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Toll-like Receptors and the Control of Immunity
Open accessAbstract
The study of innate immunity and its link to inflammation and host defense encompasses diverse areas of biology, ranging from genetics and biophysics to signal transduction and physiology. Central to our understanding of these events are the Toll-like receptors (TLRs), an evolutionarily ancient family of pattern recognition receptors. Herein, we describe the mechanisms and consequences of TLR-mediated signal transduction with a focus on themes identified in the TLR pathways that also explain the operation of other immune signaling pathways. These themes include the detection of conserved microbial structures to identify infectious agents and the use of supramolecular organizing centers (SMOCs) as signaling organelles that ensure digital cellular responses. Further themes include mechanisms of inducible gene expression, the coordination of gene regulation and metabolism, and the influence of these activities on adaptive immunity. Studies in these areas have informed the development of next-generation therapeutics, thus ensuring a bright future for research in this area.
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“TLR9 activation induces the assembly of a supramolecular organizing center called the myddosome, involving MyD88 and multiple members of the serine threonine kinase family IRAK [82,83].”
From Risk mitigation of immunogenicity: a key to personalized retinal gene therapy (2021) · cites this paper as [83]
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Cites
Defective LPS Signaling in C3H/HeJ and C57BL/10ScCr Mice: Mutations in Tlr4 Gene
Poltorak, A., He, X., Smirnova, I., Liu, M.-Y., Huffel, C. V., Du, X., Birdwell, D., Alejos, E., Silva, M., Galanos, C., et al. (1998) · Science · doi:10.1126/science.282.5396.2085 · Cited by 7,631
Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
Shi, J., Zhao, Y., Wang, K., Shi, X., Wang, Y., Huang, H., Zhuang, Y., Cai, T., Wang, F., & Shao, F. (2015) · Nature · doi:10.1038/nature15514 · Cited by 6,659
Origin and physiological roles of inflammation
Medzhitov, R. (2008) · Nature · doi:10.1038/nature07201 · Cited by 6,618
A Toll-like receptor recognizes bacterial DNA
Hemmi, H., Takeuchi, O., Kawai, T., Kaisho, T., Sato, S., Sanjo, H., Matsumoto, M., Hoshino, K., Wagner, H., Takeda, K., et al. (2000) · Nature · doi:10.1038/35047123 · Cited by 6,491
A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
Medzhitov, R., Preston-Hurlburt, P., & Janeway, C. A. J. (1997) · Nature · doi:10.1038/41131 · Cited by 6,137
Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3
Alexopoulou, L., Holt, A. C., Medzhitov, R., & Flavell, R. A. (2001) · Nature · doi:10.1038/35099560 · Cited by 6,129
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
Cyclic GMP-AMP Synthase Is a Cytosolic DNA Sensor That Activates the Type I Interferon Pathway
Sun, L., Wu, J., Du, F., Chen, X., & Chen, Z. J. (2013) · Science · doi:10.1126/science.1232458 · Cited by 4,996
Mutations affecting segment number and polarity in Drosophila
Nüsslein‐Volhard, C., & Wieschaus, E. F. (1980) · Nature · doi:10.1038/287795a0 · Cited by 4,370
Lemaître, B., Nicolas, E., Michaut, L., Reichhart, J., & Hoffmann, J. A. (1996) · Cell · doi:10.1016/s0092-8674(00)80172-5 · Cited by 4,224
Genome Regulation by Long Noncoding RNAs
Rinn, J. L., & Chang, H. Y. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051410-092902 · Cited by 4,091
CD14, a Receptor for Complexes of Lipopolysaccharide (LPS) and LPS Binding Protein
Wright, S. D., Ramos, R., Tobias, P. S., Ulevitch, R. J., & Mathison, J. C. (1990) · Science · doi:10.1126/science.1698311 · Cited by 3,996
Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8
Heil, F., Hemmi, H., Hochrein, H., Ampenberger, F., Kirschning, C., Akira, S., Lipford, G., Wagner, H., & Bauer, S. (2004) · Science · doi:10.1126/science.1093620 · Cited by 3,947
Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
Kato, H., Takeuchi, O., Sato, S., Yoneyama, M., Yamamoto, M., Matsui, K., Uematsu, S., Jung, A., Kawai, T., Ishii, K. J., et al. (2006) · Nature · doi:10.1038/nature04734 · Cited by 3,888
Mammalian microRNAs predominantly act to decrease target mRNA levels
Guo, H., Ingolia, N. T., Weissman, J. S., & Bartel, D. P. (2010) · Nature · doi:10.1038/nature09267 · Cited by 3,886
Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
Kayagaki, N., Stowe, I. B., Lee, B. L., O’Rourke, K., Anderson, K., Warming, S., Cuellar, T., Haley, B., Roose-Girma, M., Phung, Q. T., et al. (2015) · Nature · doi:10.1038/nature15541 · Cited by 3,686
