메뉴 건너뛰기




Volumn 13, Issue 6, 2013, Pages 453-460

The history of Toll-like receptors-redefining innate immunity

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1 RECEPTOR; LIPOPOLYSACCHARIDE BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MYELOID DIFFERENTIATION FACTOR 88; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; PATTERN RECOGNITION RECEPTOR; PYROGEN; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 7; TOLL LIKE RECEPTOR 8; TOLL LIKE RECEPTOR 9; TOLL LIKE RECEPTOR ADAPTOR MOLECULE 2; TOLL LIKE RECEPTOR AGONIST;

EID: 84878232476     PISSN: 14741733     EISSN: 14741741     Source Type: Journal    
DOI: 10.1038/nri3446     Document Type: Review
Times cited : (1313)

References (118)
  • 1
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway, C. A. Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb. Symp. Quant. Biol. 54, 1-13 (1989).
    • (1989) Cold Spring Harb. Symp. Quant. Biol. , vol.54 , pp. 1-13
    • Janeway Jr., C.A.1
  • 2
    • 0025777448 scopus 로고
    • Interleukin-1 and interleukin-1 antagonism
    • Dinarello, C. A. Interleukin-1 and interleukin-1 antagonism. Blood 77, 1627-1652 (1991).
    • (1991) Blood , vol.77 , pp. 1627-1652
    • Dinarello, C.A.1
  • 3
    • 0023683844 scopus 로고
    • CDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily
    • Sims, J. E. et al. cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily. Science 241, 585-589 (1988).
    • (1988) Science , vol.241 , pp. 585-589
    • Sims, J.E.1
  • 4
    • 0025774776 scopus 로고
    • Drosophila Toll and IL-1 receptor
    • Gay, N. J. & Keith, F. J. Drosophila Toll and IL-1 receptor. Nature 351, 355-356 (1991).
    • (1991) Nature , vol.351 , pp. 355-356
    • Gay, N.J.1    Keith, F.J.2
  • 5
    • 0022230197 scopus 로고
    • Establishment of dorsal-ventral polarity in the Drosophila embryo: Genetic studies on the role of the Toll gene product
    • Anderson, K. V., Jurgens, G. & Nusslein-Volhard, C. Establishment of dorsal-ventral polarity in the Drosophila embryo: genetic studies on the role of the Toll gene product. Cell 42, 779-789 (1985).
    • (1985) Cell , vol.42 , pp. 779-789
    • Anderson, K.V.1    Jurgens, G.2    Nusslein-Volhard, C.3
  • 6
    • 0023619362 scopus 로고
    • Dorsal, an embryonic polarity gene in Drosophila, is homologous to the vertebrate proto-oncogene, c-rel
    • Steward, R. Dorsal, an embryonic polarity gene in Drosophila, is homologous to the vertebrate proto-oncogene, c-rel. Science 238, 692-694 (1987).
    • (1987) Science , vol.238 , pp. 692-694
    • Steward, R.1
  • 7
    • 0022930702 scopus 로고
    • Inducibility of κ immunoglobulin enhancer-binding protein Nf-κB by a posttranslational mechanism
    • Sen, R. & Baltimore, D. Inducibility of κ immunoglobulin enhancer-binding protein Nf-κB by a posttranslational mechanism. Cell 47, 921-928 (1986).
    • (1986) Cell , vol.47 , pp. 921-928
    • Sen, R.1    Baltimore, D.2
  • 8
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle, P. A. & Henkel, T. Function and activation of NF-κB in the immune system. Annu. Rev. Immunol. 12, 141-179 (1994).
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 9
    • 0026786698 scopus 로고
    • Amino acids conserved in interleukin-1 receptors (IL-1Rs) and the Drosophila toll protein are essential for IL-1R signal transduction
    • Heguy, A., Baldari, C. T., Macchia, G., Telford, J. L. & Melli, M. Amino acids conserved in interleukin-1 receptors (IL-1Rs) and the Drosophila toll protein are essential for IL-1R signal transduction. J. Biol. Chem. 267, 2605-2609 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 2605-2609
    • Heguy, A.1    Baldari, C.T.2    MacChia, G.3    Telford, J.L.4    Melli, M.5
  • 10
    • 0027931646 scopus 로고
    • The product of the tobacco mosaic virus resistance gene N: Similarity to toll and the interleukin-1 receptor
    • Whitham, S. et al. The product of the tobacco mosaic virus resistance gene N: similarity to toll and the interleukin-1 receptor. Cell 78, 1101-1115 (1994).
    • (1994) Cell , vol.78 , pp. 1101-1115
    • Whitham, S.1
  • 11
    • 0027443688 scopus 로고
    • Dif, a dorsal-related gene that mediates an immune response in Drosophila
    • Ip, Y. T. et al. Dif, a dorsal-related gene that mediates an immune response in Drosophila. Cell 75, 753-763 (1993).
    • (1993) Cell , vol.75 , pp. 753-763
    • Ip, Y.T.1
  • 12
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner, H., Hultmark, D., Engstrom, A., Bennich, H. & Boman, H. G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292, 246-248 (1981).
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 14
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • 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).
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.M.4    Hoffmann, J.A.5
  • 15
    • 0033711445 scopus 로고    scopus 로고
    • The Rel protein DIF mediates the antifungal but not the antibacterial host defense in Drosophila
    • Rutschmann, S. et al. The Rel protein DIF mediates the antifungal but not the antibacterial host defense in Drosophila. Immunity 12, 569-580 (2000).
    • (2000) Immunity , vol.12 , pp. 569-580
    • Rutschmann, S.1
  • 17
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • 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).
