckhart, L., & Tschachler, E. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00289-9 · Cited by 346 · see citing works
Teitelbaum, D. H., & Coran, A. G. (2006) · CRC Press eBooks · doi:10.1201/b13237-67 · Cited by 341 · see citing works
Bertrand, M. J. M., Doiron, K., Labbè, K., Korneluk, R. G., Barker, P. A., & Saleh, M. (2009) · Immunity · doi:10.1016/j.immuni.2009.04.011 · Cited by 338 · see citing works
Mechanisms of caspase-1 activation by P2X7 receptor-mediated K+ release
Kahlenberg, J. M., & Dubyak, G. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00494.2003 · Cited by 337 · see citing works
Opitz, B., Püschel, A., Schmeck, B., Hocke, A. C., Rosseau, S., Hammerschmidt, S., Schumann, R. R., Suttorp, N., & Hippenstiel, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403861200 · Cited by 327 · see citing works
Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice
Saleh, M., Mathison, J. C., Wolinski, M. K., Bensinger, S. J., Fitzgerald, P., Droin, N. M., Ulevitch, R. J., Green, D. R., & Nicholson, D. W. (2006) · Nature · doi:10.1038/nature04656 · Cited by 323 · see citing works
Shao, W., Yeretssian, G., Doiron, K., Hussain, S. N. A., & Saleh, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708182200 · Cited by 321 · see citing works
Self-citationTattoli, I., Carneiro, L. A. M., Jéhanno, M., Magalhaes, J. G., Shu, Y., Philpott, D. J., Arnoult, D., & Girardin, S. E. (2008) · EMBO Reports · doi:10.1038/sj.embor.7401161 · Cited by 321 · see citing works
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 · see citing works
McGovern, D. P. B., Hysi, P. G., Ahmad, T., van Heel, D. A., Moffatt, M. F., Carey, A. H., Cookson, W., & Jewell, D. P. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi135 · Cited by 318 · see citing works
Harton, J. A., Linhoff, M. W., Zhang, J., & Ting, J. P. ‐. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.8.4088 · Cited by 316 · see citing works
Nod2 is essential for temporal development of intestinal microbial communities
Rehman, A., Sina, C., Gavrilova, O., Häsler, R., Ott, S. J., Baines, J. F., Schreiber, S., & Rosenstiel, P. C. (2011) · Gut · doi:10.1136/gut.2010.216259 · Cited by 316 · see citing works
Grenier, J. M., Wang, L., Manji, G. A., Huang, W.-J., Al-Garawi, A. A., Kelly, R., Carlson, A., Merriam, S., Lora, J. M., Briskin, M., et al. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03416-6 · Cited by 296 · see citing works
Pseudomonas aeruginosa activates caspase 1 through Ipaf
Miao, E. A., Ernst, R. K., Dors, M., Mao, D. P., & Aderem, A. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712183105 · Cited by 296 · see citing works
Brodsky, I. E., Palm, N. W., Sadanand, S., Ryndak, M. B., Sutterwala, F. S., Flavell, R. A., Bliska, J. B., & Medzhitov, R. M. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.04.009 · Cited by 295 · see citing works
XIAP mediates NOD signaling via interaction with RIP2
Krieg, A. H., Correa, R. G., Garrison, J. B., Negrate, G. L., Welsh, K., Huang, Z., Knoefel, W. T., & Reed, J. C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907131106 · Cited by 287 · see citing works
Mini‐review: Specificity and expression of CIITA, the master regulator of MHC class II genes
LeibundGut‐Landmann, S., Waldburger, J., Krawczyk, M., Otten, L., Suter, T. B., Fontana, A., Acha‐Orbea, H., & Reith, W. (2004) · European Journal of Immunology · doi:10.1002/eji.200424964 · Cited by 277 · see citing works
NLRX1 Negatively Regulates TLR-Induced NF-κB Signaling by Targeting TRAF6 and IKK
Xia, X., Cui, J., Wang, H. Y., Zhu, L., Matsueda, S., Wang, Q., Yang, X., Hong, J. K., Songyang, Z., Chen, Z. J., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.02.022 · Cited by 276 · see citing works