Takeuchi, O., Hoshino, K., Kawai, T., Sanjo, H., Takada, H., Ogawa, T., Takeda, K., & Akira, S. (1999) · Immunity · doi:10.1016/s1074-7613(00)80119-3 · Cited by 3,680
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
CpG motifs in bacterial DNA trigger direct B-cell activation
Krieg, A. M., Yi, A.-K., Matson, S., Waldschmidt, T. J., Bishop, G. A., Teasdale, R., Koretzky, G. A., & Klinman, D. M. (1995) · Nature · doi:10.1038/374546a0 · Cited by 3,508
Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA
Diebold, S. S., Kaisho, T., Hemmi, H., Akira, S., & Reis e Sousa, C. (2004) · Science · doi:10.1126/science.1093616 · Cited by 3,444
Approaching the asymptote? Evolution and revolution in immunology.Preprint
Janeway, C. (1989) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1989.054.01.003 · Cited by 3,396
Hoshino, K., Takeuchi, O., Kawai, T., Sanjo, H., Ogawa, T., Takeda, Y., Takeda, K., & Akira, S. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.7.3749 · Cited by 3,374
A guide to immunometabolism for immunologists
O'Neill, L. A. J., Kishton, R. J., & Rathmell, J. (2016) · Nature Reviews Immunology · doi:10.1038/nri.2016.70 · Cited by 3,315
Role of Adaptor TRIF in the MyD88-Independent Toll-Like Receptor Signaling Pathway
Yamamoto, M., Sato, S., Hemmi, H., Hoshino, K., Kaisho, T., Sanjo, H., Takeuchi, O., Sugiyama, M., Okabe, M., Takeda, K., et al. (2003) · Science · doi:10.1126/science.1087262 · Cited by 3,286
Bauernfeind, F. G., Horvath, G. L., Stutz, A., Alnemri, E. S., MacDonald, K. L., Speert, D. P., Fernandes‐Alnemri, T., Wu, J., Monks, B. G., Fitzgerald, K. A., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901363 · Cited by 3,087
Self-citationIL-10 inhibits cytokine production by activated macrophages
Fiorentino, D. F., Zlotnik, A., Mosmann, T. R., Howard, M., & O’Garra, A. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.147.11.3815 · Cited by 2,888
IKKε and TBK1 are essential components of the IRF3 signaling pathway
Fitzgerald, K. A., McWhirter, S. M., Faia, K. L., Rowe, D. C., Latz, E., Golenbock, D. T., Coyle, A. J., Liao, S.-M., & Maniatis, T. (2003) · Nature Immunology · doi:10.1038/ni921 · Cited by 2,680
Self-citationlincRNAs: Genomics, Evolution, and Mechanisms
Ulitsky, I., & Bartel, D. P. (2013) · Cell · doi:10.1016/j.cell.2013.06.020 · Cited by 2,652
Cyclic GMP-AMP Is an Endogenous Second Messenger in Innate Immune Signaling by Cytosolic DNA
Wu, J., Sun, L., Chen, X., Du, F., Shi, H., Chen, C., & Chen, Z. J. (2012) · Science · doi:10.1126/science.1229963 · Cited by 2,628
Small anti-viral compounds activate immune cells via the TLR7 MyD88–dependent signaling pathway
Hemmi, H., Kaisho, T., Takeuchi, O., Sato, S., Sanjo, H., Hoshino, K., Horiuchi, T., Tomizawa, H., Takeda, K., & Akira, S. (2002) · Nature Immunology · doi:10.1038/ni758 · Cited by 2,580
The structural basis of lipopolysaccharide recognition by the TLR4–MD-2 complex
Park, B. S., Song, D. H., Kim, H. M., Choi, B., Lee, H., & Lee, J. (2009) · Nature · doi:10.1038/nature07830 · Cited by 2,513
Unresponsiveness of MyD88-deficient mice to endotoxin.
Kawai, T., Adachi, O., Ogawa, T., Takeda, K., & Akira, S. (1999) · Immunity · doi:10.1016/s1074-7613(00)80086-2 · Cited by 2,367
Merad, M., Sathe, P., Helft, J., Miller, J., & Mortha, A. (2013) · Annual Review of Immunology · doi:10.1146/annurev-immunol-020711-074950 · Cited by 2,309
IRF-7 is the master regulator of type-I interferon-dependent immune responses
Honda, K., Yanai, H., Negishi, H., Asagiri, M., Sato, M., Mizutani, T., Shimada, N., Ohba, Y., Takaoka, A., Yoshida, N., et al. (2005) · Nature · doi:10.1038/nature03464 · Cited by 2,229
mTOR- and HIF-1α–mediated aerobic glycolysis as metabolic basis for trained immunity
Cheng, S.-C., Quintin, J., Cramer, R. A., Shepardson, K. M., Saeed, S., Kumar, V., Giamarellos-Bourboulis, E. J., Martens, J. H. A., Rao, N. A., Aghajanirefah, A., et al. (2014) · Science · doi:10.1126/science.1250684 · Cited by 2,224
Molecular mechanism and physiological functions of clathrin-mediated endocytosis
McMahon, H. T., & Boucrot, E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3151 · Cited by 2,223
MD-2, a Molecule that Confers Lipopolysaccharide Responsiveness on Toll-like Receptor 4
Shimazu, R., Akashi, S., Ogata, H., Nagai, Y., Fukudome, K., Miyake, K., & Kimoto, M. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.11.1777 · Cited by 2,187
TAK1 is a ubiquitin-dependent kinase of MKK and IKK
Wang, C., Deng, L., Hong, M., Akkaraju, G. R., Inoue, J.-I., & Chen, Z. J. (2001) · Nature · doi:10.1038/35085597 · Cited by 2,125
A family of human receptors structurally related to Drosophila Toll.