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 19
    • 0001575306 scopus 로고
    • Chemische erforschung von lipopolysacchariden gram-negativer bakterien
    • Westphal, O. & Luderitz, O. Chemische erforschung von lipopolysacchariden gram-negativer bakterien. Angew. Chemie 66, 407-417 (1954).
    • (1954) Angew. Chemie , vol.66 , pp. 407-417
    • Westphal, O.1    Luderitz, O.2
  • 20
    • 0020622348 scopus 로고
    • Characterization of lipopolysaccharide from a heptoseless mutant of Escherichia coli by carbon 13 nuclear magnetic resonance
    • Strain, S. M., Fesik, S. W. & Armitage, I. M. Characterization of lipopolysaccharide from a heptoseless mutant of Escherichia coli by carbon 13 nuclear magnetic resonance. J. Biol. Chem. 258, 2906-2910 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 2906-2910
    • Strain, S.M.1    Fesik, S.W.2    Armitage, I.M.3
  • 21
    • 0022462376 scopus 로고
    • Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum
    • Tobias, P. S., Soldau, K. & Ulevitch, R. J. Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum. J. Exp. Med. 164, 777-793 (1986).
    • (1986) J. Exp. Med. , vol.164 , pp. 777-793
    • Tobias, P.S.1    Soldau, K.2    Ulevitch, R.J.3
  • 22
    • 0027424403 scopus 로고
    • Endotoxin induces rapid protein tyrosine phosphorylation in 70Z/3 cells expressing CD14
    • Han, J., Lee, J. D., Tobias, P. S. & Ulevitch, R. J. Endotoxin induces rapid protein tyrosine phosphorylation in 70Z/3 cells expressing CD14. J. Biol. Chem. 268, 25009-25014 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 25009-25014
    • Han, J.1    Lee, J.D.2    Tobias, P.S.3    Ulevitch, R.J.4
  • 23
    • 0025874032 scopus 로고
    • Recognition and plasma clearance of endotoxin by scavenger receptors
    • Hampton, R. Y., Golenbock, D. T., Penman, M., Krieger, M. & Raetz, C. R. Recognition and plasma clearance of endotoxin by scavenger receptors. Nature 352, 342-344 (1991).
    • (1991) Nature , vol.352 , pp. 342-344
    • Hampton, R.Y.1    Golenbock, D.T.2    Penman, M.3    Krieger, M.4    Raetz, C.R.5
  • 24
    • 0025298591 scopus 로고
    • Identification of lipopolysaccharide-binding proteins in 70Z/3 cells by photoaffinity cross-linking
    • Kirkland, T. N. et al. Identification of lipopolysaccharide-binding proteins in 70Z/3 cells by photoaffinity cross-linking. J. Biol. Chem. 265, 9520-9525 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 9520-9525
    • Kirkland, T.N.1
  • 25
    • 0025166114 scopus 로고
    • CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein
    • 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).
    • (1990) Science , vol.249 , pp. 1431-1433
    • Wright, S.D.1    Ramos, R.A.2    Tobias, P.S.3    Ulevitch, R.J.4    Mathison, J.C.5
  • 26
    • 0025107568 scopus 로고
    • Structure and function of lipopolysaccharide binding protein
    • Schumann, R. R. et al. Structure and function of lipopolysaccharide binding protein. Science 249, 1429-1431 (1990).
    • (1990) Science , vol.249 , pp. 1429-1431
    • Schumann, R.R.1
  • 27
    • 0026463120 scopus 로고
    • Soluble CD14 participates in the response of cells to lipopolysaccharide
    • Frey, E. A. et al. Soluble CD14 participates in the response of cells to lipopolysaccharide. J. Exp. Med. 176, 1665-1671 (1992).
    • (1992) J. Exp. Med. , vol.176 , pp. 1665-1671
    • Frey, E.A.1
  • 28
    • 0027378381 scopus 로고
    • Glycosyl-phosphatidylinositol-anchored or integral membrane forms of CD14 mediate identical cellular responses to endotoxin
    • Lee, J. D. et al. Glycosyl-phosphatidylinositol-anchored or integral membrane forms of CD14 mediate identical cellular responses to endotoxin. Proc. Natl Acad. Sci. USA 90, 9930-9934 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9930-9934
    • Lee, J.D.1
  • 29
    • 0032541661 scopus 로고    scopus 로고
    • Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signalling
    • Yang, R. B. et al. Toll-like receptor-2 mediates lipopolysaccharide- induced cellular signalling. Nature 395, 284-288 (1998).
    • (1998) Nature , vol.395 , pp. 284-288
    • Yang, R.B.1
  • 30
    • 0034662239 scopus 로고    scopus 로고
    • Cutting edge: Repurification of lipopolysaccharide eliminates signaling through both human and murine toll-like receptor 2
    • Hirschfeld, M., Ma, Y., Weis, J. H., Vogel, S. N. & Weis, J. J. Cutting edge: repurification of lipopolysaccharide eliminates signaling through both human and murine toll-like receptor 2. J. Immunol. 165, 618-622 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 618-622
    • Hirschfeld, M.1    Ma, Y.2    Weis, J.H.3    Vogel, S.N.4    Weis, J.J.5
  • 31
    • 0032541638 scopus 로고    scopus 로고
    • Bacterial infection. for whom the bell tolls
    • Gerard, C. Bacterial infection. For whom the bell tolls. Nature 395, 217-219 (1998).
    • (1998) Nature , vol.395 , pp. 217-219
    • Gerard, C.1
  • 32
    • 0032509295 scopus 로고    scopus 로고
    • Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: Mutations in Tlr4 gene
    • Poltorak, A. et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 282, 2085-2088 (1998).
