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Volumn 23, Issue 1-2, 2003, Pages 15-44

Activation of mammalian Toll-like receptors by endogenous agonists

Author keywords

Coagulation; Degradation; Drosophila cascades; Endogenous; Heparan sulfate; Hyaluronic acid; Immunology; Infection; Inflammation; Innate immunity; Lipopolysaccharide; Mammalian; Matrix; Necrosis; Polysaccharides; R genes; Toll; Toll like receptors

Indexed keywords

HEPARAN SULFATE; HYALURONIC ACID; LIPOPOLYSACCHARIDE; POLYSACCHARIDE; TOLL LIKE RECEPTOR;

EID: 0038454645     PISSN: 10408401     EISSN: None     Source Type: Journal    
DOI: 10.1615/CritRevImmunol.v23.i12.20     Document Type: Review
Times cited : (141)

References (346)
  • 1
    • 0037066502 scopus 로고    scopus 로고
    • Decoding the patterns of self and nonself by the innate immune system
    • Medzhitov, R., and Janeway, C. A., Jr., Decoding the patterns of self and nonself by the innate immune system. Science 2002; 296(5566):298-300.
    • (2002) Science , vol.296 , Issue.5566 , pp. 298-300
    • Medzhitov, R.1    Janeway C.A., Jr.2
  • 2
    • 0037290876 scopus 로고    scopus 로고
    • Mammalian Toll-like receptors
    • Akira, S., Mammalian Toll-like receptors. Curr Opin Immunol 2003; 15(1):5-11.
    • (2003) Curr Opin Immunol , vol.15 , Issue.1 , pp. 5-11
    • Akira, S.1
  • 3
    • 0036839577 scopus 로고    scopus 로고
    • Endogenous ligands of Toll-like receptors: Implications for regulating inflammatory and immune responses
    • Beg, A. A., Endogenous ligands of Toll-like receptors: implications for regulating inflammatory and immune responses. Trends Immunol 2002; 23(11):509-512.
    • (2002) Trends Immunol , vol.23 , Issue.11 , pp. 509-512
    • Beg, A.A.1
  • 4
    • 0037213692 scopus 로고    scopus 로고
    • Evolutionary clues to the functions of the Toll-like family as surveillance receptors
    • Johnson, G. B., Brunn, G. J., Tang, A. H., and Platt, J. L., Evolutionary clues to the functions of the Toll-like family as surveillance receptors. Trends Immunol 2003; 24(1):19-24.
    • (2003) Trends Immunol , vol.24 , Issue.1 , pp. 19-24
    • Johnson, G.B.1    Brunn, G.J.2    Tang, A.H.3    Platt, J.L.4
  • 5
    • 0029591416 scopus 로고
    • Signaling pathways that establish the dorsal-ventral pattern of the Drosophila embryo
    • Morisato, D., and Anderson, K. V., Signaling pathways that establish the dorsal-ventral pattern of the Drosophila embryo. Annu Rev Genet 1995; 29:371-399.
    • (1995) Annu Rev Genet , vol.29 , pp. 371-399
    • Morisato, D.1    Anderson, K.V.2
  • 6
    • 0037066427 scopus 로고    scopus 로고
    • The danger model: A renewed sense of self
    • Matzinger, P., The danger model: a renewed sense of self. Science 2002; 296(5566):301-305.
    • (2002) Science , vol.296 , Issue.5566 , pp. 301-305
    • Matzinger, P.1
  • 7
    • 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., and Nusslein-Volhard, C., Establishment of dorsal-ventral polarity in the Drosophila embryo: genetic studies on the role of the Toll gene product. Cell 1985; 42(3):779-789.
    • (1985) Cell , vol.42 , Issue.3 , pp. 779-789
    • Anderson, K.V.1    Jurgens, G.2    Nusslein-Volhard, C.3
  • 8
    • 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., and Nusslein-Volhard, C., Establishment of dorsal-ventral polarity in the Drosophila embryo: the induction of polarity by the Toll gene product. Cell 1985; 42(3):791-798.