Rock, F., Hardiman, G., Timans, J., Kastelein, R., & Bazan, J. (1998) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.95.2.588 · Cited by 2,009
Hornung, V., Rothenfußer, S., Britsch, S., Krug, A., Jahrsdörfer, B., Giese, T., Endres, S., & Hartmann, G. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.9.4531 · Cited by 1,970
Chromatin–IgG complexes activate B cells by dual engagement of IgM and Toll-like receptors
Leadbetter, E. A., Rifkin, I. R., Hohlbaum, A. M., Beaudette-Zlatanova, B. C., Shlomchik, M. J., & Marshak‐Rothstein, A. (2002) · Nature · doi:10.1038/416603a · Cited by 1,929
Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation
Liu, S., Cai, X., Wu, J., Cong, Q., Chen, X., Li, T., Du, F., Ren, J., Wu, Y.-T., Grishin, N. V., et al. (2015) · Science · doi:10.1126/science.aaa2630 · Cited by 1,927
Immunometabolism governs dendritic cell and macrophage function
O'Neill, L. A. J., & Pearce, E. J. (2015) · The Journal of Experimental Medicine · doi:10.1084/jem.20151570 · Cited by 1,779
Kleinnijenhuis, J., Quintin, J., Preijers, F., Joosten, L. A. B., Ifrim, D. C., Saeed, S., Jacobs, C., van Loenhout, J., de Jong, D., Stunnenberg, H. G., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1202870109 · Cited by 1,728
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
Asseman, C., Mauze, S., Leach, M. W., Coffman, R. L., & Powrie, F. M. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.7.995 · Cited by 1,617
The IL-23-IL-17 immune axis: from mechanisms to therapeutic testing
Gaffen, S. L., Jain, R., Garg, A. V., & Cua, D. J. (2014) · Nature reviews. Immunology · doi:10.1038/nri3707 · Cited by 1,585
Endotoxin-tolerant Mice Have Mutations in Toll-like Receptor 4 ( Tlr4 )
Qureshi, S. T., Larivière, L., Leveque, G., Clermont, S., Moore, K. J., Gros, P., & Malo, D. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.4.615 · Cited by 1,532
Crystal Structure of the TLR1-TLR2 Heterodimer Induced by Binding of a Tri-Acylated Lipopeptide
Jin, M. S., Kim, S. E., Heo, J. Y., Lee, M. E., Kim, H. M., Paik, S., Lee, H., & Lee, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.008 · Cited by 1,391
Tian, J., Avalos, A. M., Mao, S.-Y., Chen, B., Senthil, K., Wu, H., Parroche, P., Drabic, S., Golenbock, D., Sirois, C., et al. (2007) · Nature Immunology · doi:10.1038/ni1457 · Cited by 1,372
Self-citationCutting Edge: Role of Toll-Like Receptor 1 in Mediating Immune Response to Microbial Lipoproteins
Takeuchi, O., Sato, S., Horiuchi, T., Hoshino, K., Takeda, K., Dong, Z., Modlin, R. L., & Akira, S. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.1.10 · Cited by 1,360
Gewirtz, A. T., Navas, T. A., Lyons, S., Godowski, P. J., & Madara, J. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.4.1882 · Cited by 1,345
Gene-specific control of inflammation by TLR-induced chromatin modifications
Foster, S. L., Hargreaves, D. C., & Medzhitov, R. (2007) · Nature · doi:10.1038/nature05836 · Cited by 1,344
TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-β
Kagan, J. C., Su, T., Horng, T., Chow, A. Y., Akira, S., & Medzhitov, R. M. (2008) · Nature Immunology · doi:10.1038/ni1569 · Cited by 1,310
Self-citationTRAF6 is a signal transducer for interleukin-1
Cao, Z., Xiong, J., Takeuchi, M., Kurama, T., & Goeddel, D. V. (1996) · Nature · doi:10.1038/383443a0 · Cited by 1,305
Quintin, J., Saeed, S., Martens, J. H. A., Giamarellos-Bourboulis, E. J., Ifrim, D. C., Logie, C., Jacobs, L., Jansen, T., Kullberg, B.-J., Wijmenga, C., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.06.006 · Cited by 1,289
Pyogenic Bacterial Infections in Humans with MyD88 Deficiency
von Bernuth, H., Pïcard, C., Jin, Z., Sranujit, R. P., Xiao, H. Q., Ku, C., Chrabieh, M., Ben‐Mustapha, I., Ghandil, P., Çamcıoğlu, Y., et al. (2008) · Science · doi:10.1126/science.1158298 · Cited by 1,287
TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signalingPreprint
Lomaga, M. A., Yeh, W., Sarosi, I., Duncan, G. S., Furlonger, C. L., Ho, A. P., Morony, S., Capparelli, C., Van, G. Y., Kaufman, S., et al. (1999) · Genes & Development · doi:10.1101/gad.13.8.1015 · Cited by 1,265
Vaccination greatly reduces disease, disability, death and inequity worldwide
Fe, A., Booy, R., Bock, H. L., Clemens, J. D., Datta, S., John, T. J., Lee, B. W., Lolekha, S., Peltola, H., Ruff, T., et al. (2008) · Bulletin of the World Health Organization · doi:10.2471/blt.07.040089 · Cited by 1,261
Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction
Fitzgerald, K. A., Pålsson‐McDermott, E. M., Bowie, A., Jefferies, C. A., Mansell, A. S., Brady, G., Brint, E. K., Dunne, A., Gray, P., Harte, M. T., et al. (2001) · Nature · doi:10.1038/35092578 · Cited by 1,258
Self-citationDiscrimination of bacterial lipoproteins by Toll-like receptor 6
Takeuchi, O., Kawai, T., Mühlradt, P. F., Morr, M., Radolf, J. D., Zychlinsky, A., Takeda, K., & Akira, S. (2001) · International Immunology · doi:10.1093/intimm/13.7.933 · Cited by 1,233
LPS-TLR4 Signaling to IRF-3/7 and NF-κB Involves the Toll Adapters TRAM and TRIF
Fitzgerald, K. A., Rowe, D. C., Barnes, B. J., Caffrey, D. R., Visintin, A., Latz, E., Monks, B. G., Pitha, P. M., & Golenbock, D. T. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20031023 · Cited by 1,193