    • (1998) Science , vol.282 , pp. 2085-2088
    • Poltorak, A.1
  • 33
    • 0345561540 scopus 로고    scopus 로고
    • Endotoxin-tolerant mice have mutations in Toll-like receptor 4 (Tlr4)
    • Qureshi, S. T. et al. Endotoxin-tolerant mice have mutations in Toll-like receptor 4 (Tlr4). J. Exp. Med. 189, 615-625 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 615-625
    • Qureshi, S.T.1
  • 34
    • 0033120081 scopus 로고    scopus 로고
    • Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: Evidence for TLR4 as the Lps gene product
    • 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).
    • (1999) J. Immunol. , vol.162 , pp. 3749-3752
    • Hoshino, K.1
  • 35
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu, R. et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J. Exp. Med. 189, 1777-1782 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 1777-1782
    • Shimazu, R.1
  • 36
    • 0035796406 scopus 로고    scopus 로고
    • Molecular genetic analysis of an endotoxin nonresponder mutant cell line: A point mutation in a conserved region of MD-2 abolishes endotoxin-induced signaling
    • 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).
    • (2001) J. Exp. Med. , vol.194 , pp. 79-88
    • Schromm, A.B.1
  • 37
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • Park, B. S. et al. The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 458, 1191-1195 (2009).
    • (2009) Nature , vol.458 , pp. 1191-1195
    • Park, B.S.1
  • 38
    • 84860832650 scopus 로고    scopus 로고
    • Structural basis of species-specific endotoxin sensing by innate immune receptor TLR4/MD-2
    • Ohto, U., Fukase, K., Miyake, K. & Shimizu, T. Structural basis of species-specific endotoxin sensing by innate immune receptor TLR4/MD-2. Proc. Natl Acad. Sci. USA 109, 7421-7426 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 7421-7426
    • Ohto, U.1    Fukase, K.2    Miyake, K.3    Shimizu, T.4
  • 39
    • 63649108380 scopus 로고    scopus 로고
    • The roles of TLRs, RLRs and NLRs in pathogen recognition
    • Kawai, T. & Akira, S. The roles of TLRs, RLRs and NLRs in pathogen recognition. Int. Immunol. 21, 317-337 (2009).
    • (2009) Int. Immunol. , vol.21 , pp. 317-337
    • Kawai, T.1    Akira, S.2
  • 40
    • 0034922923 scopus 로고    scopus 로고
    • Discrimination of bacterial lipoproteins by Toll-like receptor 6
    • Takeuchi, O. et al. Discrimination of bacterial lipoproteins by Toll-like receptor 6. Int. Immunol. 13, 933-940 (2001).
    • (2001) Int. Immunol. , vol.13 , pp. 933-940
    • Takeuchi, O.1
  • 41
    • 0036644042 scopus 로고    scopus 로고
    • Cutting edge: Role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins
    • Takeuchi, O. et al. Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins. J. Immunol. 169, 10-14 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 10-14
    • Takeuchi, O.1
  • 42
    • 34548608447 scopus 로고    scopus 로고
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
    • Jin, M. S. et al. Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell 130, 1071-1082 (2007).
    • (2007) Cell , vol.130 , pp. 1071-1082
    • Jin, M.S.1
  • 43
    • 71749118913 scopus 로고    scopus 로고
    • Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer
    • Kang, J. Y. et al. Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer. Immunity 31, 873-884 (2009).
    • (2009) Immunity , vol.31 , pp. 873-884
    • Kang, J.Y.1
  • 44
    • 0034610291 scopus 로고    scopus 로고
    • The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between toll-like receptors
    • 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).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13766-13771
    • Ozinsky, A.1
  • 45
    • 0035953543 scopus 로고    scopus 로고
    • The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5
    • Hayashi, F. et al. The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5. Nature 410, 1099-1103 (2001).
    • (2001) Nature , vol.410 , pp. 1099-1103
    • Hayashi, F.1
  • 46
    • 33746161021 scopus 로고    scopus 로고
    • + lamina propria cells
    • + lamina propria cells. Nature Immunol. 7, 868-874 (2006).
    • (2006) Nature Immunol. , vol.7 , pp. 868-874
    • Uematsu, S.1
  • 47
    • 45549099429 scopus 로고    scopus 로고
    • Regulation of humoral and cellular gut immunity by lamina propria dendritic cells expressing Toll-like receptor 5
    • Uematsu, S. et al. Regulation of humoral and cellular gut immunity by lamina propria dendritic cells expressing Toll-like receptor 5. Nature Immunol. 9, 769-776 (2008).
    • (2008) Nature Immunol. , vol.9 , pp. 769-776
    • Uematsu, S.1
  • 48
    • 1542377424 scopus 로고    scopus 로고
    • A toll-like receptor that prevents infection by uropathogenic bacteria
    • Zhang, D. et al. A toll-like receptor that prevents infection by uropathogenic bacteria. Science 303, 1522-1526 (2004).
    • (2004) Science , vol.303 , pp. 1522-1526
    • Zhang, D.1
  • 49
    • 20644433342 scopus 로고    scopus 로고
    • TLR11 activation of dendritic cells by a protozoan profilin-like protein
    • Yarovinsky, F. et al. TLR11 activation of dendritic cells by a protozoan profilin-like protein. Science 308, 1626-1629 (2005).
    • (2005) Science , vol.308 , pp. 1626-1629
    • Yarovinsky, F.1
  • 50
    • 84872596639 scopus 로고    scopus 로고
    • Combined action of nucleic acid-sensing Toll-like receptors and TLR11/TLR12 heterodimers imparts resistance to Toxoplasma gondii in mice
    • Andrade, W. A. et al. Combined action of nucleic acid-sensing Toll-like receptors and TLR11/TLR12 heterodimers imparts resistance to Toxoplasma gondii in mice. Cell Host Microbe 13, 42-53 (2013).
