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Volumn 430, Issue 6996, 2004, Pages 257-263

Inferences, questions and possibilities in Toll-like receptor signalling

Author keywords

[No Author keywords available]

Indexed keywords

DRUG PRODUCTS; MICROORGANISMS; PROTEINS; STERILIZATION (CLEANING);

EID: 3142654210     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02761     Document Type: Review
Times cited : (1334)

References (85)
  • 1
    • 0022189558 scopus 로고
    • Establishment of dorsal-ventral polarity in the Drosophila embryo: The induction of polarity by the Toll gene product
    • Anderson, K. V., Bokla, L. & Nusslein-Volhard, C. Establishment of dorsal-ventral polarity in the Drosophila embryo: the induction of polarity by the Toll gene product. Cell 42, 791-798 (1985).
    • (1985) Cell , vol.42 , pp. 791-798
    • Anderson, K.V.1    Bokla, L.2    Nusslein-Volhard, C.3
  • 2
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spatzle/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 spatzle/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
  • 3
    • 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
  • 4
    • 12144286763 scopus 로고    scopus 로고
    • TLR9 and TLR3 as essential components of innate immune defense against mouse cytomegalovirus
    • Tabeta, K. et al. TLR9 and TLR3 as essential components of innate immune defense against mouse cytomegalovirus. Proc. Natl Acad. Sci. USA 101, 3516-3521 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3516-3521
    • Tabeta, K.1
  • 5
    • 3142578451 scopus 로고    scopus 로고
    • Forward genetic dissection of afferent immunity: The role of TIR adapter proteins in innate and adaptive immune responses
    • in the press
    • Beutler, B., Hoebe, K., Georgel, P., Tabeta, K. & Du, X. Forward genetic dissection of afferent immunity: the role of TIR adapter proteins in innate and adaptive immune responses. Adv. Exp. Med. Biol. (in the press).
    • Adv. Exp. Med. Biol.
    • Beutler, B.1    Hoebe, K.2    Georgel, P.3    Tabeta, K.4    Du, X.5
  • 6
    • 0034886143 scopus 로고    scopus 로고
    • Toll-like receptors: Critical proteins linking innate and acquired immunity
    • Akira, S., Takeda, K. & Kaisho, T. Toll-like receptors: critical proteins linking innate and acquired immunity. Nature Immunol. 2, 675-680 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 675-680
    • Akira, S.1    Takeda, K.2    Kaisho, T.3
  • 7
    • 0035399862 scopus 로고    scopus 로고
    • Activation of Toll-like receptor-2 by glycosylphosphatidylinositol anchors from a protozoan parasite
    • Campos, M. A. et al. Activation of Toll-like receptor-2 by glycosylphosphatidylinositol anchors from a protozoan parasite. J. Immunol. 167, 416-423 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 416-423
    • Campos, M.A.1
  • 8
    • 1642525756 scopus 로고    scopus 로고
    • Impaired production of proinflammatory cytokines and host resistance to acute infection with Trypanosoma cruzi in mice lacking functional myeloid differentiation factor 88
    • Campos, M. A. et al. Impaired production of proinflammatory cytokines and host resistance to acute infection with Trypanosoma cruzi in mice lacking functional myeloid differentiation factor 88. J. Immunol. 172, 1711-1718 (2004).
    • (2004) J. Immunol. , vol.172 , pp. 1711-1718
    • Campos, M.A.1
  • 9
    • 0033592748 scopus 로고    scopus 로고
    • The Toll-like receptor 2 is recruited to macrophage phagosome and discriminates between pathogens
    • Underhill, D. M. et al. The Toll-like receptor 2 is recruited to macrophage phagosome and discriminates between pathogens. Nature 401, 811-815 (1999).
    • (1999) Nature , vol.401 , pp. 811-815
    • Underhill, D.M.1
  • 10
    • 0033213590 scopus 로고    scopus 로고
    • Differential roles of TLR2 and TLR4 in recognition of gram-negative and Gram-positive bacterial cell wall components
    • Takeuchi, O. et al. Differential roles of TLR2 and TLR4 in recognition of gram-negative and Gram-positive bacterial cell wall components. Immunity 11, 443-451 (1999).