Self-citationGitlin, 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
Kawai, T., Takeuchi, O., Fujita, T., Inoue, J., Mühlradt, P. F., Sato, S., Hoshino, K., & Akira, S. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.10.5887 · Cited by 1,115
Helical Assembly in the MyD88-IRAK4-IRAK2 Complex in TLR/IL-1R Signalling
Lin, S.-C., Lo, Y.-C., & Wu, H. (2010) · Nature · doi:10.1038/nature09121 · Cited by 1,111
Li, K., Foy, E. M., Ferreon, J. C., Nakamura, M., Ferreon, A. C. M., Ikeda, M., Ray, S. C., Gale, M., & Lemon, S. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408824102 · Cited by 1,092
Christensen, S. R., Shupe, J., Nickerson, K., Kashgarian, M., Flavell, R. A., & Shlomchik, M. J. (2006) · Immunity · doi:10.1016/j.immuni.2006.07.013 · Cited by 1,090
Integral role of IRF-5 in the gene induction programme activated by Toll-like receptors
Takaoka, A., Yanai, H., Kondo, S., Duncan, G. S., Negishi, H., Mizutani, T., Kano, S., Honda, K., Ohba, Y., Mak, T. W., et al. (2005) · Nature · doi:10.1038/nature03308 · Cited by 1,066
Everts, B., Amiel, E., Huang, S. C.-C., Smith, A. M., Chang, C.-H., Lam, W. Y., Redmann, V., Freitas, T. C., Blagih, J., van der Windt, G. J. W., et al. (2014) · Nature Immunology · doi:10.1038/ni.2833 · Cited by 1,064
Kawai, T., Sato, S., Ishii, K. J., Coban, C., Hemmi, H., Yamamoto, M., Terai, K., Matsuda, M., Inoue, J., Uematsu, S., et al. (2004) · Nature Immunology · doi:10.1038/ni1118 · Cited by 1,058
TLR3 Deficiency in Patients with Herpes Simplex Encephalitis
Zhang, S.-Y., Jouanguy, E., Ugolini, S., Smahi, A., Elain, G., Romero, P., Segal, D., Sancho-Shimizu, V., Lorenzo, L., Puel, A., et al. (2007) · Science · doi:10.1126/science.1139522 · Cited by 1,057
Mitchell, S. A., Vargas, J. D., & Hoffmann, A. (2016) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1331 · Cited by 1,057
Yamamoto, M., Sato, S., Hemmi, H., Uematsu, S., Hoshino, K., Kaisho, T., Takeuchi, O., Takeda, K., & Akira, S. (2003) · Nature Immunology · doi:10.1038/ni986 · Cited by 1,052
TLR11 Activation of Dendritic Cells by a Protozoan Profilin-Like Protein
Yarovinsky, F., Zhang, D., Andersen, J. F., Bannenberg, G. L., Serhan, C. N., Hayden, M. S., Hieny, S. E., Sutterwala, F. S., Flavell, R. A., Ghosh, S., et al. (2005) · Science · doi:10.1126/science.1109893 · Cited by 1,049
Necroptosis 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
CD14 Controls the LPS-Induced Endocytosis of Toll-like Receptor 4
Zanoni, I., Ostuni, R., Marek, L. R., Barresi, S., Barbalat, R., Barton, G. M., Granucci, F., & Kagan, J. C. (2011) · Cell · doi:10.1016/j.cell.2011.09.051 · Cited by 997
Self-citationTIRAP: an adapter molecule in the Toll signaling pathway
Horng, T., Barton, G. M., & Medzhitov, R. M. (2001) · Nature Immunology · doi:10.1038/ni0901-835 · Cited by 970
Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6
Häcker, H., Redecke, V., Blagoev, B., Kratchmarova, I., Hsu, L.-C., Wang, G. G., Kamps, M. P., Raz, E., Wagner, H., Häcker, G. A., et al. (2005) · Nature · doi:10.1038/nature04369 · Cited by 962
A Long Noncoding RNA Mediates Both Activation and Repression of Immune Response Genes
Carpenter, S. B., Aiello, D. A., Atianand, M., Ricci, E. P., Gandhi, P., Hall, L. L., Byron, M., Monks, B. G., Henry-Bezy, M., Lawrence, J. B., et al. (2013) · Science · doi:10.1126/science.1240925 · Cited by 957
Self-citationToll-like receptor 3 promotes cross-priming to virus-infected cells
Schulz, O., Diebold, S. S., Chen, M., Näslund, T. I., Nolte, M. A., Alexopoulou, L., Azuma, Y., Flavell, R. A., Liljeström, P., & Sousa, C. R. E. (2005) · Nature · doi:10.1038/nature03326 · Cited by 919
Spatiotemporal regulation of MyD88–IRF-7 signalling for robust type-I interferon induction
Honda, K., Ohba, Y., Yanai, H., Negishi, H., Mizutani, T., Takaoka, A., Taya, C., & Taniguchi, T. (2005) · Nature · doi:10.1038/nature03547 · Cited by 908
IRAK: A Kinase Associated with the Interleukin-1 Receptor
Cao, Z., Henzel, W. J., & Gao, X. (1996) · Science · doi:10.1126/science.271.5252.1128 · Cited by 898
MicroRNAs: the fine-tuners of Toll-like receptor signalling
O'Neill, L. A. J., Sheedy, F. J., & McCoy, C. E. (2011) · Nature reviews. Immunology · doi:10.1038/nri2957 · Cited by 881
RIP1 is an essential mediator of Toll-like receptor 3–induced NF-κB activation
Meylan, E., Burns, K., Hofmann, K., Blancheteau, V., Martinon, F., Kelliher, M. A., & Tschopp, J. (2004) · Nature Immunology · doi:10.1038/ni1061 · Cited by 877
Phosphoinositide-Mediated Adaptor Recruitment Controls Toll-like Receptor Signaling
Kagan, J. C., & Medzhitov, R. M. (2006) · Cell · doi:10.1016/j.cell.2006.03.047 · Cited by 868
Self-citationInflammatory caspases and inflammasomes: master switches of inflammation
Martinon, F., & Tschopp, J. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402038 · Cited by 848
Toll-dependent selection of microbial antigens for presentation by dendritic cells
Blander, J. M., & Medzhitov, R. M. (2006) · Nature · doi:10.1038/nature04596 · Cited by 841
Toll-like receptors in the pathogenesis of human disease
Cook, D. N., Pisetsky, D. S., & Schwartz, D. A. (2004) · Nature Immunology · doi:10.1038/ni1116 · Cited by 827
The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors
Horng, T., Barton, G. M., Flavell, R. A., & Medzhitov, R. M. (2002) · Nature · doi:10.1038/nature01180 · Cited by 825