    • (1985) Cell , vol.42 , Issue.3 , pp. 791-798
    • Anderson, K.V.1    Bokla, L.2    Nusslein-Volhard, C.3
  • 9
    • 0027931646 scopus 로고
    • The product of the tobacco mosaic virus resistance gene N: Similarity to Toll and the interleukin-1 receptor
    • Whitham, S., Dinesh-Kumar, S. P., Choi, D., Hehl, R., Corr, C., and Baker, B., The product of the tobacco mosaic virus resistance gene N: similarity to Toll and the interleukin-1 receptor. Cell 1994; 78(6):1101-1115.
    • (1994) Cell , vol.78 , Issue.6 , pp. 1101-1115
    • Whitham, S.1    Dinesh-Kumar, S.P.2    Choi, D.3    Hehl, R.4    Corr, C.5    Baker, B.6
  • 10
    • 0029730738 scopus 로고    scopus 로고
    • A conserved signaling pathway: The Drosophila Toll-dorsal pathway
    • Belvin, M. P., and Anderson, K. V., A conserved signaling pathway: the Drosophila Toll-dorsal pathway. Annu Rev Cell Dev Biol 1996; 12:393-416.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 393-416
    • Belvin, M.P.1    Anderson, K.V.2
  • 11
    • 0025774776 scopus 로고
    • Drosophila Toll and IL-1 receptor
    • Gay, N. J. and Keith, F. J., Drosophila Toll and IL-1 receptor. Nature 1991; 351(6325):355-356.
    • (1991) Nature , vol.351 , Issue.6325 , pp. 355-356
    • Gay, N.J.1    Keith, F.J.2
  • 12
    • 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., and 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 1992; 267(4):2605-2609.
    • (1992) J Biol Chem , vol.267 , Issue.4 , pp. 2605-2609
    • Heguy, A.1    Baldari, C.T.2    Macchia, G.3    Telford, J.L.4    Melli, M.5
  • 13
    • 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., and Hoffmann, J. A., The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 1996; 86:973-983.
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.4    Hoffmann, J.A.5
  • 14
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov, R., Preston-Hurlburt, P., and Janeway, C. A., Jr., A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 1997; 388(6640):394-397.
    • (1997) Nature , vol.388 , Issue.6640 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway C.A., Jr.3
  • 16
    • 0034886143 scopus 로고    scopus 로고
    • Toll-like receptors: Critical proteins linking innate and acquired immunity
    • Akira, S., Takeda, K., and Kaisho, T., Toll-like receptors: critical proteins linking innate and acquired immunity. Nat Immunol 2001; 2:675-680.
    • (2001) Nat Immunol , vol.2 , pp. 675-680
    • Akira, S.1    Takeda, K.2    Kaisho, T.3
  • 17
    • 0036467392 scopus 로고    scopus 로고
    • Toll-like receptors: Key mediators of microbe detection
    • Underhill, D. M., and Ozinsky, A., Toll-like receptors: key mediators of microbe detection. Curr Opin Immunol 2002; 14(1):103-110.
    • (2002) Curr Opin Immunol , vol.14 , Issue.1 , pp. 103-110
    • Underhill, D.M.1    Ozinsky, A.2
  • 18
    • 0036162621 scopus 로고    scopus 로고
    • Toll-like receptors: Mammalian "taste receptors" for a smorgasbord of microbial invaders
    • Sieling, P. A., and Modlin, R. L., Toll-like receptors: mammalian "taste receptors" for a smorgasbord of microbial invaders. Curr Opin Microbiol 2002; 5(1):70-75.
    • (2002) Curr Opin Microbiol , vol.5 , Issue.1 , pp. 70-75
    • Sieling, P.A.1    Modlin, R.L.2
  • 19
    • 0036134963 scopus 로고    scopus 로고
    • Toll-like receptors: How they work and what they do
    • Beutler, B., Toll-like receptors: how they work and what they do. Curr Opin Hematol 2002; 9(1):2-10.
