Toll-like receptors and innate immunity (original) (raw)

• Janeway, C. A. Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb. Symp. Quant. Biol. 54, 1–13 (1989).This is a landmark paper that introduced the concepts of pattern recognition and the role of innate immune recognition in the control of adaptive immunity.
  CAS PubMed Google Scholar
• Janeway, C. A. Jr. The immune system evolved to discriminate infectious nonself from noninfectious self. Immunol. Today 13, 11–16 (1992).
  Article CAS PubMed Google Scholar
• Medzhitov, R. & Janeway, C. A. Jr. Innate immunity: impact on the adaptive immune response. Curr. Opin. Immunol. 9, 4–9 (1997).
  CAS PubMed Google Scholar
• Hashimoto, C., Hudson, K. L. & Anderson, K. V. The Toll gene of Drosophila, required for dorsal–ventral embryonic polarity, appears to encode a transmembrane protein. Cell 52, 269–279 (1988).
  CAS PubMed Google Scholar
• Medzhitov, R., Preston-Hurlburt, P. & Janeway, C. A. Jr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 388, 394–397 (1997).
  Article CAS PubMed Google Scholar
• Rock, F. L., Hardiman, G., Timans, J. C., Kastelein, R. A. & Bazan, J. F. A family of human receptors structurally related to Drosophila Toll. Proc. Natl Acad. Sci. USA 95, 588–593 (1998).
  CAS PubMed PubMed Central Google Scholar
• Kobe, B. & Deisenhofer, J. Proteins with leucine-rich repeats. Curr. Opin. Struct. Biol. 5, 409–416 (1995).
  CAS PubMed Google Scholar
• Aravind, L., Dixit, V. M. & Koonin, E. V. Apoptotic molecular machinery: vastly increased complexity in vertebrates revealed by genome comparisons. Science 291, 1279–1284 (2001).
  CAS PubMed Google Scholar
• Muzio, M., Ni, J., Feng, P. & Dixit, V. M. IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. Science 278, 1612–1615 (1997).
  CAS PubMed Google Scholar
• Medzhitov, R. et al. MyD88 is an adaptor protein in the hToll/IL-1 receptor family signaling pathways. Mol. Cell 2, 253–258 (1998).
  Article CAS PubMed Google Scholar
• Wesche, H., Henzel, W. J., Shillinglaw, W., Li, S. & Cao, Z. MyD88: an adapter that recruits IRAK to the IL-1 receptor complex. Immunity 7, 837–847 (1997).
  CAS PubMed Google Scholar
• Burns, K. et al. MyD88, an adapter protein involved in interleukin-1 signaling. J. Biol. Chem. 273, 12203–12209 (1998).
  CAS PubMed Google Scholar
• Horng, T., Barton, G. M. & Medzhitov, R. TIRAP: an adapter molecule in the Toll signaling pathway. Nature Immunol. 2, 835–841 (2001).
  CAS Google Scholar
• Anderson, K. V. Toll signaling pathways in the innate immune response. Curr. Opin. Immunol. 12, 13–19 (2000).
  CAS PubMed Google Scholar
• Belvin, M. P. & Anderson, K. V. A conserved signaling pathway: the Drosophila Toll-dorsal pathway. Annu. Rev. Cell Dev. Biol. 12, 393–416 (1996).
  CAS PubMed Google Scholar
• Lemaitre, B., Nicolas, E., Michaut, L., Reichhart, J. M. & Hoffmann, J. A. The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 86, 973–983 (1996).This is a seminal study that showed the role of the Toll pathway in Drosophila immunity.
  CAS PubMed Google Scholar
• Meng, X., Khanuja, B. S. & Ip, Y. T. Toll receptor-mediated Drosophila immune response requires Dif, an NF-κB factor. Genes Dev. 13, 792–797 (1999).
  CAS PubMed PubMed Central Google Scholar
• Rutschmann, S. et al. The Rel protein DIF mediates the antifungal but not the antibacterial host defense in Drosophila. Immunity 12, 569–580 (2000).