Humke, E. W., Shriver, S. K., Starovasnik, M. A., Fairbrother, W. J., & Dixit, V. M. (2000) · Cell · doi:10.1016/s0092-8674(00)00108-2 · Cited by 270 · see citing works
Watanabe, T., Asano, N., Fichtner‐Feigl, S., Gorelick, P. L., Tsuji, Y., Matsumoto, Y. M., Chiba, T., Fuss, I. J., Kitani, A., & Strober, W. (2010) · Journal of Clinical Investigation · doi:10.1172/jci39481 · Cited by 265 · see citing works
The innate immune receptor Nod1 protects the intestine from inflammation-induced tumorigenesis
Chen, G. Y., Shaw, M. H., Redondo, G., & Núñez, G. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-2061 · Cited by 261 · see citing works
Critical role for Ipaf in Pseudomonas aeruginosa‐induced caspase‐1 activation
Franchi, L., Stoolman, J. S., Kanneganti, T., Verma, A., Ramphal, R., & Núñez, G. (2007) · European Journal of Immunology · doi:10.1002/eji.200737532 · Cited by 259 · see citing works
T cells dampen innate immune responses through inhibition of NLRP1 and NLRP3 inflammasomes
Guarda, G., Dostert, C., Staehli, F., Cabalzar, K., Castillo, R., Tardivel, A., Schneider, P., & Tschopp, J. (2009) · Nature · doi:10.1038/nature08100 · Cited by 250 · see citing works
Kim, Y., Kamada, N., Shaw, M. H., Warner, N. E., Chen, G., Franchi, L., & Núñez, G. (2011) · Immunity · doi:10.1016/j.immuni.2011.04.013 · Cited by 242 · see citing works
NLRC5 Limits the Activation of Inflammatory Pathways
Benkő, S., Magalhaes, J. G., Philpott, D. J., & Girardin, S. E. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903900 · Cited by 235 · see citing works
Harder, J., Franchi, L., Muñoz-Planillo, R., Park, J., Reimer, T., & Núñez, G. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900444 · Cited by 235 · see citing works
Henson, P. M. (2005) · Nature Immunology · doi:10.1038/ni1205-1179 · Cited by 233 · see citing works
Regulation of apoptosis by the redox state of cytochrome c
Brown, G. C., & Borutaitė, V. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.024 · Cited by 228 · see citing works
Lysosomal destabilization in p53-induced apoptosis
Yuan, X., Li, W., Dalen, H., Lotem, J., Kama, R., Sachs, L., & Brunk, U. T. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092135599 · Cited by 226 · see citing works
Physiological Concentrations of K+ Inhibit Cytochrome c-dependent Formation of the Apoptosome
Cain, K., Langlais, C., Sun, X.-M., Brown, D. G., & Cohen, G. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107419200 · Cited by 197 · see citing works
Hasegawa, M., Yamazaki, T., Kamada, N., Tawaratsumida, K., Kim, Y., Núñez, G., & Inohara, N. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003761 · Cited by 187 · see citing works
Coordinated Regulation of Toll-Like Receptor and NOD2 Signaling by K63-Linked Polyubiquitin Chains
Abbott, D. W., Yang, Y., Hutti, J. E., Madhavarapu, S., Kelliher, M. A., & Cantley, L. C. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00270-07 · Cited by 183 · see citing works
Hasegawa, M., Yang, K., Hashimoto, M., Park, J., Kim, Y., Fujimoto, Y., Núñez, G., Fukase, K., & Inohara, N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602638200 · Cited by 175 · see citing works
Druilhe, A., Srinivasula, S. M., Razmara, M., Ahmad, M., & Alnemri, E. S. (2001) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400881 · Cited by 175 · see citing works
CARD-8 Protein, a New CARD Family Member That Regulates Caspase-1 Activation and Apoptosis
Razmara, M., Srinivasula, S. M., Wang, L., Poyet, J., Geddes, B. J., DiStefano, P. S., Bertin, J., & Alnemri, E. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107811200 · Cited by 173 · see citing works
Kumar, H., Kumagai, Y., Tsuchida, T., Koenig, P.-A., Satoh, T. K., Guo, Z., Jang, M. H., Saitoh, T., Akira, S., & Kawai, T. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0902477 · Cited by 172 · see citing works