    • (2002) Curr Opin Hematol , vol.9 , Issue.1 , pp. 2-10
    • Beutler, B.1
  • 20
    • 0026791975 scopus 로고
    • The immune system evolved to discriminate infectious nonself from noninfectious self
    • Janeway, C. A., The immune system evolved to discriminate infectious nonself from noninfectious self. Immunol Today 1992; 13(1):11-16.
    • (1992) Immunol Today , vol.13 , Issue.1 , pp. 11-16
    • Janeway, C.A.1
  • 21
    • 0031050034 scopus 로고    scopus 로고
    • Innate immunity: Impact on the adaptive immune response
    • Medzhitov, R., and Janeway, C. A., Innate immunity: impact on the adaptive immune response. Curr Opin Immunol 1997; 9:4-9.
    • (1997) Curr Opin Immunol , vol.9 , pp. 4-9
    • Medzhitov, R.1    Janeway, C.A.2
  • 22
    • 0033952703 scopus 로고    scopus 로고
    • Tlr4: Central component of the sole mammalian LPS sensor
    • Beutler, B., Tlr4: central component of the sole mammalian LPS sensor. Curr Opin Immunol 2000; 12:20-26.
    • (2000) Curr Opin Immunol , vol.12 , pp. 20-26
    • Beutler, B.1
  • 23
    • 0035428081 scopus 로고    scopus 로고
    • Lipopolysaccharide as a target for the development of novel therapeutics in Gram-negative bacteria
    • Yethon, J. A., and Whitfield, C., Lipopolysaccharide as a target for the development of novel therapeutics in Gram-negative bacteria. Curr Drug Targets Infect Disord 2001; 1(2):91-106.
    • (2001) Curr Drug Targets Infect Disord , vol.1 , Issue.2 , pp. 91-106
    • Yethon, J.A.1    Whitfield, C.2
  • 24
    • 0034619794 scopus 로고    scopus 로고
    • A Toll-like receptor recognizes bacterial DNA
    • [See comments.] [Erratum appears in Nature 2001 Feb 1;409 (6820):646]
    • Hemmi, H., Takeuchi, O., Kawai, T., Kaisho, T., Sato, S., Sanjo, H., Matsumoto, M., Hoshino, K., Wagner, H., Takeda, K., and Akira, S., A Toll-like receptor recognizes bacterial DNA. [See comments.] [Erratum appears in Nature 2001 Feb 1;409 (6820):646.]. Nature 2000; 408(6813):740-745.
    • (2000) Nature , vol.408 , Issue.6813 , pp. 740-745
    • Hemmi, H.1    Takeuchi, O.2    Kawai, T.3    Kaisho, T.4    Sato, S.5    Sanjo, H.6    Matsumoto, M.7    Hoshino, K.8    Wagner, H.9    Takeda, K.10    Akira, S.11
  • 25
    • 0035909372 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3
    • Alexopoulou, L., Holt, A. C., Medzhitov, R., and Flavell, R. A., Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3. Nature 2001; 413(6857):732-738.
    • (2001) Nature , vol.413 , Issue.6857 , pp. 732-738
    • Alexopoulou, L.1    Holt, A.C.2    Medzhitov, R.3    Flavell, R.A.4
  • 26
    • 0034650420 scopus 로고    scopus 로고
    • Cutting edge: Preferentially the R-stereoisomer stercoisomer of the mycoplasmal lipopeptide macrophage-activating lipopeptide-2 activates immune cells through a Toll-like receptor 2- and MyD88-dependent signaling pathway
    • Takeuchi, O., Kaufmann, A., Grote, K., Kawai, T., Hoshino, K., Morr, M., Muhlradt, P. F., and Akira, S., Cutting edge: preferentially the R-stereoisomer stercoisomer of the mycoplasmal lipopeptide macrophage-activating lipopeptide-2 activates immune cells through a Toll-like receptor 2- and MyD88-dependent signaling pathway. J Immunol 2000; 164(2):554-557.