    • (2013) Cell Host Microbe , vol.13 , pp. 42-53
    • Andrade, W.A.1
  • 51
    • 84872761427 scopus 로고    scopus 로고
    • Recognition of profilin by Toll-like receptor 12 is critical for host resistance to Toxoplasma gondii
    • Koblansky, A. A. et al. Recognition of profilin by Toll-like receptor 12 is critical for host resistance to Toxoplasma gondii. Immunity 38, 119-130 (2013).
    • (2013) Immunity , vol.38 , pp. 119-130
    • Koblansky, A.A.1
  • 52
    • 84865571191 scopus 로고    scopus 로고
    • TLR13 recognizes bacterial 23S rRNA devoid of erythromycin resistance-forming modification
    • Oldenburg, M. et al. TLR13 recognizes bacterial 23S rRNA devoid of erythromycin resistance-forming modification. Science 337, 1111-1115 (2012).
    • (2012) Science , vol.337 , pp. 1111-1115
    • Oldenburg, M.1
  • 53
    • 84877579519 scopus 로고    scopus 로고
    • Sequence specific detection of bacterial 23S ribosomal RNA by TLR13
    • Li, X. D. & Chen, Z. J. Sequence specific detection of bacterial 23S ribosomal RNA by TLR13. eLife 1, e00102 (2012).
    • (2012) ELife , vol.1
    • Li, X.D.1    Chen, Z.J.2
  • 54
    • 84866159316 scopus 로고    scopus 로고
    • Cutting edge: TLR13 is a receptor for bacterial RNA
    • Hidmark, A., von Saint Paul, A. & Dalpke, A. H. Cutting edge: TLR13 is a receptor for bacterial RNA. J. Immunol. 189, 2717-2721 (2012).
    • (2012) J. Immunol. , vol.189 , pp. 2717-2721
    • Hidmark, A.1    Von Saint Paul, A.2    Dalpke, A.H.3
  • 55
    • 0034730146 scopus 로고    scopus 로고
    • A46R and A52R from vaccinia virus are antagonists of host IL-1 and toll-like receptor signaling
    • 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).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10162-10167
    • Bowie, A.1
  • 56
    • 5944261457 scopus 로고    scopus 로고
    • Pattern recognition receptors TLR4 and CD14 mediate response to respiratory syncytial virus
    • Kurt-Jones, E. A. et al. Pattern recognition receptors TLR4 and CD14 mediate response to respiratory syncytial virus. Nature Immunol. 1, 398-401 (2000).
    • (2000) Nature Immunol. , vol.1 , pp. 398-401
    • Kurt-Jones, E.A.1
  • 57
    • 0035909372 scopus 로고    scopus 로고
    • 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. Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3. Nature 413, 732-738 (2001).
    • (2001) Nature , vol.413 , pp. 732-738
    • Alexopoulou, L.1    Holt, A.C.2    Medzhitov, R.3    Flavell, R.A.4
  • 58
    • 42349090335 scopus 로고    scopus 로고
    • Structural basis of toll-like receptor 3 signaling with double-stranded RNA
    • Liu, L. et al. Structural basis of toll-like receptor 3 signaling with double-stranded RNA. Science 320, 379-381 (2008).
    • (2008) Science , vol.320 , pp. 379-381
    • Liu, L.1
  • 59
    • 48749128643 scopus 로고    scopus 로고
    • Structures of the toll-like receptor family and its ligand complexes
    • Jin, M. S. & Lee, J. O. Structures of the toll-like receptor family and its ligand complexes. Immunity 29, 182-191 (2008).
    • (2008) Immunity , vol.29 , pp. 182-191
    • Jin, M.S.1    Lee, J.O.2
  • 60
    • 84857335818 scopus 로고    scopus 로고
    • Structural basis of TLR5-flagellin recognition and signaling
    • Yoon, S. I. et al. Structural basis of TLR5-flagellin recognition and signaling. Science 335, 859-864 (2012).
    • (2012) Science , vol.335 , pp. 859-864
    • Yoon, S.I.1
  • 61
    • 0034619794 scopus 로고    scopus 로고
    • A Toll-like receptor recognizes bacterial DNA
    • Hemmi, H. et al. A Toll-like receptor recognizes bacterial DNA. Nature 408, 740-745 (2000).
    • (2000) Nature , vol.408 , pp. 740-745
    • Hemmi, H.1
  • 62
    • 0042123694 scopus 로고    scopus 로고
    • Toll-like receptor 9-mediated recognition of Herpes simplex virus-2 by plasmacytoid dendritic cells
    • Lund, J., Sato, A., Akira, S., Medzhitov, R. & Iwasaki, A. Toll-like receptor 9-mediated recognition of Herpes simplex virus-2 by plasmacytoid dendritic cells. J. Exp. Med. 198, 513-520 (2003).
    • (2003) J. Exp. Med. , vol.198 , pp. 513-520
    • Lund, J.1    Sato, A.2    Akira, S.3    Medzhitov, R.4    Iwasaki, A.5
  • 63
    • 3142683548 scopus 로고    scopus 로고
    • TLR9-dependent recognition of MCMV by IPC and DC generates coordinated cytokine responses that activate antiviral NK cell function
    • Krug, A. et al. TLR9-dependent recognition of MCMV by IPC and DC generates coordinated cytokine responses that activate antiviral NK cell function. Immunity 21, 107-119 (2004).
    • (2004) Immunity , vol.21 , pp. 107-119
    • Krug, A.1
  • 64
    • 0842328805 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 activates murine natural interferon-producing cells through tolllike receptor 9
    • Krug, A. et al. Herpes simplex virus type 1 activates murine natural interferon-producing cells through tolllike receptor 9. Blood 103, 1433-1437 (2004).