  CAS PubMed Google Scholar
• Levashina, E. A. et al. Constitutive activation of Toll-mediated antifungal defense in serpin-deficient Drosophila. Science 285, 1917–1919 (1999).
  CAS PubMed Google Scholar
• Khush, R. S., Leulier, F. & Lemaitre, B. Drosophila immunity: two paths to NF-κB. Trends Immunol. 22, 260–264 (2001).
  CAS PubMed Google Scholar
• Lemaitre, B., Reichhart, J. M. & Hoffmann, J. A. Drosophila host defense: differential induction of antimicrobial peptide genes after infection by various classes of microorganisms. Proc. Natl Acad. Sci. USA 94, 14614–14619 (1997).This study indicated that Drosophila can discriminate between different pathogen classes and induce an appropriate set of antimicrobial peptides.
  CAS PubMed PubMed Central Google Scholar
• Lemaitre, B. et al. A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense. Proc. Natl Acad. Sci. USA 92, 9465–9469 (1995).
  CAS PubMed PubMed Central Google Scholar
• Imler, J. L. & Hoffmann, J. A. Signaling mechanisms in the antimicrobial host defense of Drosophila. Curr. Opin. Microbiol. 3, 16–22 (2000).
  CAS PubMed Google Scholar
• Georgel, P. et al. Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defence and can promote apoptosis. Dev. Cell 1, 503–514 (2001)
  Article CAS PubMed Google Scholar
• Elrod-Erickson, M., Mishra, S. & Schneider, D. Interactions between the cellular and humoral immune responses in Drosophila. Curr. Biol. 10, 781–784 (2000).
  CAS PubMed Google Scholar
• Leulier, F., Rodriguez, A., Khush, R. S., Abrams, J. M. & Lemaitre, B. The Drosophila caspase Dredd is required to resist Gram-negative bacterial infection. EMBO Rep. 1, 353–358 (2000).
  CAS PubMed PubMed Central Google Scholar
• Lu, Y., Wu, L. P. & Anderson, K. V. The antibacterial arm of the Drosophila innate immune response requires an IκB kinase. Genes Dev. 15, 104–110 (2001).
  CAS PubMed PubMed Central Google Scholar
• Silverman, N. et al. A Drosophila IκB kinase complex required for relish cleavage and antibacterial immunity. Genes Dev. 14, 2461–2471 (2000).
  CAS PubMed PubMed Central Google Scholar
• Rutschmann, S. et al. Role of Drosophila IKK-γ in a Toll-independent antibacterial immune response. Nature Immunol. 1, 342–347 (2000).
  CAS Google Scholar
• Vidal, S. et al. Mutations in the Drosophila dTAK1 gene reveal a conserved function for MAPKKKs in the control of rel/NF-κB-dependent innate immune responses. Genes Dev. 15, 1900–1912 (2001).
  CAS PubMed PubMed Central Google Scholar
• Hedengren, M. et al. Relish, a central factor in the control of humoral but not cellular immunity in Drosophila. Mol. Cell 4, 827–837 (1999).
  CAS PubMed Google Scholar
• Chen, P., Rodriguez, A., Erskine, R., Thach, T. & Abrams, J. M. Dredd, a novel effector of the apoptosis activators reaper, grim, and hid in Drosophila. Dev. Biol. 201, 202–216 (1998).
  CAS PubMed Google Scholar
• Karin, M. & Delhase, M. The IκB kinase (IKK) and NF-κB: key elements of proinflammatory signalling. Semin. Immunol. 12, 85–98 (2000).
  CAS PubMed Google Scholar
• Dushay, M. S., Asling, B. & Hultmark, D. Origins of immunity: Relish, a compound Rel-like gene in the antibacterial defense of Drosophila. Proc. Natl Acad. Sci. USA 93, 10343–10347 (1996).
  CAS PubMed PubMed Central Google Scholar
• Tauszig, S., Jouanguy, E., Hoffmann, J. A. & Imler, J. L. From the cover: Toll-related receptors and the control of antimicrobial peptide expression in Drosophila. Proc. Natl Acad. Sci. USA 97, 10520–10525 (2000).