    • (2000) J Immunol , vol.164 , Issue.2 , pp. 554-557
    • Takeuchi, O.1    Kaufmann, A.2    Grote, K.3    Kawai, T.4    Hoshino, K.5    Morr, M.6    Muhlradt, P.F.7    Akira, S.8
  • 28
    • 0037213692 scopus 로고    scopus 로고
    • Evolutionary dues to the functions of the Toll-like family as surveillance receptors
    • Johnson, G. B., Brunn, G. J., Tang, A. H., and Platt, J. L., Evolutionary dues to the functions of the Toll-like family as surveillance receptors, Trends Immunol 2003; 24(1):19-24.
    • (2003) Trends Immunol , vol.24 , Issue.1 , pp. 19-24
    • Johnson, G.B.1    Brunn, G.J.2    Tang, A.H.3    Platt, J.L.4
  • 30
    • 0037013856 scopus 로고    scopus 로고
    • The Toll and Imd pathways are the major regulators of the immune response in Drosophila
    • De Gregorio, E., Spellman, P. T., Tzou, P., Rubin, G. M., and Lemaitre, B., The Toll and Imd pathways are the major regulators of the immune response in Drosophila. EMBO J 2002; 21(11):2568-2579.
    • (2002) EMBO J , vol.21 , Issue.11 , pp. 2568-2579
    • De Gregorio, E.1    Spellman, P.T.2    Tzou, P.3    Rubin, G.M.4    Lemaitre, B.5
  • 31
    • 0036167107 scopus 로고    scopus 로고
    • Drosophila innate immunity: An evolutionary perspective
    • Hoffmann, J. A., and Reichhart, J. M., Drosophila innate immunity: an evolutionary perspective. Nat Immunol 2002; 3(2):121-126.
    • (2002) Nat Immunol , vol.3 , Issue.2 , pp. 121-126
    • Hoffmann, J.A.1    Reichhart, J.M.2
  • 32
    • 0034920683 scopus 로고    scopus 로고
    • Primitive Toll signalling-bugs, flies, worms and man
    • Fallon, P. G., Allen, R. L., and Rich, T., Primitive Toll signalling-bugs, flies, worms and man. Trends Immunol 2001; 22(2):63-66.
    • (2001) Trends Immunol , vol.22 , Issue.2 , pp. 63-66
    • Fallon, P.G.1    Allen, R.L.2    Rich, T.3
  • 33
    • 0035321067 scopus 로고    scopus 로고
    • The evolution and genetics of innate immunity
    • Kimbrell, D. A., and Beutler, B., The evolution and genetics of innate immunity. Nat Rev Genet 2001; 2(4):256-267.
    • (2001) Nat Rev Genet , vol.2 , Issue.4 , pp. 256-267
    • Kimbrell, D.A.1    Beutler, B.2
  • 34
    • 0034304668 scopus 로고    scopus 로고
    • The Toll/interleukin-1 receptor domain: A molecular switch for inflammation and host defence
    • O'Neill, L., The Toll/interleukin-1 receptor domain: a molecular switch for inflammation and host defence. Biochem Soc Trans 2000; 28(5):557-563.
    • (2000) Biochem Soc Trans , vol.28 , Issue.5 , pp. 557-563
    • O'Neill, L.1
  • 35
    • 0037290889 scopus 로고    scopus 로고
    • Resistance gene signaling in plants - Complex similarities to animal innate immunity
    • Holt, B. F., Hubert, D. A., and Dangl, J. L., Resistance gene signaling in plants - complex similarities to animal innate immunity. Curr Opin Immunol 2003; 15(1):20-25.