    • (1999) Immunity , vol.11 , pp. 443-451
    • Takeuchi, O.1
  • 11
    • 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
  • 12
    • 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
  • 13
    • 0043198157 scopus 로고    scopus 로고
    • Toll-like receptor (TLR) 2 and TLR4 are essential for Aspergillus-induced activation of murinemacrophages
    • Meier, A. et al. Toll-like receptor (TLR) 2 and TLR4 are essential for Aspergillus-induced activation of murinemacrophages. Cell Microbiol. 5, 561-370 (2003).
    • (2003) Cell Microbiol. , vol.5 , pp. 561-370
    • Meier, A.1
  • 14
    • 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
  • 15
    • 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
  • 16
    • 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
  • 17
    • 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 E Sousa, C.5
  • 18
    • 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
  • 19
    • 0041827164 scopus 로고    scopus 로고
    • Nods, Nalps and Naip: Intracellular regulators of bacterial-induced inflammation
    • Chamaillard, M., Girardin, S. E., Viala, J. & Philpott, D. J. Nods, Nalps and Naip: intracellular regulators of bacterial-induced inflammation. Cell Microbiol. 5, 581-592 (2003).
    • (2003) Cell Microbiol. , vol.5 , pp. 581-592
    • Chamaillard, M.1    Girardin, S.E.2    Viala, J.3    Philpott, D.J.4
  • 20
    • 0035805110 scopus 로고    scopus 로고
    • Vital involvement of a natural killer cell activation receptor in resistance to viral infection
    • Brown, M. G. et al. Vital involvement of a natural killer cell activation receptor in resistance to viral infection. Science 292, 934-937 (2001).
    • (2001) Science , vol.292 , pp. 934-937
    • Brown, M.G.1
  • 21
    • 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
  • 22
    • 0034775153 scopus 로고    scopus 로고
    • Toll-like receptors control activation of adaptive immune responses
    • Schnare, M. et al. Toll-like receptors control activation of adaptive immune responses. Nature Immunol. 2, 947-950 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 947-950
    • Schnare, M.1
  • 23
    • 0022371461 scopus 로고
    • Identity of tumour necrosis factor and the macrophage-secreted factor cachectin
    • Beutler, B. et al. Identity of tumour necrosis factor and the macrophage-secreted factor cachectin. Nature 316, 552-554 (1985).
    • (1985) Nature , vol.316 , pp. 552-554
    • Beutler, B.1
  • 24
    • 0022411888 scopus 로고
    • Passive immunization against cachectin/tumor necrosis factor (TNF) protects mice from the lethal effect of endotoxin
    • Beutler, B., Milsark, I. W. & Cerami, A. Passive immunization against cachectin/tumor necrosis factor (TNF) protects mice from the lethal effect of endotoxin. Science 229, 869-871 (1985).
    • (1985) Science , vol.229 , pp. 869-871
    • Beutler, B.1    Milsark, I.W.2    Cerami, A.3
  • 25
    • 0028222122 scopus 로고
    • Interferon γ receptor deficient mice are resistant to endotoxic shock
    • Car, B. D. et al. Interferon γ receptor deficient mice are resistant to endotoxic shock. J. Exp. Med. 179, 1437-1444 (1994).
    • (1994) J. Exp. Med. , vol.179 , pp. 1437-1444
    • Car, B.D.1
  • 26
    • 0038476601 scopus 로고    scopus 로고
    • Central role for type 1 interferons and Tyk2 in lipopolysaccharide- induced endotoxin shock
    • Karaghiosoff, M. et al. Central role for type 1 interferons and Tyk2 in lipopolysaccharide-induced endotoxin shock. Nature Immunol. 4, 471-477 (2003).
    • (2003) Nature Immunol. , vol.4 , pp. 471-477
    • Karaghiosoff, M.1
  • 27
    • 0028987562 scopus 로고
    • Interleukin-12 is required for interferon-γ production and lethality in lipopolysaccharide-induced shock in mice
    • Wysocka, M. et al. Interleukin-12 is required for interferon-γ production and lethality in lipopolysaccharide-induced shock in mice. Eur. J. Immunol. 25, 672-676 (1995).