Stehlik, C., Krajewska, M., Welsh, K., Krajewski, S., Godzik, A., & Reed, J. C. (2003) · Biochemical Journal · doi:10.1042/bj20030304 · Cited by 169 · see citing works
Apoptosis in the development of the immune system
Opferman, J. T. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402182 · Cited by 169 · see citing works
Nod1 Participates in the Innate Immune Response to Pseudomonas aeruginosa
Travassos, L. H., Carneiro, L. A. M., Girardin, S. E., Boneca, I. G., Lemos, R., Bozza, M. T., Domingues, R. M. C. P., Coyle, A. J., Bertin, J., Philpott, D. J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501649200 · Cited by 166 · see citing works
Spread of an Inactive Form of Caspase-12 in Humans Is Due to Recent Positive Selection
Xue, Y., Daly, A., Yngvadóttir, B., Liu, M., Coop, G., Kim, Y., Sabeti, P. C., Chen, Y., Stalker, J., Huckle, E. J., et al. (2006) · The American Journal of Human Genetics · doi:10.1086/503116 · Cited by 159 · see citing works
The microbial and danger signals that activate Nod-like receptors
Benkő, S., Philpott, D. J., & Girardin, S. E. (2008) · Cytokine · doi:10.1016/j.cyto.2008.07.013 · Cited by 153 · see citing works
Arthur, J. C., Lich, J. D., Ye, Z., Allen, I. C., Gris, D., Wilson, J. E., Schneider, M., Roney, K. E., O’Connor, B. P., Moore, C. B., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1002227 · Cited by 153 · see citing works
The NOD/RIP2 Pathway Is Essential for Host Defenses Against Chlamydophila pneumoniae Lung Infection
Shimada, K., Chen, S., Dempsey, P. W., Sorrentino, R., Alsabeh, R., Slepenkin, A. V., Peterson, E. M., Doherty, T. M., Underhill, D. M., Crother, T. R., et al. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000379 · Cited by 153 · see citing works
The PYRIN domain: A member of the death domain‐fold superfamily
Fairbrother, W. J., Gordon, N. C., Humke, E. W., O’Rourke, K. M., Starovasnik, M. A., Yin, J., & Dixit, V. M. (2001) · Protein Science · doi:10.1110/ps.13801 · Cited by 152 · see citing works
Bruey, J. M., Bruey-Sédano, N., Newman, R. M., Chandler, S., Stehlik, C., & Reed, J. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406741200 · Cited by 152 · see citing works
Green, D. R. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.05.004 · Cited by 138 · see citing works
Critical Role of NOD2 in Regulating the Immune Response to Staphylococcus aureus
Deshmukh, H. S., Hamburger, J. B., Ahn, S. H., McCafferty, D. G., Yang, S., & Fowler, V. G. (2009) · Infection and Immunity · doi:10.1128/iai.00940-08 · Cited by 130 · see citing works
COPs and POPs: modulators of inflammasome activity
Stehlik, C., & Dorfleutner, A. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.12.7993 · Cited by 130 · see citing works
Non-apoptotic role of BID in inflammation and innate immunity
Yeretssian, G., Correa, R. G., Doiron, K., Fitzgerald, P., Dillon, C. P., Green, D. R., Reed, J. C., & Saleh, M. (2011) · Nature · doi:10.1038/nature09982 · Cited by 122 · see citing works
Self-citationLeBlanc, P. M., Yeretssian, G., Rutherford, N., Doiron, K., Nadiri, A., Zhu, L., Green, D. R., Gruenheid, S., & Saleh, M. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.02.004 · Cited by 120 · see citing works
Self-citationRosenstiel, P. C., Huse, K., Till, A., Hampe, J., Hellmig, S., Sina, C., Billmann-Born, S., von Kampen, O., Waetzig, G. H., Platzer, M., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505423103 · Cited by 118 · see citing works
Intestinal Epithelial Stem Cells and Progenitors
Bjerknes, M., & Cheng, H. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)19014-x · Cited by 112 · see citing works