  CAS PubMed PubMed Central Google Scholar
• Williams, M. J., Rodriguez, A., Kimbrell, D. A. & Eldon, E. D. The 18-wheeler mutation reveals complex antibacterial gene regulation in Drosophila host defense. EMBO J. 16, 6120–6130 (1997).
  CAS PubMed PubMed Central Google Scholar
• Akira, S., Takeda, K. & Kaisho, T. Toll-like receptors: critical proteins linking innate and acquired immunity. Nature Immunol. 2, 675–680 (2001).
  CAS Google Scholar
• Poltorak, A. et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 282, 2085–2088 (1998).
  Article CAS PubMed Google Scholar
• Qureshi, S. T. et al. Endotoxin-tolerant mice have mutations in Toll-like receptor 4 (Tlr4). J. Exp. Med. 189, 615–625 (1999); erratum 189, 1518 (1999). | PubMed |
  CAS PubMed PubMed Central Google Scholar
• Hoshino, K. et al. Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product. J. Immunol. 162, 3749–3752 (1999).References 38–40 describe the first indication of TLR4 function in vivo.
  CAS PubMed Google Scholar
• Wright, S. D., Tobias, P. S., Ulevitch, R. J. & Ramos, R. A. Lipopolysaccharide (LPS) binding protein opsonizes LPS-bearing particles for recognition by a novel receptor on macrophages. J. Exp. Med. 170, 1231–1241 (1989).
  CAS PubMed Google Scholar
• Wright, S. D., Ramos, R. A., Tobias, P. S., Ulevitch, R. J. & Mathison, J. C. CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein. Science 249, 1431–1433 (1990).
  CAS PubMed Google Scholar
• Haziot, A. et al. Resistance to endotoxin shock and reduced dissemination of Gram-negative bacteria in CD14-deficient mice. Immunity 4, 407–414 (1996).
  CAS PubMed Google Scholar
• Shimazu, R. et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J. Exp. Med. 189, 1777–1782 (1999).
  CAS PubMed PubMed Central Google Scholar
• Schromm, A. B. et al. Molecular genetic analysis of an endotoxin nonresponder mutant cell line. A point mutation in a conserved region of md-2 abolishes endotoxin-induced signaling. J. Exp. Med. 194, 79–88 (2001).
  CAS PubMed PubMed Central Google Scholar
• Lien, E. et al. Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide. J. Clin. Invest. 105, 497–504 (2000).
  CAS PubMed PubMed Central Google Scholar
• Poltorak, A., Ricciardi-Castagnoli, P., Citterio, S. & Beutler, B. Physical contact between lipopolysaccharide and Toll-like receptor 4 revealed by genetic complementation. Proc. Natl Acad. Sci. USA 97, 2163–2167 (2000).
  CAS PubMed PubMed Central Google Scholar
• Da Silva Correia, J., Soldau, K., Christen, U., Tobias, P. S. & Ulevitch, R. J. Lipopolysaccharide is in close proximity to each of the proteins in its membrane receptor complex. Transfer from CD14 to TLR4 and MD-2. J. Biol. Chem. 276, 21129–21135 (2001).
  CAS PubMed Google Scholar
• Miyake, K., Yamashita, Y., Ogata, M., Sudo, T. & Kimoto, M. RP105, a novel B cell surface molecule implicated in B cell activation, is a member of the leucine-rich repeat protein family. J. Immunol. 154, 3333–3340 (1995).
  CAS PubMed Google Scholar
• Chan, V. W. et al. The molecular mechanism of B cell activation by Toll-like receptor protein RP-105. J. Exp. Med. 188, 93–101 (1998).
  CAS PubMed PubMed Central Google Scholar
• Miyake, K. et al. Mouse MD-1, a molecule that is physically associated with RP105 and positively regulates its expression. J. Immunol. 161, 1348–1353 (1998).
  CAS PubMed Google Scholar
• Ogata, H. et al. The Toll-like receptor protein RP105 regulates lipopolysaccharide signaling in B cells. J. Exp. Med. 192, 23–29 (2000).