    • (1995) Eur. J. Immunol. , vol.25 , pp. 672-676
    • Wysocka, M.1
  • 28
    • 0028143211 scopus 로고
    • Randomised double-blind comparison of chimeric monoclonal antibody to tumour necrosis factor α (cA2) versus placebo in rheumatoid arthritis
    • Elliott, M. J. et al. Randomised double-blind comparison of chimeric monoclonal antibody to tumour necrosis factor α (cA2) versus placebo in rheumatoid arthritis. Lancet 344, 1105-1110 (1994).
    • (1994) Lancet , vol.344 , pp. 1105-1110
    • Elliott, M.J.1
  • 29
    • 0034094123 scopus 로고    scopus 로고
    • Succesful treatment of active ankylosing spondylitis with the anti-tumor necrosis factor α monoclonal antibody infliximab
    • Brandt, J. et al. Succesful treatment of active ankylosing spondylitis with the anti-tumor necrosis factor α monoclonal antibody infliximab. Arthritis Rheum. 43, 1346-1352 (2000).
    • (2000) Arthritis Rheum. , vol.43 , pp. 1346-1352
    • Brandt, J.1
  • 30
    • 0029050742 scopus 로고
    • Treatment of Crohn's disease with anti-tumor necrosis factor chimeric monoclonal antibody (cA2)
    • Van Dullemen, H. M. et al. Treatment of Crohn's disease with anti-tumor necrosis factor chimeric monoclonal antibody (cA2). Gastroenterology 109, 129-135 (1995).
    • (1995) Gastroenterology , vol.109 , pp. 129-135
    • Van Dullemen, H.M.1
  • 31
    • 0036174873 scopus 로고    scopus 로고
    • Etanercept for severe psoriasis and psoriatic arthritis: Observations on combination therapy
    • Iyer, S., Yamauchi, P. & Lowe, N. J. Etanercept for severe psoriasis and psoriatic arthritis: observations on combination therapy. Br. J. Dermatol. 146, 118-121 (2002).
    • (2002) Br. J. Dermatol. , vol.146 , pp. 118-121
    • Iyer, S.1    Yamauchi, P.2    Lowe, N.J.3
  • 32
    • 18044400563 scopus 로고    scopus 로고
    • Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis
    • Georgel, P. et al. Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis. Dev. Cell 1, 503-514 (2001).
    • (2001) Dev. Cell , vol.1 , pp. 503-514
    • Georgel, P.1
  • 33
    • 0026082710 scopus 로고
    • Structure and expression of the attacin genes in Hyalophora cecropia
    • Sun, S. C., Lindstrom, I., Lee, J. Y. & Faye, I. Structure and expression of the attacin genes in Hyalophora cecropia. Eur. J. Biochem. 196, 247-254 (1991).
    • (1991) Eur. J. Biochem. , vol.196 , pp. 247-254
    • Sun, S.C.1    Lindstrom, I.2    Lee, J.Y.3    Faye, I.4
  • 34
    • 0026557911 scopus 로고
    • Insect immunity: Developmental and inducible activity of the Drosophila diptericin promoter
    • Reichhart, J. M. et al. Insect immunity: developmental and inducible activity of the Drosophila diptericin promoter. EMBO J. 11, 1469-1477 (1992).
    • (1992) EMBO J. , vol.11 , pp. 1469-1477
    • Reichhart, J.M.1
  • 35
    • 0027749495 scopus 로고
    • Insect immunity: The diptericin promoter contains multiple functional regulatory sequences homologous to mammalian acute-phase response elements
    • Georgel, P. et al. Insect immunity: the diptericin promoter contains multiple functional regulatory sequences homologous to mammalian acute-phase response elements. Biochem. Biophys. Res. Commun. 197, 508-517 (1993).
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 508-517
    • Georgel, P.1
  • 36
    • 0033711445 scopus 로고    scopus 로고
    • The Rel protein D1F mediates the antifungal but not the antibacterial host defense in Drosophila
    • Rutschmann, S. et al. The Rel protein D1F 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
  • 37
    • 0025186678 scopus 로고
    • κB-type enhancers are involved in lipopolysaccharide-mediated transcriptional activation of the tumor necrosis factor α gene in primary macrophages
    • Shakhov, A. N., Collart, M. A., Vassalli, P., Nedospasov, S. A. & Jongeneel, C. V. κB-type enhancers are involved in lipopolysaccharide- mediated transcriptional activation of the tumor necrosis factor α gene in primary macrophages. J. Exp. Med. 171, 35-47 (1990).