    • (2004) Blood , vol.103 , pp. 1433-1437
    • Krug, A.1
  • 65
    • 0036008014 scopus 로고    scopus 로고
    • Small anti-viral compounds activate immune cells via the TLR7 MyD88-dependent signaling pathway
    • Hemmi, H. et al. Small anti-viral compounds activate immune cells via the TLR7 MyD88-dependent signaling pathway. Nature Immunol. 3, 196-200 (2002).
    • (2002) Nature Immunol. , vol.3 , pp. 196-200
    • Hemmi, H.1
  • 66
    • 1542317578 scopus 로고    scopus 로고
    • Species-specific recognition of single-stranded RNA via Toll-like receptor 7 and 8
    • Heil, F. et al. Species-specific recognition of single-stranded RNA via Toll-like receptor 7 and 8. Science 303, 1526-1529 (2004).
    • (2004) Science , vol.303 , pp. 1526-1529
    • Heil, F.1
  • 67
    • 1542317550 scopus 로고    scopus 로고
    • 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. Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA. Science 303, 1529-1531 (2004).
    • (2004) Science , vol.303 , pp. 1529-1531
    • Diebold, S.S.1    Kaisho, T.2    Hemmi, H.3    Akira, S.4    Reis Sousae, C.5
  • 68
    • 1842631428 scopus 로고    scopus 로고
    • Recognition of single-stranded RNA viruses by Toll-like receptor 7
    • Lund, J. M. et al. Recognition of single-stranded RNA viruses by Toll-like receptor 7. Proc. Natl Acad. Sci. USA 101, 5598-5603 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 5598-5603
    • Lund, J.M.1
  • 69
    • 0037061453 scopus 로고    scopus 로고
    • Chromatin-IgG complexes activate B cells by dual engagement of IgM and Toll-like receptors
    • Leadbetter, E. A. et al. Chromatin-IgG complexes activate B cells by dual engagement of IgM and Toll-like receptors. Nature 416, 603-607 (2002).
    • (2002) Nature , vol.416 , pp. 603-607
    • Leadbetter, E.A.1
  • 70
    • 85047693371 scopus 로고    scopus 로고
    • Human lupus autoantibody-DNA complexes activate DCs through cooperation of CD32 and TLR9
    • Means, T. K. et al. Human lupus autoantibody-DNA complexes activate DCs through cooperation of CD32 and TLR9. J. Clin. Invest. 115, 407-417 (2005).
    • (2005) J. Clin. Invest. , vol.115 , pp. 407-417
    • Means, T.K.1
  • 71
    • 28544449709 scopus 로고    scopus 로고
    • Immune stimulation mediated by autoantigen binding sites within small nuclear RNAs involves Toll-like receptors 7 and 8
    • Vollmer, J. et al. Immune stimulation mediated by autoantigen binding sites within small nuclear RNAs involves Toll-like receptors 7 and 8. J. Exp. Med. 202, 1575-1585 (2005).
    • (2005) J. Exp. Med. , vol.202 , pp. 1575-1585
    • Vollmer, J.1
  • 72
    • 27744444832 scopus 로고    scopus 로고
    • RNA-associated autoantigens activate B cells by combined B cell antigen receptor/Toll-like receptor 7 engagement
    • Lau, C. M. et al. RNA-associated autoantigens activate B cells by combined B cell antigen receptor/Toll-like receptor 7 engagement. J. Exp. Med. 202, 1171-1177 (2005).
    • (2005) J. Exp. Med. , vol.202 , pp. 1171-1177
    • Lau, C.M.1
  • 73
    • 0031423761 scopus 로고    scopus 로고
    • MyD88: An adapter that recruits IRAK to the IL-1 receptor complex
    • 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).
    • (1997) Immunity , vol.7 , pp. 837-847
    • Wesche, H.1    Henzel, W.J.2    Shillinglaw, W.3    Li, S.4    Cao, Z.5
  • 74
    • 0030694108 scopus 로고    scopus 로고
    • IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling
    • 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).
    • (1997) Science , vol.278 , pp. 1612-1615
    • Muzio, M.1    Ni, J.2    Feng, P.3    Dixit, V.M.4
  • 75
    • 78049431237 scopus 로고    scopus 로고
    • The interleukin-1 receptor-associated kinases: Critical regulators of innate immune signalling
    • Flannery, S. & Bowie, A. G. The interleukin-1 receptor-associated kinases: critical regulators of innate immune signalling. Biochem. Pharmacol. 80, 1981-1991 (2010).
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 1981-1991
    • Flannery, S.1    Bowie, A.G.2
  • 76
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling
    • O'Neill, L. A. & Bowie, A. G. The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. Nature Rev. Immunol. 7, 353-364 (2007).
    • (2007) Nature Rev. Immunol. , vol.7 , pp. 353-364
    • O'Neill, L.A.1    Bowie, A.G.2
  • 77
    • 0036318851 scopus 로고    scopus 로고
    • Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments
    • Ahmad-Nejad, P. et al. Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments. Eur. J. Immunol. 32, 1958-1968 (2002).
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1958-1968
    • Ahmad-Nejad, P.1
  • 78
    • 2442565738 scopus 로고    scopus 로고
    • Ligand-regulated chimeric receptor approach reveals distinctive subcellular localization and signaling properties of the Toll-like receptors
    • Nishiya, T. & DeFranco, A. L. Ligand-regulated chimeric receptor approach reveals distinctive subcellular localization and signaling properties of the Toll-like receptors. J. Biol. Chem. 279, 19008-19017 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 19008-19017
    • Nishiya, T.1    Defranco, A.L.2
  • 79
    • 10744219675 scopus 로고    scopus 로고
    • TLR9 signals after translocating from the ER to CpG DNA in the lysosome
    • Latz, E. et al. TLR9 signals after translocating from the ER to CpG DNA in the lysosome. Nature Immunol. 5, 190-198 (2004).