HIF1α and metabolic reprogramming in inflammation
Corcoran, S. E., & O'Neill, L. A. J. (2016) · Journal of Clinical Investigation · doi:10.1172/jci84431 · Cited by 814
Human Monocytes Engage an Alternative Inflammasome Pathway
Gaidt, M. M., Ebert, T. S., Chauhan, D., Schmidt, T., Schmid-Burgk, J. L., Rapino, F. A., Robertson, A. A. B., Cooper, M. A., Graf, T., & Hornung, V. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.012 · Cited by 808
TLR4, but not TLR2, mediates IFN-β–induced STAT1α/β-dependent gene expression in macrophages
Toshchakov, V. Y., Jones, B. W., Perera, P., Thomas, K., Cody, M. J., Zhang, S., Williams, B. R. G., Major, J. A., Hamilton, T. A., Fenton, M. J., et al. (2002) · Nature Immunology · doi:10.1038/ni774 · Cited by 802
Recognition of Lipopeptide Patterns by Toll-like Receptor 2-Toll-like Receptor 6 Heterodimer
Kang, J. Y., Nan, X., Jin, M. S., Youn, S.-J., Ryu, Y. H., Mah, S., Han, S. H., Lee, H., Paik, S., & Lee, J. (2009) · Immunity · doi:10.1016/j.immuni.2009.09.018 · Cited by 800
Control of B-cell responses by Toll-like receptors
Pasare, C., & Medzhitov, R. M. (2005) · Nature · doi:10.1038/nature04267 · Cited by 752
A cell biological view of Toll-like receptor function: regulation through compartmentalization
Barton, G. M., & Kagan, J. C. (2009) · Nature reviews. Immunology · doi:10.1038/nri2587 · Cited by 746
Self-citationActivation of Lysosomal Function During Dendritic Cell Maturation
Trombetta, E. S., Ebersold, M. W., Garrett, W. S., Pypaert, M., & Mellman, I. (2003) · Science · doi:10.1126/science.1080106 · Cited by 740
TRIF Licenses Caspase-11-Dependent NLRP3 Inflammasome Activation by Gram-Negative Bacteria
Rathinam, V. A. K., Vanaja, S. K., Waggoner, L., Sokolovska, A., Becker, C., Stuart, L. M., Leong, J. M., & Fitzgerald, K. A. (2012) · Cell · doi:10.1016/j.cell.2012.07.007 · Cited by 729
Self-citationHerpes Simplex Virus Encephalitis in Human UNC-93B Deficiency
Casrouge, A., Zhang, S.-Y., Eidenschenk, C., Jouanguy, E., Puel, A., Yang, K., Alcais, A., Picard, C., Mahfoufi, N., Nicolas, N., et al. (2006) · Science · doi:10.1126/science.1128346 · Cited by 725
Deubiquitination of NLRP3 by BRCC3 Critically Regulates Inflammasome Activity
Py, B. F., Kim, M.-S., Vakifahmetoglu-Norberg, H., & Yuan, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.009 · Cited by 718
Gottar, M., Gobert, V., Michel, T., Belvin, M. P., Duyk, G. M., Hoffmann, J. A., Ferrandon, D., & Royet, J. (2002) · Nature · doi:10.1038/nature734 · Cited by 715
IRAK-4: A novel member of the IRAK family with the properties of an IRAK-kinase
Li, S., Strelow, A., Fontana, E. J., & Wesche, H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082100399 · Cited by 714
Barton, G. M., Kagan, J. C., & Medzhitov, R. M. (2005) · Nature Immunology · doi:10.1038/ni1280 · Cited by 701
Self-citationAnderson, K. V., Jürgens, G., & Nüsslein-Volhard, C. (1985) · Cell · doi:10.1016/0092-8674(85)90274-0 · Cited by 691
Cell intrinsic immunity spreads to bystander cells via the intercellular transfer of cGAMP
Ablasser, A., Schmid-Burgk, J. L., Hemmerling, I., Horvath, G. L., Schmidt, T., Latz, E., & Hornung, V. (2013) · Nature · doi:10.1038/nature12640 · Cited by 682
Soluble CD14 participates in the response of cells to lipopolysaccharide.
Frey, E. A., Miller, D. S., Jahr, T. G., Sundan, A., Bažil, V., Espevik, T., Finlay, B. B., & Wright, S. D. (1992) · The Journal of Experimental Medicine · doi:10.1084/jem.176.6.1665 · Cited by 682
UNC93B1 delivers nucleotide-sensing toll-like receptors to endolysosomes
Kim, Y.-M., Brinkmann, M. M., Paquet, M.-E., & Ploegh, H. L. (2008) · Nature · doi:10.1038/nature06726 · Cited by 645
Anderson, K. V., Bokla, L., & Nüsslein‐Volhard, C. (1985) · Cell · doi:10.1016/0092-8674(85)90275-2 · Cited by 623
Drosophila Toll and IL-1 receptor
Gay, N. J., & Keith, F. J. (1991) · Nature · doi:10.1038/351355b0 · Cited by 623
Crystal Structure of Human Toll-Like Receptor 3 (TLR3) Ectodomain
Choe, J., Kelker, M. S., & Wilson, I. A. (2005) · Science · doi:10.1126/science.1115253 · Cited by 620
Tabeta, K., Hoebe, K., Janssen, E. M., Du, X., Georgel, P., Crozat, K., Mudd, S., Mann, N., Sovath, S., Goode, J., et al. (2006) · Nature Immunology · doi:10.1038/ni1297 · Cited by 600
Triantafilou, M., Miyake, K., Golenbock, D. T., & Triantafilou, K. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.12.2603 · Cited by 581
Franchi, L., Eigenbrod, T., & Núñez, G. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900173 · Cited by 574
Structures of the Toll-like Receptor Family and Its Ligand Complexes
Jin, M. S., & Lee, J. (2008) · Immunity · doi:10.1016/j.immuni.2008.07.007 · Cited by 573
Toll receptors, CD14, and macrophage activation and deactivation by LPS
Dobrovolskaia, M. A., & Vogel, S. N. (2002) · Microbes and Infection · doi:10.1016/s1286-4579(02)01613-1 · Cited by 562
O'Neill, L. A. J., & Greene, C. M. (1998) · Journal of Leukocyte Biology · doi:10.1002/jlb.63.6.650 · Cited by 556
Edwards, A. D., Diebold, S. S., Slack, E. M. C., Tomizawa, H., Hemmi, H., Kaisho, T., Akira, S., & Sousa, C. R. E. (2003) · European Journal of Immunology · doi:10.1002/eji.200323797 · Cited by 550
Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum.