Pyrin-Only Protein 2 Modulates NF-κB and Disrupts ASC:CLR Interactions
Bedoya, F., Sandler, L., & Harton, J. A. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.6.3837 · Cited by 101 · see citing works
Frutuoso, M. S., Hori, J. I., Pereira, M. S. F., Lima-Junior, D. S., Sônego, F., Kobayashi, K. S., Flavell, R. A., Cunha, F. Q., & Zamboni, D. S. (2010) · Microbes and Infection · doi:10.1016/j.micinf.2010.05.006 · Cited by 97 · see citing works
Faustin, B., Chen, Y., Zhai, D., Negrate, G. L., Lartigue, L., Satterthwait, A. C., & Reed, J. C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809414106 · Cited by 86 · see citing works
A Shope Fibroma virus PYRIN-only protein modulates the host immune response
Dorfleutner, A., Talbott, S. J., Bryan, N. B., Funya, K. N., Rellick, S. L., Reed, J. C., Shi, X., Rojanasakul, Y., Flynn, D. C., & Stehlik, C. (2007) · Virus Genes · doi:10.1007/s11262-007-0141-9 · Cited by 85 · see citing works
Nickerson, K. M., Sisk, T. J., Inohara, N., Yee, C. S. K., Kennell, J. A., Cho, M.-C., Yannie, P. J., Núñez, G., & Chang, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101295200 · Cited by 79 · see citing works
NOD1 and NOD2 regulation of pulmonary innate immunity to Legionella pneumophila
Berrington, W. R., Iyer, R. F., Wells, R. D., Smith, K. D., Skerrett, S. J., & Hawn, T. R. (2010) · European Journal of Immunology · doi:10.1002/eji.201040518 · Cited by 78 · see citing works
Haverson, K., Šinkorová, Z., Šinkora, J., Šver, L., & Bailey, M. (2007) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2007.05.022 · Cited by 73 · see citing works
Yeretssian, G., Doiron, K., Shao, W., Leavitt, B. R., Hayden, M. R., Nicholson, D. W., & Saleh, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813362106 · Cited by 62 · see citing works
Self-citationMolecular regulation of inflammation and cell death
Yeretssian, G., Labbè, K., & Saleh, M. (2008) · Cytokine · doi:10.1016/j.cyto.2008.07.015 · Cited by 50 · see citing works
Self-citationLabbè, K., Miu, J., Yeretssian, G., Serghides, L., Tam, M., Finney, C. A. M., Erdman, L. K., Goulet, M.-L., Kain, K. C., Stevenson, M. M., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1002517 · Cited by 45 · see citing works
Self-citationFortier, A. H., Doiron, K., Saleh, M., Grinstein, S., & Gros, P. (2009) · Infection and Immunity · doi:10.1128/iai.01546-08 · Cited by 40 · see citing works
Lü, W. (2010) · World Journal of Gastroenterology · doi:10.3748/wjg.v16.i34.4348 · Cited by 32 · see citing works
Microbial control of regulatory and effector T cell responses in the gut
Hand, T. W., & Belkaid, Y. (2010) · Current Opinion in Immunology · doi:10.1016/j.coi.2010.01.008 · Cited by 30 · see citing works
Before They Were Gut Dendritic Cells
Rescigno, M. (2009) · Immunity · doi:10.1016/j.immuni.2009.08.015 · Cited by 28 · see citing works
Self-nonself discrimination, histoincompatibility, and the concept of immunology
Klein, J. P. (1999) · Immunogenetics · doi:10.1007/s002510050587 · Cited by 12 · see citing works
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Host-gut microbiota metabolic interactions
Nicholson, J. K., Holmes, E., Kinross, J., Burcelin, R., Gibson, G., Jia, W., & Pettersson, S. (2012) · Science · doi:10.1126/science.1223813 · Cited by 4,760 · see citing works
Regulation of Intestinal Barrier Function by Microbial Metabolites
Ghosh, S., Whitley, C. S., Haribabu, B., & Jala, V. R. (2021) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2021.02.007 · Cited by 835 · see citing works
The Role of Probiotics and Prebiotics in Inducing Gut Immunity
Vieira, A. T., Teixeira, M. M., & Martins, F. S. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00445 · Cited by 275 · see citing works
NOD-Like Receptors: Master Regulators of Inflammation and Cancer