    • (2004) Nature Immunol. , vol.5 , pp. 190-198
    • Latz, E.1
  • 80
    • 5444274514 scopus 로고    scopus 로고
    • Interferon-α induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6
    • Kawai, T. et al. Interferon-α induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6. Nature Immunol. 5, 1061-1068 (2004).
    • (2004) Nature Immunol. , vol.5 , pp. 1061-1068
    • Kawai, T.1
  • 81
    • 17844380477 scopus 로고    scopus 로고
    • Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction
    • Honda, K. et al. Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction. Nature 434, 1035-1040 (2005).
    • (2005) Nature , vol.434 , pp. 1035-1040
    • Honda, K.1
  • 82
    • 0035817925 scopus 로고    scopus 로고
    • Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction
    • Fitzgerald, K. A. et al. Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction. Nature 413, 78-83 (2001).
    • (2001) Nature , vol.413 , pp. 78-83
    • Fitzgerald, K.A.1
  • 83
    • 0035555301 scopus 로고    scopus 로고
    • TIRAP: An adapter molecule in the Toll signaling pathway
    • Horng, T., Barton, G. M. & Medzhitov, R. TIRAP: an adapter molecule in the Toll signaling pathway. Nature Immunol. 2, 835-841 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 835-841
    • Horng, T.1    Barton, G.M.2    Medzhitov, R.3
  • 84
    • 0033166472 scopus 로고    scopus 로고
    • Unresponsiveness of MyD88-deficient mice to endotoxin
    • Kawai, T., Adachi, O., Ogawa, T., Takeda, K. & Akira, S. Unresponsiveness of MyD88-deficient mice to endotoxin. Immunity 11, 115-122 (1999).
    • (1999) Immunity , vol.11 , pp. 115-122
    • Kawai, T.1    Adachi, O.2    Ogawa, T.3    Takeda, K.4    Akira, S.5
  • 85
    • 0035889228 scopus 로고    scopus 로고
    • Lipopolysaccharide stimulates the MyD88-independent pathway and results in activation of IFN-regulatory factor 3 and the expression of a subset of lipopolysaccharide-inducible genes
    • Kawai, T. et al. Lipopolysaccharide stimulates the MyD88-independent pathway and results in activation of IFN-regulatory factor 3 and the expression of a subset of lipopolysaccharide-inducible genes. J. Immunol. 167, 5887-5894 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 5887-5894
    • Kawai, T.1
  • 86
    • 0035339861 scopus 로고    scopus 로고
    • Endotoxin-induced maturation of MyD88-deficient dendritic cells
    • Kaisho, T., Takeuchi, O., Kawai, T., Hoshino, K. & Akira, S. Endotoxin-induced maturation of MyD88-deficient dendritic cells. J. Immunol. 166, 5688-5694 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 5688-5694
    • Kaisho, T.1    Takeuchi, O.2    Kawai, T.3    Hoshino, K.4    Akira, S.5
  • 87
    • 0037153130 scopus 로고    scopus 로고
    • The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors
    • Horng, T., Barton, G. M., Flavell, R. A. & Medzhitov, R. The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors. Nature 420, 329-333 (2002).
    • (2002) Nature , vol.420 , pp. 329-333
    • Horng, T.1    Barton, G.M.2    Flavell, R.A.3    Medzhitov, R.4
  • 88
    • 0037153191 scopus 로고    scopus 로고
    • Essential role for TIRAP in activation of the signalling cascade shared by TLR2 and TLR4
    • Yamamoto, M. et al. Essential role for TIRAP in activation of the signalling cascade shared by TLR2 and TLR4. Nature 420, 324-329 (2002).
    • (2002) Nature , vol.420 , pp. 324-329
    • Yamamoto, M.1
  • 89
    • 33646908228 scopus 로고    scopus 로고
    • Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling
    • Kagan, J. C. & Medzhitov, R. Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling. Cell 125, 943-955 (2006).
    • (2006) Cell , vol.125 , pp. 943-955
    • Kagan, J.C.1    Medzhitov, R.2
  • 90
    • 70349324347 scopus 로고    scopus 로고
    • MyD88 adaptor-like is not essential for TLR2 signaling and inhibits signaling by TLR3
    • Kenny, E. F. et al. MyD88 adaptor-like is not essential for TLR2 signaling and inhibits signaling by TLR3. J. Immunol. 183, 3642-3651 (2009).
    • (2009) J. Immunol. , vol.183 , pp. 3642-3651
    • Kenny, E.F.1
  • 91
    • 0037114185 scopus 로고    scopus 로고
    • Cutting edge: A novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-β promoter in the Toll-like receptor signaling
    • Yamamoto, M. et al. Cutting edge: a novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-β promoter in the Toll-like receptor signaling. J. Immunol. 169, 6668-6672 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 6668-6672
    • Yamamoto, M.1
  • 92
    • 0037320451 scopus 로고    scopus 로고
    • TICAM-1 an adaptor molecule that participates in Toll-like receptor 3-mediated interferon-β induction
    • Oshiumi, H., Matsumoto, M., Funami, K., Akazawa, T. & Seya, T. TICAM-1, an adaptor molecule that participates in Toll-like receptor 3-mediated interferon-β induction. Nature Immunol. 4, 161-167 (2003).
    • (2003) Nature Immunol. , vol.4 , pp. 161-167
    • Oshiumi, H.1    Matsumoto, M.2    Funami, K.3    Akazawa, T.4    Seya, T.5
  • 93
    • 0042679529 scopus 로고    scopus 로고
    • Identification of Lps2 as a key transducer of MyD88-independent TIR signalling
    • Hoebe, K. et al. Identification of Lps2 as a key transducer of MyD88-independent TIR signalling. Nature 424, 743-748 (2003).