Tobias, P. S., Soldau, K., & Ulevitch, R. J. (1986) · The Journal of Experimental Medicine · doi:10.1084/jem.164.3.777 · Cited by 547
McWhirter, S. M., Fitzgerald, K. A., Rosains, J., Rowe, D. C., Golenbock, D. T., & Maniatis, T. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2237236100 · Cited by 542
Self-citationCaspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1
Broz, P., Ruby, T., Belhocine, K., Bouley, D. M., Kayagaki, N., Dixit, V. M., & Monack, D. M. (2012) · Nature · doi:10.1038/nature11419 · Cited by 535
Honda, K., Yanai, H., Mizutani, T., Negishi, H., Shimada, N., Suzuki, N., Ohba, Y., Takaoka, A., Yeh, W., & Taniguchi, T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406933101 · Cited by 526
Toll-like receptor 9 controls anti-DNA autoantibody production in murine lupus
Christensen, S. R., Kashgarian, M. J., Alexopoulou, L., Flavell, R. A., Akira, S., & Shlomchik, M. J. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050338 · Cited by 521
NLRP3 Phosphorylation Is an Essential Priming Event for Inflammasome Activation
Song, N., Liu, Z.-S., Xue, W., Bai, Z., Wang, Q., Dai, J., Liu, X., Huang, Y.-J., Cai, H., Zhan, X., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.017 · Cited by 521
Identification of a monocyte specific pre-interleukin 1 beta convertase activity.
Kostura, M. J., Tocci, M. J., Limjuco, G. A., Chin, J., Cameron, P. M., Hillman, A. G., Chartrain, N. A., & Schmidt, J. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.14.5227 · Cited by 518
Interferon-λ: Immune Functions at Barrier Surfaces and Beyond
Lazear, H. M., Nice, T. J., & Diamond, M. (2015) · Immunity · doi:10.1016/j.immuni.2015.07.001 · Cited by 493
Uematsu, S., Sato, S., Yamamoto, M., Hirotani, T., Kato, H., Takeshita, F., Matsuda, M., Coban, C., Ishii, K. J., Kawai, T., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20042372 · Cited by 488
Steward, R. (1987) · Science · doi:10.1126/science.3118464 · Cited by 486
A mammalian pseudogene lncRNA at the interface of inflammation and anti-inflammatory therapeutics
Rapicavoli, N. A., Qu, K., Zhang, J., Mikhail, M. E., Laberge, R.-M., & Chang, H. Y. (2013) · eLife · doi:10.7554/elife.00762 · Cited by 482
Transport of Peptide-MHC Class II Complexes in Developing Dendritic Cells
Turley, S. J., Inaba, K., Garrett, W. S., Ebersold, M. W., Unternaehrer, J., Steinman, R. M., & Mellman, I. (2000) · Science · doi:10.1126/science.288.5465.522 · Cited by 477
Barbalat, R., Lau, L., Locksley, R. M., & Barton, G. M. (2009) · Nature Immunology · doi:10.1038/ni.1792 · Cited by 477
Triantafilou, M., Gamper, F. G. J., Haston, R. M., Mouratis, M. A., Morath, S., Härtung, T., & Triantafilou, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602794200 · Cited by 471
A46R and A52R from vaccinia virus are antagonists of host IL-1 and toll-like receptor signaling
Bowie, A., Kiss‐Toth, E., Symons, J. A., Smith, G. L., Dower, S., & O'Neill, L. A. J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160027697 · Cited by 466
Song, H., Liu, B., Huai, W., Yu, Z., Wang, W., Zhao, J., Han, L., Jiang, G., Zhang, L., Gao, C., et al. (2016) · Nature Communications · doi:10.1038/ncomms13727 · Cited by 466
Ligand-induced conformational changes allosterically activate Toll-like receptor 9
Latz, E., Verma, A., Visintin, A., Gong, M., Sirois, C. M., Klein, D. C. G., Monks, B. G., McKnight, C. J., Lamphier, M. S., Duprex, W. P., et al. (2007) · Nature Immunology · doi:10.1038/ni1479 · Cited by 462
Toll-like receptors: linking innate and adaptive immunity
Pasare, C., & Medzhitov, R. M. (2004) · Microbes and Infection · doi:10.1016/j.micinf.2004.08.018 · Cited by 461
Zhang, Z., Ohto, U., Shibata, T., Krayukhina, E., Taoka, M., Yamauchi, Y., Tanji, H., Isobe, T., Uchiyama, S., Miyake, K., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.09.011 · Cited by 461
Akashi, S., Shimazu, R., Ogata, H., Nagai, Y., Takeda, K., Kimoto, M., & Miyake, K. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.7.3471 · Cited by 459
A Long Noncoding RNA lincRNA-EPS Acts as a Transcriptional Brake to Restrain Inflammation
Atianand, M., Hu, W., Satpathy, A. T., Shen, Y., Ricci, E. P., Alvarez‐Dominguez, J. R., Bhatta, A., Schattgen, S., McGowan, J. D., Blin, J., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.075 · Cited by 446
Self-citationHoebe, K. H. N., Janssen, E. M., Kim, S. O., Alexopoulou, L., Flavell, R. A., Han, J., & Beutler, B. (2003) · Nature Immunology · doi:10.1038/ni1010 · Cited by 444
Activation of the canonical IKK complex by K63/M1-linked hybrid ubiquitin chains
Emmerich, C. H., Ordureau, A., Strickson, S., Arthur, J. S. C., Pedrioli, P. G. A., Komander, D., & Cohen, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314715110 · Cited by 442