  CAS PubMed PubMed Central Google Scholar
• Takeuchi, O. et al. Differential roles of TLR2 and TLR4 in recognition of Gram-negative and Gram-positive bacterial cel wall components. Immunity 11, 443–451 (1999).
  CAS PubMed Google Scholar
• Means, T. K. et al. Human Toll-like receptors mediate cellular activation by Mycobacterium tuberculosis. J. Immunol. 163, 3920–3927 (1999).
  CAS PubMed Google Scholar
• Ohashi, K., Burkart, V., Flohe, S. & Kolb, H. Cutting edge: heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex. J. Immunol. 164, 558–561 (2000).
  CAS PubMed Google Scholar
• Li, M. et al. An essential role of the NF-κB/Toll-like receptor pathway in induction of inflammatory and tissue-repair gene expression by necrotic cells. J. Immunol. 166, 7128–7135 (2001).
  CAS PubMed Google Scholar
• Kurt-Jones, E. A. et al. Pattern recognition receptors TLR4 and CD14 mediate response to respiratory syncytial virus. Nature Immunol. 1, 398–401 (2000).
  CAS Google Scholar
• Bowie, A. et al. A46R and A52R from vaccinia virus are antagonists of host IL-1 and Toll-like receptor signaling. Proc. Natl Acad. Sci. USA 97, 10162–10167 (2000).
  CAS PubMed PubMed Central Google Scholar
• Schwandner, R., Dziarski, R., Wesche, H., Rothe, M. & Kirschning, C. J. Peptidoglycan- and lipoteichoic acid-induced cell activation is mediated by Toll-like receptor 2. J. Biol. Chem. 274, 17406–17409 (1999).
  CAS PubMed Google Scholar
• Takeuchi, O. et al. Cutting edge: preferentially the R-stereoisomer of the mycoplasmal lipopeptide macrophage-activating lipopeptide-2 activates immune cells through a Toll-like receptor 2- and MyD88-dependent signaling pathway. J. Immunol. 164, 554–557 (2000).
  CAS PubMed Google Scholar
• Aliprantis, A. O. et al. Cell activation and apoptosis by bacterial lipoproteins through Toll-like receptor-2. Science 285, 736–739 (1999).
  CAS PubMed Google Scholar
• Brightbill, H. D. et al. Host defense mechanisms triggered by microbial lipoproteins through Toll-like receptors. Science 285, 732–736 (1999).
  CAS PubMed Google Scholar
• Means, T. K. et al. The CD14 ligands lipoarabinomannan and lipopolysaccharide differ in their requirement for Toll-like receptors. J. Immunol. 163, 6748–6755 (1999).
  CAS PubMed Google Scholar
• Underhill, D. M., Ozinsky, A., Smith, K. D. & Aderem, A. Toll-like receptor-2 mediates mycobacteria-induced proinflammatory signaling in macrophages. Proc. Natl Acad. Sci. USA 96, 14459–14463 (1999).
  CAS PubMed PubMed Central Google Scholar
• Campos, M. A. et al. Activation of Toll-like receptor-2 by glycosylphosphatidylinositol anchors from a protozoan parasite. J. Immunol. 167, 416–423 (2001).
  CAS PubMed Google Scholar
• Hajjar, A. M. et al. Cutting edge: functional interactions between Toll-like receptor (TLR) 2 and TLR1 or TLR6 in response to phenol-soluble modulin. J. Immunol. 166, 15–19 (2001).
  CAS PubMed Google Scholar
• Underhill, D. et al. The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens. Nature 401, 811–815 (1999).
  CAS PubMed Google Scholar
• Werts, C. et al. Leptospiral lipopolysaccharide activates cells through a TLR2-dependent mechanism. Nature Immunol. 2, 346–352 (2001).
  CAS Google Scholar
• Hirschfeld, M. et al. Signaling by Toll-like receptor 2 and 4 agonists results in differential gene expression in murine macrophages. Infect. Immun. 69, 1477–1482 (2001).
  CAS PubMed PubMed Central Google Scholar
• Ozinsky, A. et al. The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between Toll-like receptors. Proc. Natl Acad. Sci. USA 97, 13766–13771 (2000).