    • (2003) Nature , vol.424 , pp. 743-748
    • Hoebe, K.1
  • 94
    • 0043176281 scopus 로고    scopus 로고
    • Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway
    • Yamamoto, M. et al. Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway. Science 301, 640-643 (2003).
    • (2003) Science , vol.301 , pp. 640-643
    • Yamamoto, M.1
  • 95
    • 0141959224 scopus 로고    scopus 로고
    • LPS-TLR4 signaling to IRF-3/7 and NF-κB involves the toll adapters TRAM and TRIF
    • Fitzgerald, K. A. et al. LPS-TLR4 signaling to IRF-3/7 and NF-κB involves the toll adapters TRAM and TRIF. J. Exp. Med. 198, 1043-1055 (2003).
    • (2003) J. Exp. Med. , vol.198 , pp. 1043-1055
    • Fitzgerald, K.A.1
  • 96
    • 0242624622 scopus 로고    scopus 로고
    • TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway
    • Yamamoto, M. et al. TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway. Nature Immunol. 4, 1144-1150 (2003).
    • (2003) Nature Immunol. , vol.4 , pp. 1144-1150
    • Yamamoto, M.1
  • 97
    • 0345991221 scopus 로고    scopus 로고
    • TIR-containing adapter molecule (TICAM)-2, a bridging adapter recruiting to toll-like receptor 4 TICAM-1 that induces interferon-β
    • Oshiumi, H. et al. TIR-containing adapter molecule (TICAM)-2, a bridging adapter recruiting to toll-like receptor 4 TICAM-1 that induces interferon-β. J. Biol. Chem. 278, 49751-49762 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 49751-49762
    • Oshiumi, H.1
  • 98
    • 33748871187 scopus 로고    scopus 로고
    • The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling
    • Carty, M. et al. The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling. Nature Immunol. 7, 1074-1081 (2006).
    • (2006) Nature Immunol. , vol.7 , pp. 1074-1081
    • Carty, M.1
  • 99
    • 84864332905 scopus 로고    scopus 로고
    • DSarm/Sarm1 is required for activation of an injury-induced axon death pathway
    • Osterloh, J. M. et al. dSarm/Sarm1 is required for activation of an injury-induced axon death pathway. Science 337, 481-484 (2012).
    • (2012) Science , vol.337 , pp. 481-484
    • Osterloh, J.M.1
  • 100
    • 84856008042 scopus 로고    scopus 로고
    • Role for B-cell adapter for PI3K (BCAP) as a signaling adapter linking Toll-like receptors (TLRs) to serine/threonine kinases PI3K/Akt
    • Troutman, T. D. et al. Role for B-cell adapter for PI3K (BCAP) as a signaling adapter linking Toll-like receptors (TLRs) to serine/threonine kinases PI3K/Akt. Proc. Natl Acad. Sci. USA 109, 273-278 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 273-278
    • Troutman, T.D.1
  • 101
    • 84855992592 scopus 로고    scopus 로고
    • B-cell adaptor for PI3K (BCAP) negatively regulates Toll-like receptor signaling through activation of PI3K
    • Ni, M. et al. B-cell adaptor for PI3K (BCAP) negatively regulates Toll-like receptor signaling through activation of PI3K. Proc. Natl Acad. Sci. USA 109, 267-272 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 267-272
    • Ni, M.1
  • 102
    • 67649422321 scopus 로고    scopus 로고
    • Therapeutic targeting of Toll-like receptors for infectious and inflammatory diseases and cancer
    • O'Neill, L. A., Bryant, C. E. & Doyle, S. L. Therapeutic targeting of Toll-like receptors for infectious and inflammatory diseases and cancer. Pharmacol. Rev. 61, 177-197 (2009).
    • (2009) Pharmacol. Rev. , vol.61 , pp. 177-197
    • O'Neill, L.A.1    Bryant, C.E.2    Doyle, S.L.3
  • 103
    • 27844541797 scopus 로고    scopus 로고
    • Control of B-cell responses by Toll-like receptors
    • Pasare, C. & Medzhitov, R. Control of B-cell responses by Toll-like receptors. Nature 438, 364-368 (2005).
    • (2005) Nature , vol.438 , pp. 364-368
    • Pasare, C.1    Medzhitov, R.2
  • 104
    • 0036789814 scopus 로고    scopus 로고
    • Taking toll: Lipid A mimetics as adjuvants and immunomodulators
    • Persing, D. H. et al. Taking toll: lipid A mimetics as adjuvants and immunomodulators. Trends Microbiol. 10, S32-S37 (2002).
    • (2002) Trends Microbiol. , vol.10
    • Persing, D.H.1
  • 105
    • 0034123135 scopus 로고    scopus 로고
    • Differential expression and regulation of toll-like receptors (TLR) in human leukocytes: Selective expression of TLR3 in dendritic cells
    • 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).