Saxena, M., & Yeretssian, G. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00327 · Cited by 272 · see citing works
Self-citationIntestinal antimicrobial peptides during homeostasis, infection, and disease
Muniz, L. R., Knosp, C. A., & Yeretssian, G. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00310 · Cited by 252 · see citing works
Self-citationThe NLR family of innate immune and cell death sensors
Sundaram, B., Tweedell, R. E., Kumar, S. P., & Kanneganti, T. (2024) · Immunity · doi:10.1016/j.immuni.2024.03.012 · Cited by 213 · see citing works
The role of NOD-like receptors in innate immunity
Almeida-da-Silva, C. L. C., Savio, L. E. B., Coutinho‐Silva, R., & Ojcius, D. M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1122586 · Cited by 160 · see citing works
Zhu, H., Wang, H., Wang, S.-H., Tu, Z., Zhang, L., Wang, X., Hou, Y., Wang, C., Chen, J., & Liu, Y. (2018) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201700814 · Cited by 85 · see citing works
Cellular and molecular effects of yeast probiotics on cancer
Saber, A., Alipour, B., Faghfoori, Z., & Khosroushahi, A. Y. (2016) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2016.1179622 · Cited by 83 · see citing works
NOD-like receptors in intestinal homeostasis and epithelial tissue repair
Parlato, M., & Yeretssian, G. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15069594 · Cited by 79 · see citing works
Self-citationInflammasomes are important mediators of cyclophosphamide-induced bladder inflammation
Hughes, F. M., Vivar, N. P., Kennis, J. G., Pratt-Thomas, J. D., Lowe, D. W., Shaner, B. E., Nietert, P. J., Spruill, L., & Purves, J. T. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00297.2013 · Cited by 77 · see citing works
Aguilera, M., Darby, T. M., & Melgar, S. (2014) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2014.04.003 · Cited by 59 · see citing works
Hu, S., Du, X., Huang, Y., Fu, Y., Yang, Y., Zhan, X., He, W., Wen, Q., Zhou, X., Zhou, C., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007266 · Cited by 59 · see citing works
Shamekhi, S., Lotfi, H., Abdolalizadeh, J., Bonabi, E., & Zarghami, N. (2020) · Clinical & Translational Oncology · doi:10.1007/s12094-019-02270-0 · Cited by 44 · see citing works
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Oh, S., Choi, Y. K., & Lee, S. (2025) · Molecules and Cells · doi:10.1016/j.mocell.2025.100239 · Cited by 40 · see citing works
Nabergoj, S., Mlinarič‐Raščan, I., & Jakopin, Ž. (2018) · Medicinal Research Reviews · doi:10.1002/med.21557 · Cited by 38 · see citing works
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Hornef, M. W., & Fulde, M. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00474 · Cited by 22 · see citing works
Yi, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147580 · Cited by 21 · see citing works
Garg, S., Sharma, N., Bharmjeet, & Das, A. (2023) · Cancer Reports · doi:10.1002/cnr2.1892 · Cited by 19 · see citing works
Kern, M., Aschenbach, J. R., Tedin, K., Pieper, R., Loß, H., & Lodemann, U. (2017) · Immunological Investigations · doi:10.1080/08820139.2017.1360341 · Cited by 16 · see citing works
Choltus, H., Lavergne, M., Outeiro, C. D. S. D., Coste, K., Belville, C., Blanchon, L., & Sapin, V. (2021) · Biomedicines · doi:10.3390/biomedicines9091123 · Cited by 14 · see citing works
RETRACTED: Human Gut Microbiota: Dysbiosis and Manipulation
Shen, D., Liu, C., Xu, R., & Zhang, F. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00123 · Cited by 14 · see citing works
RetractedZouiten, L., Serghini, M., Fekih, M., Kallel, L., Matri, S., Mustapha, N. B., Boubaker, J., & Filali, A. (2013) · médecine/sciences · doi:10.1051/medsci/20132912019 · Cited by 13 · see citing works