    • (1990) J. Exp. Med. , vol.171 , pp. 35-47
    • Shakhov, A.N.1    Collart, M.A.2    Vassalli, P.3    Nedospasov, S.A.4    Jongeneel, C.V.5
  • 38
    • 0025098538 scopus 로고
    • Endotoxin-responsive sequences control cachectin/TNF biosynthesis at the translational level
    • Han, J., Brown, T. & Beutler, B. Endotoxin-responsive sequences control cachectin/TNF biosynthesis at the translational level. J. Exp. Med. 171, 465-475 (1990).
    • (1990) J. Exp. Med. , vol.171 , pp. 465-475
    • Han, J.1    Brown, T.2    Beutler, B.3
  • 39
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu, H. L., Shu, H. B., Pan, M. G. & Goeddel, D. V. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84, 299-308 (1996).
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.L.1    Shu, H.B.2    Pan, M.G.3    Goeddel, D.V.4
  • 40
    • 0028978626 scopus 로고
    • TRAF2-mediated activation of NF-κB by TNF receptor 2 and CD40
    • Rothe, M., Sarma, V., Dixit, V. W. & Goeddel, D. V. TRAF2-mediated activation of NF-κB by TNF receptor 2 and CD40. Science 269, 1424-1427 (1995).
    • (1995) Science , vol.269 , pp. 1424-1427
    • Rothe, M.1    Sarma, V.2    Dixit, V.W.3    Goeddel, D.V.4
  • 41
    • 0032240080 scopus 로고    scopus 로고
    • Transforming growth factor-β1 (TGF-β1) promotes IL-2 mRNA expression through the up-regulation of NF-κB, AP-1 and NF-AT in EL4 cells
    • Han, S. H., Yea, S. S., Jeon, Y. J., Yang, K. H. & Kaminski, N. E. Transforming growth factor-β1 (TGF-β1) promotes IL-2 mRNA expression through the up-regulation of NF-κB, AP-1 and NF-AT in EL4 cells. J. Pharmacol. Exp. Ther. 287, 1105-1112 (1998).
    • (1998) J. Pharmacol. Exp. Ther. , vol.287 , pp. 1105-1112
    • Han, S.H.1    Yea, S.S.2    Jeon, Y.J.3    Yang, K.H.4    Kaminski, N.E.5
  • 42
    • 0037461958 scopus 로고    scopus 로고
    • Transient activation of NF-κB through a TAK1/1KK kinase pathway by TGF-β1 inhibits AP-1/SMAD signaling and apoptosis: Implications in liver tumor formation
    • Arsura, M. et al. Transient activation of NF-κB through a TAK1/1KK kinase pathway by TGF-β1 inhibits AP-1/SMAD signaling and apoptosis: implications in liver tumor formation. Oncogene 22, 412-425 (2003).
    • (2003) Oncogene , vol.22 , pp. 412-425
    • Arsura, M.1
  • 43
    • 0032589462 scopus 로고    scopus 로고
    • IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain
    • Sakurai, H., Chiba, H., Miyoshi, H., Sugita, T. & Toriumi, W. IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain. J. Biol. Chem. 274, 30353-30356 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 30353-30356
    • Sakurai, H.1    Chiba, H.2    Miyoshi, H.3    Sugita, T.4    Toriumi, W.5
  • 44
    • 0033537866 scopus 로고    scopus 로고
    • Functional interactions of transforming growth factor β-activated kinase 1 with IκB kinases to stimulate NF-κB activation
    • Sakurai, H., Miyoshi, H., Toriumi, W. & Sugita, T. Functional interactions of transforming growth factor β-activated kinase 1 with IκB kinases to stimulate NF-κB activation. J. Biol. Chem. 274, 10641-10648 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 10641-10648
    • Sakurai, H.1    Miyoshi, H.2    Toriumi, W.3    Sugita, T.4
  • 45
    • 0028229065 scopus 로고
    • Calcineurin mediates human tumor necrosis factor α gene induction in stimulated T and B cells
    • Goldfeld, A. E. et al. Calcineurin mediates human tumor necrosis factor α gene induction in stimulated T and B cells. J. Exp. Med. 180, 763-768 (1994).