    • (2003) Curr Opin Immunol , vol.15 , Issue.1 , pp. 20-25
    • Holt, B.F.1    Hubert, D.A.2    Dangl, J.L.3
  • 36
    • 0037070113 scopus 로고    scopus 로고
    • Toll-like receptors as adjuvant receptors
    • Kaisho, T., and Akira, S., Toll-like receptors as adjuvant receptors. Biochim Biophys Acta 2002; 1589 (1):1-13.
    • (2002) Biochim Biophys Acta , vol.1589 , Issue.1 , pp. 1-13
    • Kaisho, T.1    Akira, S.2
  • 37
    • 0035142623 scopus 로고    scopus 로고
    • The role of Toll-like receptors in host defense against microbial infection
    • Krutzik, S. R., Sieling, P. A., and Modlin, R. L., The role of Toll-like receptors in host defense against microbial infection. Curr Opin Immunol 2001; 13:104-108.
    • (2001) Curr Opin Immunol , vol.13 , pp. 104-108
    • Krutzik, S.R.1    Sieling, P.A.2    Modlin, R.L.3
  • 38
    • 0033968116 scopus 로고    scopus 로고
    • Endotoxin, Toll-like receptor 4, and the afferent limb of innate immunity
    • Beutler, B., Endotoxin, Toll-like receptor 4, and the afferent limb of innate immunity. Curr Opin Microbiol 2000; 3(1):23-28.
    • (2000) Curr Opin Microbiol , vol.3 , Issue.1 , pp. 23-28
    • Beutler, B.1
  • 39
    • 0037111078 scopus 로고    scopus 로고
    • Human Toll-like receptor 4 mutations but not CD14 polymorphisms are associated with an increased risk of Gram-negative infections
    • Agnese, D. M., Calvano, J. E., Hahm, S. J., Coyle, S. M., Corbett, S. A., Calvano, S. E., and Lowry, S. F., Human Toll-like receptor 4 mutations but not CD14 polymorphisms are associated with an increased risk of Gram-negative infections. J Infect Dis 2002; 186(10):1522-1525.
    • (2002) J Infect Dis , vol.186 , Issue.10 , pp. 1522-1525
    • Agnese, D.M.1    Calvano, J.E.2    Hahm, S.J.3    Coyle, S.M.4    Corbett, S.A.5    Calvano, S.E.6    Lowry, S.F.7
  • 40
    • 0022261144 scopus 로고
    • Additional evidence that the Lps gene locus regulates natural resistance to S. typhimurium in mice
    • O'Brien, A. D., Weinstein, D. A., Soliman, M. Y., and Rosenstreich, D. L., Additional evidence that the Lps gene locus regulates natural resistance to S. typhimurium in mice. J Immunol 1985; 134(5):2820-2823.
    • (1985) J Immunol , vol.134 , Issue.5 , pp. 2820-2823
    • O'Brien, A.D.1    Weinstein, D.A.2    Soliman, M.Y.3    Rosenstreich, D.L.4
  • 41
    • 0018841829 scopus 로고
    • Genetic control of susceptibility to Salmonella typhimurium in mice: Role of the LPS gene
    • O'Brien, A. D., Rosenstreich, D. L., Scher, I., Campbell, G. H., MacDermott, R. P., and Formal, S. B., Genetic control of susceptibility to Salmonella typhimurium in mice: role of the LPS gene. J Immunol 1980; 124(1):20-24.
    • (1980) J Immunol , vol.124 , Issue.1 , pp. 20-24
    • O'Brien, A.D.1    Rosenstreich, D.L.2    Scher, I.3    Campbell, G.H.4    MacDermott, R.P.5    Formal, S.B.6
  • 42
    • 0037083557 scopus 로고    scopus 로고
    • Cutting edge: The Toll pathway is required for resistance to Gram-positive bacterial infections in Drosophila
    • Rutschmann, S., Kilinc, A., and Ferrandon, D., Cutting edge: the Toll pathway is required for resistance to Gram-positive bacterial infections in Drosophila. J Immunol 2002; 168(4):1542-1546.