  CAS PubMed PubMed Central Google Scholar
• Takeuchi, O. et al. Discrimination of bacterial lipoproteins by Toll-like receptor 6. Int. Immunol. 13, 933–940 (2001).
  CAS PubMed Google Scholar
• Muzio, M. et al. Differential expression and regulation of Toll-like receptors (TLR) in human leukocytes: selective expression of TLR3 in dendritic cells. J. Immunol. 164, 5998–6004 (2000).
  CAS PubMed Google Scholar
• Alexopoulou, L., Holt, A. C., Medzhitov, R. & Flavell, R. A. Recognition of double stranded RNA and activation of NF-κB by Toll-like receptor 3. Nature 413, 732–738 (2001).
  CAS PubMed Google Scholar
• Williams, B. R. PKR; a sentinel kinase for cellular stress. Oncogene 18, 6112–6120 (1999).
  CAS PubMed Google Scholar
• Chu, W. M. et al. JNK2 and IKKβ are required for activating the innate response to viral infection. Immunity 11, 721–731 (1999).
  CAS PubMed Google Scholar
• Hayashi, F. et al. The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5. Nature 410, 1099–1103 (2001).
  CAS PubMed Google Scholar
• Samatey, F. A. et al. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature 410, 331–337 (2001).
  CAS PubMed Google Scholar
• Gewirtz, A. T., Navas, T. A., Lyons, S., Godowski, P. J. & Madara, J. L. Cutting edge: bacterial flagellin activates basolaterally expressed TLR5 to induce epithelial proinflammatory gene expression. J. Immunol. 167, 1882–1885 (2001).
  CAS PubMed Google Scholar
• Hemmi, H. et al. A Toll-like receptor recognizes bacterial DNA. Nature 408, 740–745 (2000).
  CAS PubMed Google Scholar
• Krieg, A. M. et al. CpG motifs in bacterial DNA trigger direct B-cell activation. Nature 374, 546–549 (1995).
  CAS PubMed Google Scholar
• Hacker, H. et al. CpG-DNA-specific activation of antigen-presenting cells requires stress kinase activity and is preceded by non-specific endocytosis and endosomal maturation. EMBO J. 17, 6230–6240 (1998).
  CAS PubMed PubMed Central Google Scholar
• Thieblemont, N. & Wright, S. D. Transport of bacterial lipopolysaccharide to the Golgi apparatus. J. Exp. Med. 190, 523–534 (1999).
  CAS PubMed PubMed Central Google Scholar
• Krieg, A. M. The role of CpG motifs in innate immunity. Curr. Opin. Immunol. 12, 35–43 (2000).
  CAS PubMed Google Scholar
• Bauer, S. et al. Human TLR9 confers responsiveness to bacterial DNA via species-specific CpG motif recognition. Proc. Natl Acad. Sci. USA 98, 9237–9242 (2001).
  CAS PubMed PubMed Central Google Scholar
• Thoma-Uszynski, S. et al. Induction of direct antimicrobial activity through mammalian Toll-like receptors. Science 291, 1544–1547 (2001).
  CAS PubMed Google Scholar
• Burns, K. et al. Tollip, a new component of the IL-1RI pathway, links IRAK to the IL-1 receptor. Nature Cell Biol. 2, 346–351 (2000).
  CAS PubMed Google Scholar
• Bulut, Y., Faure, E., Thomas, L., Equils, O. & Arditi, M. Cooperation of Toll-Like receptor 2 and 6 for cellular activation by soluble tuberculosis factor and Borrelia burgdorferi outer surface protein A lipoprotein: role of Toll-interacting protein and IL-1 receptor signaling molecules in Toll-like receptor 2 signaling. J. Immunol. 167, 987–994 (2001).
  CAS PubMed Google Scholar
• Cao, Z., Henzel, W. J. & Gao, X. IRAK: a kinase associated with the interleukin-1 receptor. Science 271, 1128–1131 (1996).
  CAS PubMed Google Scholar
• Cao, Z., Xiong, J., Takeuchi, M., Kurama, T. & Goeddel, D. V. TRAF6 is a signal transducer for interleukin-1. Nature 383, 443–446 (1996).