    • (1994) J. Exp. Med. , vol.180 , pp. 763-768
    • Goldfeld, A.E.1
  • 46
    • 0026332710 scopus 로고
    • Activation of interleukin-2 gene transcription via the T-cell surface molecule CD28 is mediated through an NF-κB-like response element
    • Verweij, C. L., Geerts, M. & Aarden, L. A. Activation of interleukin-2 gene transcription via the T-cell surface molecule CD28 is mediated through an NF-κB-like response element. J. Biol. Chem. 266, I4179-I4182 (1991).
    • (1991) J. Biol. Chem. , vol.266
    • Verweij, C.L.1    Geerts, M.2    Aarden, L.A.3
  • 47
    • 0029977948 scopus 로고    scopus 로고
    • CD28 mediates a potent costimulatory signal for rapid degradation of IκBβ which is associated with accelerated activation of various NF-κB/Rel heterodimers
    • Harhaj, E. W., Maggirwar, S. B., Good, L. & Sun, S. C. CD28 mediates a potent costimulatory signal for rapid degradation of IκBβ which is associated with accelerated activation of various NF-κB/Rel heterodimers. Mol. Cell. Biol. 16, 6736-6743 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6736-6743
    • Harhaj, E.W.1    Maggirwar, S.B.2    Good, L.3    Sun, S.C.4
  • 48
    • 0034073381 scopus 로고    scopus 로고
    • Mixed-lineage kinase 3 delivers CD3/CD28-derived signals into the IκB kinase complex
    • Hehner, S. P. et al. Mixed-lineage kinase 3 delivers CD3/CD28-derived signals into the IκB kinase complex. Mol. Cell. Biol. 20, 2556-2568 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2556-2568
    • Hehner, S.P.1
  • 49
    • 0034031401 scopus 로고    scopus 로고
    • Protein kinase C-θ participates in NF-κB activation induced by CD3-CD28 costimulation through selective activation of IκB kinase β
    • Lin, X., O'Mahony, A., Mu, Y., Geleziunas, R. & Greene, W. C. Protein kinase C-θ participates in NF-κB activation induced by CD3-CD28 costimulation through selective activation of IκB kinase β. Mol. Cell. Biol. 20, 2933-2940 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2933-2940
    • Lin, X.1    O'Mahony, A.2    Mu, Y.3    Geleziunas, R.4    Greene, W.C.5
  • 50
    • 0037827638 scopus 로고    scopus 로고
    • Identifying the MAGUK protein Carma-1 as a central regulator of humoral immune responses and atopy by genome-wide mouse mutagenesis
    • Jun, J. E. et al. Identifying the MAGUK protein Carma-1 as a central regulator of humoral immune responses and atopy by genome-wide mouse mutagenesis. Immunity 18, 751-762 (2003).
    • (2003) Immunity , vol.18 , pp. 751-762
    • Jun, J.E.1
  • 51
    • 1942437466 scopus 로고    scopus 로고
    • CD28 delivers a unique signal leading to the selective recruitment of Re1A and p52 NF-κB subunits on IL-8 and Bcl-xL gene promoters
    • Marinari, B., Costanzo, A., Marzano, V., Piccolella, E. & Tuosto, L. CD28 delivers a unique signal leading to the selective recruitment of Re1A and p52 NF-κB subunits on IL-8 and Bcl-xL gene promoters. Proc. Natl Acad. Sci. USA 101, 6098-6103 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6098-6103
    • Marinari, B.1    Costanzo, A.2    Marzano, V.3    Piccolella, E.4    Tuosto, L.5
  • 52
    • 0346993668 scopus 로고    scopus 로고
    • CD3/CD28 costimulation-induced NF-κB activation is mediated by recruitment of protein kinase C-η, Bcl10, and IκB kinase β to the immunological synapse through CARMA1
    • Wang, D. et al. CD3/CD28 costimulation-induced NF-κB activation is mediated by recruitment of protein kinase C-η, Bcl10, and IκB kinase β to the immunological synapse through CARMA1. Mol. Cell. Biol. 24, 164-171 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 164-171
    • Wang, D.1
  • 53
    • 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
  • 54
    • 0347480224 scopus 로고    scopus 로고
    • Activation of autoreactive B cells by CpG dsDNA
    • Viglianti, G. A. et al. Activation of autoreactive B cells by CpG dsDNA. Immunity 19, 837-847 (2003).