Ryu, J., Kim, S. J., Rah, S.-H., Kang, J. I., Jung, H. E., Lee, D., Lee, H. K., Lee, J., Park, B. S., Yoon, T., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.11.007 · Cited by 437
Clinical Features and Outcome of Patients With IRAK-4 and MyD88 Deficiency
Pïcard, C., von Bernuth, H., Ghandil, P., Chrabieh, M., Levy, O., Arkwright, P. D., McDonald, D. R., Geha, R. S., Takada, H., Krause, J. C., et al. (2010) · Medicine · doi:10.1097/md.0b013e3181fd8ec3 · Cited by 425
The interferon regulatory factor, IRF5, is a central mediator of toll-like receptor 7 signaling
Schoenemeyer, A., Barnes, B. J., Mancl, M. E., Latz, E., Goutagny, N., Pitha, P. M., Fitzgerald, K. A., & Golenbock, D. T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412584200 · Cited by 411
Yang, Y., Liu, B., Dai, J., Srivastava, P. K., Zammit, D. J., Lefrançois, L., & Li, Z. (2007) · Immunity · doi:10.1016/j.immuni.2006.12.005 · Cited by 410
TLR13 Recognizes Bacterial 23 S rRNA Devoid of Erythromycin Resistance–Forming Modification
Oldenburg, M., Krüger, A., Ferstl, R., Kaufmann, A., Nees, G., Sigmund, A., Bathke, B., Lauterbach, H., Suter, M., Dreher, S., et al. (2012) · Science · doi:10.1126/science.1220363 · Cited by 405
Virulence factors of Yersinia pestis are overcome by a strong lipopolysaccharide response
Paquette, S. W. M., Khan, N. N., McGrath, S. C., Walkowicz, M. J., Sharp, F. A., Conlon, J. E., Fukase, K., Kusumoto, S., Sweet, C. R., Miyake, K., et al. (2006) · Nature Immunology · doi:10.1038/ni1386 · Cited by 404
Toll-like receptor 8 senses degradation products of single-stranded RNA
Tanji, H., Ohto, U., Shibata, T., Taoka, M., Yamauchi, Y., Isobe, T., Miyake, K., & Shimizu, T. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2943 · Cited by 404
Motshwene, P. G., Moncrieffe, M. C., Grossmann, J. G., Kao, C. C., Murali, A., Sandercock, A. M., Robinson, C. V., Latz, E., & Gay, N. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022392 · Cited by 403
Antimicrobial peptide resistance mediates resilience of prominent gut commensals during inflammation
Cullen, T. W., Schofield, W. B., Barry, N. A., Putnam, E. E., Rundell, E. A., Trent, M. S., Degnan, P. H., Booth, C. J., Yu, H., & Goodman, A. L. (2015) · Science · doi:10.1126/science.1260580 · Cited by 395
The instructive role of dendritic cells on T cell responses: lineages, plasticity and kinetics
Lanzavecchia, A., & Sallusto, F. (2001) · Current Opinion in Immunology · doi:10.1016/s0952-7915(00)00218-1 · Cited by 386
Toll-Dependent Control Mechanisms of CD4 T Cell Activation
Pasare, C., & Medzhitov, R. M. (2004) · Immunity · doi:10.1016/j.immuni.2004.10.006 · Cited by 383
Structural basis of CpG and inhibitory DNA recognition by Toll-like receptor 9
Ohto, U., Shibata, T., Tanji, H., Ishida, H., Krayukhina, E., Uchiyama, S., Miyake, K., & Shimizu, T. (2015) · Nature · doi:10.1038/nature14138 · Cited by 377
Anders, H., Banas, B., & Schlöndorff, D. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000121781.89599.16 · Cited by 374
The Poxvirus Protein A52R Targets Toll-like Receptor Signaling Complexes to Suppress Host Defense
Harte, M. T., Haga, I. R., Maloney, G., Gray, P., Reading, P. C., Bartlett, N. W., Smith, G. L., Bowie, A., & O'Neill, L. A. J. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021652 · Cited by 372
Viganò, E., Diamond, C. E., Spreafico, R., Balachander, A., Sobota, R. M., & Mortellaro, A. (2015) · Nature Communications · doi:10.1038/ncomms9761 · Cited by 367
Gioannini, T. L., Teghanemt, A., Zhang, D., Coussens, N. P., Dockstader, W., Ramaswamy, S., & Weiss, J. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306906101 · Cited by 366
Hermance, N. M., Khurana, S., Lee, T. H.-Y., Fitzgerald, K. A., & Kelliher, M. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506831200 · Cited by 359
Self-citationBifurcation of Toll-Like Receptor 9 Signaling by Adaptor Protein 3
Sasai, M., Linehan, M. M., & Iwasaki, A. (2010) · Science · doi:10.1126/science.1187029 · Cited by 357
Activation of Drosophila Toll During Fungal Infection by a Blood Serine Protease
Ligoxygakis, P., Pelte, N., Hoffmann, J. A., & Reichhart, J. (2002) · Science · doi:10.1126/science.1072391 · Cited by 354
de Diego, R. P., Sancho‐Shimizu, V., Lorenzo, L., Puel, A., Plancoulaine, S., Pïcard, C., Casadio, M., Cardon, A., Durandy, A., Bustamante, J. C., et al. (2010) · Immunity · doi:10.1016/j.immuni.2010.08.014 · Cited by 348
Nair-Gupta, P., Baccarini, A., Tung, N., Seyffer, F., Florey, O., Huang, Y., Banerjee, M., Overholtzer, M., Roche, P. A., Tampé, R., et al. (2014) · Cell · doi:10.1016/j.cell.2014.04.054 · Cited by 344
Contribution of dendritic cells to stimulation of the murine syngeneic mixed leukocyte reaction.