    • (2000) J. Immunol. , vol.164 , pp. 5998-6004
    • Muzio, M.1
  • 106
    • 0034443265 scopus 로고    scopus 로고
    • Maturation of human dendritic cells by cell wall skeleton of Mycobacterium bovis bacillus Calmette-Guérin: Involvement of toll-like receptors
    • Tsuji, S. et al. Maturation of human dendritic cells by cell wall skeleton of Mycobacterium bovis bacillus Calmette-Guérin: involvement of toll-like receptors. Infect. Immun. 68, 6883-6890 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 6883-6890
    • Tsuji, S.1
  • 107
    • 0035865232 scopus 로고    scopus 로고
    • Microbial lipopeptides stimulate dendritic cell maturation via Toll-like receptor 2
    • Hertz, C. J. et al. Microbial lipopeptides stimulate dendritic cell maturation via Toll-like receptor 2. J. Immunol. 166, 2444-2450 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 2444-2450
    • Hertz, C.J.1
  • 108
    • 0347146027 scopus 로고    scopus 로고
    • Upregulation of costimulatory molecules induced by lipopolysaccharide and double-stranded RNA occurs by Trif-dependent and Trif-independent pathways
    • Hoebe, K. et al. Upregulation of costimulatory molecules induced by lipopolysaccharide and double-stranded RNA occurs by Trif-dependent and Trif-independent pathways. Nature Immunol. 4, 1223-1229 (2003).
    • (2003) Nature Immunol. , vol.4 , pp. 1223-1229
    • Hoebe, K.1
  • 109
    • 33846456617 scopus 로고    scopus 로고
    • A phase II, double-blind, placebo-controlled, ascending-dose study of Eritoran (E5564), a lipid A antagonist, in patients undergoing cardiac surgery with cardiopulmonary bypass
    • Bennett-Guerrero, E. et al. A phase II, double-blind, placebo-controlled, ascending-dose study of Eritoran (E5564), a lipid A antagonist, in patients undergoing cardiac surgery with cardiopulmonary bypass. Anesth. Analg. 104, 378-383 (2007).
    • (2007) Anesth. Analg. , vol.104 , pp. 378-383
    • Bennett-Guerrero, E.1
  • 110
    • 80052968260 scopus 로고    scopus 로고
    • Influence of severity of illness on the effects of eritoran tetrasodium (E5564) and on other therapies for severe sepsis
    • Kalil, A. C., LaRosa, S. P., Gogate, J., Lynn, M. & Opal, S. M. Influence of severity of illness on the effects of eritoran tetrasodium (E5564) and on other therapies for severe sepsis. Shock 36, 327-331 (2011).
    • (2011) Shock , vol.36 , pp. 327-331
    • Kalil, A.C.1    Larosa, S.P.2    Gogate, J.3    Lynn, M.4    Opal, S.M.5
  • 111
    • 77953723966 scopus 로고    scopus 로고
    • TLR recognition of self nucleic acids hampers glucocorticoid activity in lupus
    • Guiducci, C. et al. TLR recognition of self nucleic acids hampers glucocorticoid activity in lupus. Nature 465, 937-941 (2010).
    • (2010) Nature , vol.465 , pp. 937-941
    • Guiducci, C.1
  • 112
    • 84860789456 scopus 로고    scopus 로고
    • Treatment with OPN-305, a humanized anti-Toll-Like receptor-2 antibody, reduces myocardial ischemia/reperfusion injury in pigs
    • Arslan, F. et al. Treatment with OPN-305, a humanized anti-Toll-Like receptor-2 antibody, reduces myocardial ischemia/reperfusion injury in pigs. Circ. Cardiovasc. Interv. 5, 279-287 (2012).
    • (2012) Circ. Cardiovasc. Interv. , vol.5 , pp. 279-287
    • Arslan, F.1
  • 113
    • 84856521251 scopus 로고    scopus 로고
    • Inhibition of TLR2 promotes graft function in a murine model of renal transplant ischemia-reperfusion injury
    • Farrar, C. A. et al. Inhibition of TLR2 promotes graft function in a murine model of renal transplant ischemia-reperfusion injury. FASEB J. 26, 799-807 (2012).
    • (2012) FASEB J. , vol.26 , pp. 799-807
    • Farrar, C.A.1
  • 114
    • 84862068459 scopus 로고    scopus 로고
    • Genetic variation in Toll-like receptors and disease susceptibility
    • Netea, M. G., Wijmenga, C. & O'Neill, L. A. Genetic variation in Toll-like receptors and disease susceptibility. Nature Immunol. 13, 535-542 (2012).
    • (2012) Nature Immunol. , vol.13 , pp. 535-542
    • Netea, M.G.1    Wijmenga, C.2    O'Neill, L.A.3
  • 115
    • 34548699323 scopus 로고    scopus 로고
    • TLR3 deficiency in patients with herpes simplex encephalitis
    • Zhang, S. Y. et al. TLR3 deficiency in patients with herpes simplex encephalitis. Science 317, 1522-1527 (2007).
    • (2007) Science , vol.317 , pp. 1522-1527
    • Zhang, S.Y.1
  • 116
    • 48749109290 scopus 로고    scopus 로고
    • Pyogenic bacterial infections in humans with MyD88 deficiency
    • von Bernuth, H. et al. Pyogenic bacterial infections in humans with MyD88 deficiency. Science 321, 691-696 (2008).
    • (2008) Science , vol.321 , pp. 691-696
    • Von Bernuth, H.1
  • 117
    • 34948904198 scopus 로고    scopus 로고
    • Selective predisposition to bacterial infections in IRAK-4-deficient children: IRAK-4-dependent TLRs are otherwise redundant in protective immunity
    • Ku, C. L. et al. Selective predisposition to bacterial infections in IRAK-4-deficient children: IRAK-4-dependent TLRs are otherwise redundant in protective immunity. J. Exp. Med. 204, 2407-2422 (2007).
    • (2007) J. Exp. Med. , vol.204 , pp. 2407-2422
    • Ku, C.L.1
  • 118
    • 79551686422 scopus 로고    scopus 로고
    • Oncogenically active MYD88 mutations in human lymphoma
    • Ngo, V. N. et al. Oncogenically active MYD88 mutations in human lymphoma. Nature 470, 115-119 (2011).
    • (2011) Nature , vol.470 , pp. 115-119
    • Ngo, V.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.