    • (2003) Immunity , vol.19 , pp. 837-847
    • Viglianti, G.A.1
  • 56
    • 0025166114 scopus 로고
    • CD14, a receptor for complexes of lipopolysaccharide 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 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
  • 58
    • 0033551819 scopus 로고    scopus 로고
    • CD14-dependent internalization and metabolism of extracellular phosphatidylinositol by monocytes
    • Wang, P. Y. & Munford, R. S. CD14-dependent internalization and metabolism of extracellular phosphatidylinositol by monocytes. J. Biol. Chem. 274, 23235-23241 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 23235-23241
    • Wang, P.Y.1    Munford, R.S.2
  • 60
    • 0030833817 scopus 로고    scopus 로고
    • CD36 mediates the in vitro inhibitory effects of thrombospondin-1 on endothelial cells
    • Dawson, D. W. et al. CD36 mediates the in vitro inhibitory effects of thrombospondin-1 on endothelial cells. J. Cell Biol. 138, 707-717 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 707-717
    • Dawson, D.W.1
  • 61
    • 0027280397 scopus 로고
    • CD36 is a receptor for oxidized low density lipoprotein 2
    • Endemann, G. et al. CD36 is a receptor for oxidized low density lipoprotein 2. J. Biol. Chem. 268, 11811-11816 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 11811-11816
    • Endemann, G.1
  • 62
    • 0038204838 scopus 로고    scopus 로고
    • CD36 mediates the innate host response to β-amyloid I
    • El Khoury, J. B. et al. CD36 mediates the innate host response to β-amyloid I. J. Exp. Med. 197, 1657-1666 (2003).
    • (2003) J. Exp. Med. , vol.197 , pp. 1657-1666
    • El Khoury, J.B.1
  • 63
    • 12344320716 scopus 로고    scopus 로고
    • Thrombospondin-1 is a major activator of TGF-β1 in vivo
    • Crawford, S. E. et al. Thrombospondin-1 is a major activator of TGF-β1 in vivo. Cell 93, 1159-1170 (1998).
    • (1998) Cell , vol.93 , pp. 1159-1170
    • Crawford, S.E.1
  • 64
    • 0007094269 scopus 로고
    • The formation of anti-sheep hemolytic amboceptor in the normal and tuberculous guinea pig
    • Lewis, P. A. & Loomis, D. The formation of anti-sheep hemolytic amboceptor in the normal and tuberculous guinea pig. J. Exp. Med. 40, 503 (1924).
    • (1924) J. Exp. Med. , vol.40 , pp. 503
    • Lewis, P.A.1    Loomis, D.2
  • 65
    • 84954971084 scopus 로고
    • Sensitization to horse serum by means of adjuvants
    • Freund, J. & McDermott, K. Sensitization to horse serum by means of adjuvants. Proc. Soc. Exp. Biol. Med. 49, 548-553 (1942).
    • (1942) Proc. Soc. Exp. Biol. Med. , vol.49 , pp. 548-553
    • Freund, J.1    McDermott, K.2
  • 66
    • 0345883301 scopus 로고
    • Effect of meningococcal endotoxin on the immune response
    • Condie, R. M., Zak, S. J. & Good, R. A. Effect of meningococcal endotoxin on the immune response. Proc. Soc. Exp. Biol. Med. 90, 355-360 (1955).