Nussenzweig, M. C., & Steinman, R. M. (1980) · The Journal of Experimental Medicine · doi:10.1084/jem.151.5.1196 · Cited by 327
Schneider, D. S., Hudson, K. L., Lin, T. Y., & Anderson, K. V. (1991) · Genes & Development · doi:10.1101/gad.5.5.797 · Cited by 325
Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
Randow, F., & Seed, B. (2001) · Nature Cell Biology · doi:10.1038/ncb1001-891 · Cited by 316
Mukherjee, A., Morosky, S. A., Delorme‐Axford, E., Dybdahl-Sissoko, N., Oberste, M. S., Wang, T., & Coyne, C. B. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1001311 · Cited by 316
Ewald, S. E., Engel, A., Lee, J., Wang, M., Bogyo, M. S., & Barton, G. M. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20100682 · Cited by 314
SMOCs: supramolecular organizing centres that control innate immunity
Kagan, J. C., Magupalli, V. G., & Wu, H. (2014) · Nature reviews. Immunology · doi:10.1038/nri3757 · Cited by 310
Self-citationNegishi, H., Fujita, Y., Yanai, H., Sakaguchi, S., Ouyang, X., Shinohara, M., Takayanagi, H., Ohba, Y., Taniguchi, T., & Honda, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607181103 · Cited by 310
Selective requirement for c-Rel during IL-12 P40 gene induction in macrophages
Sanjabi, S., Hoffmann, A., Liou, H., Baltimore, D., & Smale, S. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.230436397 · Cited by 308
Molecular Genetic Analysis of an Endotoxin Nonresponder Mutant Cell Line
Schromm, A. B., Lien, E., Henneke, P., Chow, J. C., Yoshimura, A., Heine, H., Latz, E., Monks, B. G., Schwartz, D. A., Miyake, K., et al. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.194.1.79 · Cited by 297
Helicobacter pylori Flagellin Evades Toll‐Like Receptor 5–Mediated Innate Immunity
Gewirtz, A. T., Yu, Y., Krishna, U. S., Israel, D. A., Lyons, S., & Peek, R. M. (2004) · The Journal of Infectious Diseases · doi:10.1086/386289 · Cited by 295
Rowe, D. C., McGettrick, A. F., Latz, E., Monks, B. G., Gay, N. J., Yamamoto, M., Akira, S., O'Neill, L. A. J., Fitzgerald, K. A., & Golenbock, D. T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510041103 · Cited by 286
Self-citationIRAK-1 bypasses priming and directly links TLRs to rapid NLRP3 inflammasome activation
Lin, K.-M., Hu, W., Troutman, T. D., Jennings, M., Brewer, T., Li, X., Nanda, S. K., Cohen, P., Thomas, J. A., & Pasare, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1320294111 · Cited by 285
UNC93B1 mediates differential trafficking of endosomal TLRs
Lee, B. L., Moon, J. E., Shu, J. H., Yuan, L., Newman, Z. R., Schekman, R., & Barton, G. M. (2013) · eLife · doi:10.7554/elife.00291 · Cited by 281
The TLR3 signaling complex forms by cooperative receptor dimerization
Leonard, J. N., Ghirlando, R., Askins, J., Bell, J. K., Margulies, D. H., Davies, D. R., & Segal, D. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710779105 · Cited by 279
Gasdermins and their role in immunity and inflammation
Ørning, P., Lien, E., & Fitzgerald, K. A. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20190545 · Cited by 277
Self-citationA critical role for IRAK4 kinase activity in Toll-like receptor–mediated innate immunity
Kim, T. W., Staschke, K. A., Bulek, K., Yao, J., Peters, K. L., Oh, K., Vandenburg, Y. R., Xiao, H. Q., Wen, Q., Hamilton, T., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20061825 · Cited by 276
Shimada, T., Park, B. G., Wolf, A. J., Brikos, C., Goodridge, H. S., Becker, C. A., Reyes, C. N., Miao, E. A., Aderem, A., Götz, F., et al. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2009.12.008 · Cited by 274
Homeostatic MyD88-dependent signals cause lethal inflamMation in the absence of A20
Turer, E. E., Tavares, R. M., Mortier, E., Hitotsumatsu, O., Advincula, R., Lee, B. L., Shifrin, N. T., Malynn, B. A., & Ma, A. I. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20071108 · Cited by 267
Sato, M., Tanaka, N., Hata, N., Oda, E., & Taniguchi, T. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00210-5 · Cited by 264
The LPS-inducible lncRNA Mirt2 is a negative regulator of inflammation
Du, M., Yuan, L., Tan, X., Huang, D., Wang, X., Zheng, Z., Mao, X., Li, X., Yang, L., Huang, K., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02229-1 · Cited by 264
Labéta, M. O., Vidal, K., Nores, J. E. R., Arias, M. A., Vita, N., Morgan, B. P., Guillemot, J. C., Loyaux, D., Ferrara, P., Schmid, D., et al. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.191.10.1807 · Cited by 254
Schappe, M. S., Szteyn, K., Stremska, M. E., Mendu, S. K., Downs, T. K., Seegren, P. V., Mahoney, M. A., Dixit, S., Krupa, J. K., Stipes, E. J., et al. (2018) · Immunity · doi:10.1016/j.immuni.2017.11.026 · Cited by 254
Zhang, J., Stirling, B., Temmerman, S. T., Ma, C. A., Fuss, I. J., Derry, J. M. J., & Jain, A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28746 · Cited by 245
A long noncoding RNA associated with susceptibility to celiac disease
Castellanos–Rubio, A., Fernández‐Jiménez, N., Kratchmarov, R., Luo, X., Bhagat, G., Green, P. H. R., Schneider, R. J., Kiledjian, M., Bilbao, J. R., & Ghosh, S. (2016) · Science · doi:10.1126/science.aad0467 · Cited by 245
Cutting Edge: TLR Signaling Licenses IRAK1 for Rapid Activation of the NLRP3 Inflammasome
Fernandes‐Alnemri, T., Kang, S., Anderson, C., Sagara, J., Fitzgerald, K. A., & Alnemri, E. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301681 · Cited by 243
Self-citationThe translation of non-canonical open reading frames controls mucosal immunity
Jackson, R., Kroehling, L., Khitun, A., Bailis, W., Jarret, A., York, A. G., Khan, O. M., Brewer, J. R., Skadow, M. H., Duizer, C., et al. (2018) · Nature · doi:10.1038/s41586-018-0794-7 · Cited by 242
Buchon, N., Poidevin, M., Kwon, H., Guillou, A., Sottas, V., Lee, B., & Lemaître, B. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901924106 · Cited by 233
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de Bouteiller, O., Merck, E., Hasan, U. A., Hubac, S., Benguigui, B., Trinchieri, G., Bates, E. E. M., & Caux, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507163200 · Cited by 220
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Metadata
- Authors
- Fitzgerald, K. A., & Kagan, J. C.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Boston Children's Hospital (US)
- Corresponding author
- Fitzgerald, Katherine A.
- Kagan, Jonathan C.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-03
- Volume
- 180
- Issue
- 6
- Pages
- 1044-1066
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC9358771
- OpenAlex
- W3012283572
- Cited by
- 2,168
- References
- 272
- Citations by year
- 2026: 299 · 2025: 392 · 2024: 428 · 2023: 386 · 2022: 343 · 2021: 244 · 2020: 73
- FWCI
- 25.68
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 383 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases
- National Institute of Diabetes and Digestive and Kidney Diseases
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
- Keywords
- Toll-like receptors, innate immunity, pattern recognition receptors, inducible gene expression, adaptive immunity, inflammation, host defense, therapeutics
- MeSH terms
- Animals, Humans, Immunity, Innate, Inflammation, Organelles, Signal Transduction, Toll-Like Receptors, Adaptive Immunity
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