    • (2002) J Immunol , vol.168 , Issue.4 , pp. 1542-1546
    • Rutschmann, S.1    Kilinc, A.2    Ferrandon, D.3
  • 43
    • 0033376608 scopus 로고    scopus 로고
    • The Lps locus: Genetic regulation of host responses to bacterial lipopolysaccharide
    • Qureshi, S, T., Gros, P., and Malo, D., The Lps locus: genetic regulation of host responses to bacterial lipopolysaccharide. Inflamm Res 1999; 48(12):613-620.
    • (1999) Inflamm Res , vol.48 , Issue.12 , pp. 613-620
    • Qureshi, S.T.1    Gros, P.2    Malo, D.3
  • 44
    • 0035210242 scopus 로고    scopus 로고
    • Sepsis begins at the interface of pathogen and host
    • Beutler, B., Sepsis begins at the interface of pathogen and host. Biochem Soc Trans 2001; 29(Pt 6):853-859.
    • (2001) Biochem Soc Trans , vol.29 , Issue.PART 6 , pp. 853-859
    • Beutler, B.1
  • 45
    • 0035210242 scopus 로고    scopus 로고
    • Sepsis begins at the interface of pathogen and host
    • Beutler, B., Sepsis begins at the interface of pathogen and host. Biochem Soc Trans 2001; 29:853-859.
    • (2001) Biochem Soc Trans , vol.29 , pp. 853-859
    • Beutler, B.1
  • 46
    • 0001827705 scopus 로고    scopus 로고
    • Brade, H., Opal, S. M., Vogel, S. N., and Morrison, D. C., editors. Basel: Marcel Dekker
    • b. Rietschel, E. T. and Westphal, O., Endotoxins in health and disease. In: Brade, H., Opal, S. M., Vogel, S. N., and Morrison, D. C., editors. Basel: Marcel Dekker, 1999:1-30.
    • (1999) Endotoxins in Health and Disease , pp. 1-30
    • Rietschel, E.T.1    Westphal, O.2
  • 47
    • 0037090077 scopus 로고    scopus 로고
    • Two lipoproteins extracted from Escherichia coli K-12 LCD25 lipopolysaccharide are the major components responsible for Toll-like receptor 2-mediated signaling
    • Lee, H. K., Lee, J., and Tobias, P. S., Two lipoproteins extracted from Escherichia coli K-12 LCD25 lipopolysaccharide are the major components responsible for Toll-like receptor 2-mediated signaling. J Immunol 2002; 168(8):4012-4017.
    • (2002) J Immunol , vol.168 , Issue.8 , pp. 4012-4017
    • Lee, H.K.1    Lee, J.2    Tobias, P.S.3
  • 48
    • 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., and Weis, J. J., Cutting edge: repurification of lipopolysaccharide eliminates signaling through both human and murine Toll-like receptor 2. J Immunol 2000; 165(2):618-622.
    • (2000) J Immunol , vol.165 , Issue.2 , pp. 618-622
    • Hirschfeld, M.1    Ma, Y.2    Weis, J.H.3    Vogel, S.N.4    Weis, J.J.5
  • 51
    • 0031987912 scopus 로고    scopus 로고
    • Molecular basis of host-pathogen interaction in septic shock
    • Heumann, D., Glauser, M. P., and Calandra, T., Molecular basis of host-pathogen interaction in septic shock. Curr Opin Microbiol 1998; 1(1):49-55.
    • (1998) Curr Opin Microbiol , vol.1 , Issue.1 , pp. 49-55
    • Heumann, D.1    Glauser, M.P.2    Calandra, T.3
  • 52
    • 0034958947 scopus 로고    scopus 로고
    • Epidemiology of severe sepsis in the United States: Analysis of incidence, outcome, and associated costs of care
    • Angus, D. C., Linde-Zwirble, W. T., Lidicker, J., Clermont, G., Carcillo, J., and Pinsky, M. R., Epidemiology of severe sepsis in the United States: analysis of incidence, outcome, and associated costs of care. Crit Care Med 2001; 29(7):1303-1310.