    • (1955) Proc. Soc. Exp. Biol. Med. , vol.90 , pp. 355-360
    • Condie, R.M.1    Zak, S.J.2    Good, R.A.3
  • 67
    • 0035030376 scopus 로고    scopus 로고
    • Type 1 interferons potently enhance humoral immunity and can promote isotype switching by stimulating dendritic cells in vivo
    • Le Bon, A. et al. Type 1 interferons potently enhance humoral immunity and can promote isotype switching by stimulating dendritic cells in vivo. Immunity 14, 461-470 (2001).
    • (2001) Immunity , vol.14 , pp. 461-470
    • Le Bon, A.1
  • 68
    • 0036668242 scopus 로고    scopus 로고
    • Links between innate and adaptive immunity via type 1 interferon
    • Le Bon, A. & Tough, D. F. Links between innate and adaptive immunity via type 1 interferon. Curr. Opin. Immunol. 14, 432-436 (2002).
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 432-436
    • Le Bon, A.1    Tough, D.F.2
  • 69
    • 0141703238 scopus 로고    scopus 로고
    • Selective contribution of IFN-α/β signaling to the maturation of dendritic cells induced by double-stranded RNA or viral infection
    • Honda, K. et al. Selective contribution of IFN-α/β signaling to the maturation of dendritic cells induced by double-stranded RNA or viral infection Proc. Natl Acad. Sci. USA 100, 10872-10877 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10872-10877
    • Honda, K.1
  • 70
    • 2342558523 scopus 로고    scopus 로고
    • Antitumor applications of stimulating toll-like receptor 9 with CpG oligodeoxynucleotides
    • Krieg, A. M. Antitumor applications of stimulating toll-like receptor 9 with CpG oligodeoxynucleotides. Curr. Oncol. Rep. 6, 88-95 (2004).
    • (2004) Curr. Oncol. Rep. , vol.6 , pp. 88-95
    • Krieg, A.M.1
  • 71
    • 0036686398 scopus 로고    scopus 로고
    • CPG-DNA aided cross-presentation of soluble antigens by dendritic cells
    • Maurer, T. et al. CPG-DNA aided cross-presentation of soluble antigens by dendritic cells. Eur. J. Immunol. 32, 2356-2364 (2002).
    • (2002) Eur. J. Immunol. , vol.32 , pp. 2356-2364
    • Maurer, T.1
  • 72
    • 0842343142 scopus 로고    scopus 로고
    • Lymphoid follicle destruction and immunosuppression after repeated CpG oligodeoxynucleotide administration
    • Heikenwalder, M. et al. Lymphoid follicle destruction and immunosuppression after repeated CpG oligodeoxynucleotide administration. Nature Med. 10, 187-192 (2004).
    • (2004) Nature Med. , vol.10 , pp. 187-192
    • Heikenwalder, M.1
  • 73
    • 0042493163 scopus 로고    scopus 로고
    • Therapeutic targeting of toll-like receptors for inflammatory and infectious diseases
    • O'Neill, L. A. Therapeutic targeting of toll-like receptors for inflammatory and infectious diseases. Curr. Opin. Pharmacol. 3, 396-403 (2003).
    • (2003) Curr. Opin. Pharmacol. , vol.3 , pp. 396-403
    • O'Neill, L.A.1
  • 74
    • 0032915186 scopus 로고    scopus 로고
    • DNA-based immunization for asthma
    • Broide, D. & Raz, E. DNA-Based immunization for asthma. Int. Arch. Allergy Immunol. 118, 453-456 (1999).
    • (1999) Int. Arch. Allergy Immunol. , vol.118 , pp. 453-456
    • Broide, D.1    Raz, E.2
  • 75
    • 0037974914 scopus 로고    scopus 로고
    • Critical role of the Toll-like receptor signal adaptor protein MyD88 in acute allograft rejection
    • Goldstein, D. R., Tesar, B. M., Akira, S. & Lakkis, F. G. Critical role of the Toll-like receptor signal adaptor protein MyD88 in acute allograft rejection. J. Clin. Invest. 111, 1571-1578 (2003).
    • (2003) J. Clin. Invest. , vol.111 , pp. 1571-1578
    • Goldstein, D.R.1    Tesar, B.M.2    Akira, S.3    Lakkis, F.G.4
  • 76
    • 0035826096 scopus 로고    scopus 로고
    • Efficacy and safety of recombinant human activated protein C for severe sepsis
    • Bernard, G. R. et al. Efficacy and safety of recombinant human activated protein C for severe sepsis. N. Engl. J. Med. 344, 699-709 (2001).