  CAS PubMed Google Scholar
• Lomaga, M. A. et al. TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40, and LPS signaling. Genes Dev. 13, 1015–1024 (1999).
  CAS PubMed PubMed Central Google Scholar
• Adachi, O. et al. Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-mediated function. Immunity 9, 143–150 (1998).
  CAS PubMed Google Scholar
• Kawai, T., Adachi, O., Ogawa, T., Takeda, K. & Akira, S. Unresponsiveness of MyD88-deficient mice to endotoxin. Immunity 11, 115–122 (1999).
  CAS PubMed Google Scholar
• Wang, C. et al. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412, 346–351 (2001).
  CAS PubMed Google Scholar
• Arbibe, L. et al. Toll-like receptor 2-mediated NF-κB activation requires a Rac1-dependent pathway. Nature Immunol. 1, 533–540 (2000).
  CAS Google Scholar
• Schnare, M., Holt, A. C., Takeda, K., Akira, S. & Medzhitov, R. Recognition of CpG DNA is mediated by signaling pathways dependent on the adaptor protein MyD88. Curr. Biol. 10, 1139–1142 (2000).
  CAS PubMed Google Scholar
• Kaisho, T., Takeuchi, O., Kawai, T., Hoshino, K. & Akira, S. Endotoxin-induced maturation of Myd88-deficient dendritic cells. J. Immunol. 166, 5688–5694 (2001).
  CAS PubMed Google Scholar
• Seki, E. et al. Lipopolysaccharide-induced IL-18 secretion from murine Kupffer cells independently of myeloid differentiation factor 88 that is critically involved in induction of production of IL-12 and IL-1β. J. Immunol. 166, 2651–2657 (2001).
  CAS PubMed Google Scholar
• Fitzgerald, K. A. et al. Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction. Nature 413, 78–83 (2001).
  CAS PubMed Google Scholar
• Goh, K. C., deVeer, M. J. & Williams, B. R. The protein kinase PKR is required for p38 MAPK activation and the innate immune response to bacterial endotoxin. EMBO J. 19, 4292–4297 (2000).
  CAS PubMed PubMed Central Google Scholar
• Banchereau, J. & Steinman, R. M. Dendritic cells and the control of immunity. Nature 392, 245–252 (1998).
  CAS PubMed Google Scholar
• Schnare, M. et al. Toll-like receptors control activation of adaptive immune responses. Nature Immunol. 2, 947–950 (2001).
  CAS Google Scholar
• Holmskov, U. L. Collectins and collectin receptors in innate immunity. APMIS Suppl. 100, 1–59 (2000).
  CAS PubMed Google Scholar
• Gewurz, H., Mold, C., Siegel, J. & Fiedel, B. C-reactive protein and the acute phase response. Adv. Intern. Med. 27, 345–372 (1982).
  CAS PubMed Google Scholar
• Schwalbe, R. A., Dahlback, B., Coe, J. E. & Nelsestuen, G. L. Pentraxin family of proteins interact specifically with phosphorylcholine and/or phosphorylethanolamine. Biochemistry 31, 4907–4915 (1992).
  CAS PubMed Google Scholar
• Fraser, I. P., Koziel, H. & Ezekowitz, R. A. The serum mannose-binding protein and the macrophage mannose receptor are pattern recognition molecules that link innate and adaptive immunity. Semin. Immunol. 10, 363–372 (1998).
  CAS PubMed Google Scholar
• Pearson, A. M. Scavenger receptors in innate immunity. Curr. Opin. Immunol. 8, 20–28 (1996).
  CAS PubMed Google Scholar
• Elomaa, O. et al. Cloning of a novel bacteria-binding receptor structurally related to scavenger receptors and expressed in a subset of macrophages. Cell 80, 603–609. (1995).
  CAS PubMed Google Scholar
• Inohara, N. et al. Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-κB. J. Biol. Chem. 274, 14560–14567 (1999).
  CAS PubMed Google Scholar
• Bertin, J. et al. Human CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-κB. J. Biol. Chem. 274, 12955–12958 (1999).
  CAS PubMed Google Scholar