    • (2001) Crit Care Med , vol.29 , Issue.7 , pp. 1303-1310
    • Angus, D.C.1    Linde-Zwirble, W.T.2    Lidicker, J.3    Clermont, G.4    Carcillo, J.5    Pinsky, M.R.6
  • 54
    • 0037426726 scopus 로고    scopus 로고
    • The pathophysiology and treatment of sepsis
    • Hotchkiss, R. S., and Karl, I. E., The pathophysiology and treatment of sepsis. N Engl J Med 2003; 348 (2):138-150.
    • (2003) N Engl J Med , vol.348 , Issue.2 , pp. 138-150
    • Hotchkiss, R.S.1    Karl, I.E.2
  • 55
    • 0036629937 scopus 로고    scopus 로고
    • Structure and function of lipopolysaccharides
    • Erridge, C., Bennett-Guerrero, E., and Poxton, I. R., Structure and function of lipopolysaccharides. Microbes Infect 2002; 4(8):837-851.
    • (2002) Microbes Infect , vol.4 , Issue.8 , pp. 837-851
    • Erridge, C.1    Bennett-Guerrero, E.2    Poxton, I.R.3
  • 56
    • 0021339146 scopus 로고
    • Role of lipopolysaccharide in virulence of Pseudomonas aeruginosa
    • Cryz, S. J., Jr., Pitt, T. L., Furer, E., and Germanier, R., Role of lipopolysaccharide in virulence of Pseudomonas aeruginosa. Infect Immun 1984; 44(2):508-513.
    • (1984) Infect Immun , vol.44 , Issue.2 , pp. 508-513
    • Cryz S.J., Jr.1    Pitt, T.L.2    Furer, E.3    Germanier, R.4
  • 57
    • 0034647874 scopus 로고    scopus 로고
    • Structure of the Bordetella pertussis 1414 endotoxin
    • Caroff, M., Brisson, J., Martin, A., and Karibian, D., Structure of the Bordetella pertussis 1414 endotoxin. FEBS Lett 2000; 477(1-2):8-14.
    • (2000) FEBS Lett , vol.477 , Issue.1-2 , pp. 8-14
    • Caroff, M.1    Brisson, J.2    Martin, A.3    Karibian, D.4
  • 58
    • 0021289324 scopus 로고
    • Biological activities of synthetic lipid A analogs: Pyrogenicity, lethal toxicity, anticomplement activity, and induction of gelation of Limulus amoebocyte lysate
    • Tanamoto, K., Zahringer, U., McKenzie, G. R., Galanos, C., Rietschel, E. T., Luderitz, O., Kusumoto, S., and Shiba, T., Biological activities of synthetic lipid A analogs: pyrogenicity, lethal toxicity, anticomplement activity, and induction of gelation of Limulus amoebocyte lysate. Infect Immun 1984; 44(2):421-426.
    • (1984) Infect Immun , vol.44 , Issue.2 , pp. 421-426
    • Tanamoto, K.1    Zahringer, U.2    McKenzie, G.R.3    Galanos, C.4    Rietschel, E.T.5    Luderitz, O.6    Kusumoto, S.7    Shiba, T.8
  • 59
    • 0034650823 scopus 로고    scopus 로고
    • Cutting edge: Cationic antimicrobial peptides block the binding of lipopolysaccharide (LPS) to LPS binding protein
    • Scott, M. G., Vreugdenhil, A. C., Buurman, W. A., Hancock, R. E., and Gold, M. R., Cutting edge: cationic antimicrobial peptides block the binding of lipopolysaccharide (LPS) to LPS binding protein. J Immunol 2000; 164(2):549-553.