    • (2001) N. Engl. J. Med. , vol.344 , pp. 699-709
    • Bernard, G.R.1
  • 77
    • 0037151571 scopus 로고    scopus 로고
    • Effect of treatment with low doses of hydrocortisone and fludrocortisone on mortality in patients with septic shock
    • Annane, D. et al. Effect of treatment with low doses of hydrocortisone and fludrocortisone on mortality in patients with septic shock. J. Am. Med. Assoc. 288, 862-871 (2002).
    • (2002) J. Am. Med. Assoc. , vol.288 , pp. 862-871
    • Annane, D.1
  • 78
    • 0037947560 scopus 로고    scopus 로고
    • Assay of locus-specific genetic load implicates rare Toll-like receptor 4 mutations in meningococcal susceptibility
    • Smirnova, I. et al. Assay of locus-specific genetic load implicates rare Toll-like receptor 4 mutations in meningococcal susceptibility Proc. Natl Acad. Sci. USA 100, 6075-6080 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6075-6080
    • Smirnova, I.1
  • 79
    • 10744226016 scopus 로고    scopus 로고
    • A common dominant TLR5 stop codon polymorphism abolishes flagellin signaling and is associated with susceptibility to legionnaires' disease
    • Hawn, T. R. et al. A common dominant TLR5 stop codon polymorphism abolishes flagellin signaling and is associated with susceptibility to legionnaires' disease. J. Exp. Med. 198, 1563-1572 (2003).
    • (2003) J. Exp. Med. , vol.198 , pp. 1563-1572
    • Hawn, T.R.1
  • 80
    • 0342712508 scopus 로고    scopus 로고
    • E5531, a synthetic non-toxic lipid A derivafive blocks the immunobiological activities of lipopolysaccharide
    • Kawata, T. et al. E5531, a synthetic non-toxic lipid A derivafive blocks the immunobiological activities of lipopolysaccharide. Br. J. Pharmacol. 127, 853-862 (1999).
    • (1999) Br. J. Pharmacol. , vol.127 , pp. 853-862
    • Kawata, T.1
  • 81
    • 0037596457 scopus 로고    scopus 로고
    • A low molecular weight mimic of the Toll/IL-1 receptor/resistance domain inhibits IL-1 receptor-mediated responses
    • Bartfai T. et al. A low molecular weight mimic of the Toll/IL-1 receptor/resistance domain inhibits IL-1 receptor-mediated responses. Proc. Natl Acad. Sci. USA 100, 7971-7976 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7971-7976
    • Bartfai, T.1
  • 82
    • 0037129212 scopus 로고    scopus 로고
    • Severe impairment of interleukin-1 and Toll-like receptor signalling in mice lacking IRAK-4
    • Suzuki, N. et al. Severe impairment of interleukin-1 and Toll-like receptor signalling in mice lacking IRAK-4. Nature 416, 750-756 (2002).
    • (2002) Nature , vol.416 , pp. 750-756
    • Suzuki, N.1
  • 83
    • 0043176281 scopus 로고    scopus 로고
    • Role of adapter TRIF in the MyD88-independent Toll-like receptor signaling pathway
    • Yamamoto, M. et al. Role of adapter 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
  • 84
    • 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
  • 85
    • 0038714270 scopus 로고    scopus 로고
    • Poly(I-C)-induced Toll-like receptor 3 (TLR3)-mediated activation of NFκB and MAP kinase is through an interleukin-1 receptor-associated kinase (IRAK)-independent pathway employing the signaling components TLR3-TRAF6-TAK1-TAB2-PKR
    • Jiang, Z. et al. Poly(I-C)-induced Toll-like receptor 3 (TLR3)-mediated activation of NFκB and MAP kinase is through an interleukin-1 receptor-associated kinase (IRAK)-independent pathway employing the signaling components TLR3-TRAF6-TAK1-TAB2-PKR. J. Biol. Chem. 278, 16713-16719 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 16713-16719
    • Jiang, Z.1


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