Sai, J., Xiong, L., Zheng, J., Liu, C.-G., Lu, Y., Wang, G., Wang, Y., Wang, T., Guan, X., Chen, F., et al. (2016) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2016/2758140 · Cited by 13 · see citing works
Aabdin, Z. U., Bilal, M. S., Dai, H., Abaker, J. A., Liu, X., Sahito, B., Yan, J., & Shen, X. (2018) · Microbial Pathogenesis · doi:10.1016/j.micpath.2018.05.045 · Cited by 12 · see citing works
Multi-Step Regulation of Interferon Induction by Hepatitis C Virus
Oshiumi, H., Funami, K., Aly, H. H., Matsumoto, M., & Seya, T. (2013) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-012-0214-x · Cited by 11 · see citing works
Xu, S., Wei, S., Guo, Y., Cui, D.-L., & Yao, J.-F. (2018) · Pancreas · doi:10.1097/mpa.0000000000000977 · Cited by 11 · see citing works
Mitochondrial damage and clearance in retinal pigment epithelial cells
Gurubaran, I. S. (2024) · Acta Ophthalmologica · doi:10.1111/aos.16661 · Cited by 10 · see citing works
Wang, L., Chen, S., Cai, X. T., Zheng, Y., Zheng, C., & Yao, Y. (2026) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1720484 · Cited by 7 · see citing works
Calvello, R., Caponio, G. R., Cianciulli, A., Porro, C., Ruggiero, M., Celano, G., Angelis, M. D., & Panaro, M. A. (2025) · Antioxidants · doi:10.3390/antiox14030356 · Cited by 6 · see citing works
Toll-like receptors and NOD-like receptors at the implantation site
Liao, A., & Muyayalo, K. P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-818508-7.00001-4 · Cited by 2 · see citing works
Molecular signaling of inflammatory responses in macrophages
Yi, Y. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-822368-0.00005-0 · Cited by 1 · see citing works
Preventive Effects of Probiotics and Prebiotics in Food Allergy: Potentials and Promise
Shahali, Y., & Dadar, M. (2021) · Microorganisms for sustainability · doi:10.1007/978-981-16-0223-8_3 · Cited by 1 · see citing works
Halliez, M. C. M. (2014) · Libraries and Cultural Resources (University of Calgary) · doi:10.11575/prism/27133 · Cited by 1 · see citing works
Prenatal and neonatal probiotic intake in pediatric allergy
Shahali, Y., Mojgani, N., & Dadar, M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-823733-5.00029-5
Regulation of DNA Methylation Through EBP1 Interaction with NLRP2 and NLRP7
Son, N. H., So, M., & Lupfer, C. R. (2025) · DNA · doi:10.3390/dna5040049
Neuroimmune Regulation of NLRP3 Signalling in Parkinson’s Disease
Rymbai, E., & Roy, D. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06040-2
- Authors
- Yeretssian, G.
- Affiliations
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Yeretssian, Garabet
- ORCID
- Yeretssian, Garabet
- Venue
- Immunologic Research
- Published
- 2012-03-28
- Volume
- 54
- Issue
- 1-3
- Pages
- 25-36
- ISSN
- 0257-277X (ISSN-L)
- 1559-0755
- OpenAlex
- W2057359745
- Cited by
- 37
- References
- 168
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2023: 2 · 2022: 1 · 2021: 6 · 2020: 1 · 2018: 5 · 2017: 1 · 2016: 2 · 2014: 5 · 2013: 4 · 2012: 3
- FWCI
- 0.35
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Immunologic Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Leona M. and Harry B. Helmsley Charitable Trust
- 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 › Immunology and Microbiology › Immunology › IL-33, ST2, and ILC Pathways
- Keywords
- NLR, intestinal innate immunity, inflammasome, caspase-1, NF-κB signaling, MAPK signaling, intestinal epithelial barrier, gut microbiota, cell death, inflammatory bowel disease, tissue repair, intestinal tumorigenesis, antimicrobial defense
- MeSH terms
- Animals, Humans, Immunity, Innate, Intestines, Cell Death, Intracellular Signaling Peptides and Proteins, Inflammasomes
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