    • (2000) J Immunol , vol.164 , Issue.2 , pp. 549-553
    • Scott, M.G.1    Vreugdenhil, A.C.2    Buurman, W.A.3    Hancock, R.E.4    Gold, M.R.5
  • 60
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock, R. E., and Lehrer, R., Cationic peptides: a new source of antibiotics. Trends Biotechnol 1998; 16(2):82-88.
    • (1998) Trends Biotechnol , vol.16 , Issue.2 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 61
    • 0023279472 scopus 로고
    • A new class of synthetic antibacterials acting on lipopolysaccharide biosynthesis
    • Hammond, S. M., Claesson, A., Jansson, A. M., Larsson, L. G., Pring, B. G., Town, C. M., and Ekstrom, B., A new class of synthetic antibacterials acting on lipopolysaccharide biosynthesis. Nature 1987; 327(6124):730-732.
    • (1987) Nature , vol.327 , Issue.6124 , pp. 730-732
    • Hammond, S.M.1    Claesson, A.2    Jansson, A.M.3    Larsson, L.G.4    Pring, B.G.5    Town, C.M.6    Ekstrom, B.7
  • 62
    • 0033565407 scopus 로고    scopus 로고
    • Signaling events induced by lipopolysaccharide-activated Toll-like receptor 2
    • Yang, R. B., Mark, M. R., Gurney,A. L., and Godowski, P. J., Signaling events induced by lipopolysaccharide-activated Toll-like receptor 2. J Immunol 1999; 163(2):639-643.
    • (1999) J Immunol , vol.163 , Issue.2 , pp. 639-643
    • Yang, R.B.1    Mark, M.R.2    Gurney, A.L.3    Godowski, P.J.4
  • 63
    • 0031774181 scopus 로고    scopus 로고
    • Human Toll-like receptor 2 confers responsiveness to bacterial Epopolysaccharide
    • Kirschning, C. J., Wesche, H., Merrill Ayres, T., and Rothe, M., Human Toll-like receptor 2 confers responsiveness to bacterial Epopolysaccharide. J Exp Med 1998; 188(11):2091-2097.
    • (1998) J Exp Med , vol.188 , Issue.11 , pp. 2091-2097
    • Kirschning, C.J.1    Wesche, H.2    Merrill Ayres, T.3    Rothe, M.4
  • 65
    • 0033564325 scopus 로고    scopus 로고
    • Cutting edge: Cells that carry a null allele for Toll-like receptor 2 are capable of responding to endotoxin
    • Heine, H., Kirschning, C.J., Lien, E., Monks, B. G., Rothe, M., and Golenbock, D. T., Cutting edge: cells that carry a null allele for Toll-like receptor 2 are capable of responding to endotoxin. J Immunol 1999; 162(12):6971-6975.
    • (1999) J Immunol , vol.162 , Issue.12 , pp. 6971-6975
    • Heine, H.1    Kirschning, C.J.2    Lien, E.3    Monks, B.G.4    Rothe, M.5    Golenbock, D.T.6
  • 66
    • 0037439663 scopus 로고    scopus 로고
    • Lipopolysaccharides from Legionella and Rhizobium stimulate mouse bone marrow granulocytes via Toll-like receptor 2
    • Girard, R., Pedron, T., Uematsu, S., Balloy, V., Chignard, M., Akira, S., and Chaby, R., Lipopolysaccharides from Legionella and Rhizobium stimulate mouse bone marrow granulocytes via Toll-like receptor 2. J Cell Sci 2003; 116(Pt 2):293-302.
    • (2003) J Cell Sci , vol.116 , Issue.PART 2 , pp. 293-302
    • Girard, R.1    Pedron, T.2    Uematsu, S.3    Balloy, V.4    Chignard, M.5    Akira, S.6    Chaby, R.7
  • 67
    • 0034819316 scopus 로고    scopus 로고
    • Essential roles of CD14 and lipopolysaccharide-binding protein for activation of Toll-like receptor (TLR)2 as well as TLR4 reconstitution of TLR2- and TLR4-activation by distinguishable ligands in LPS preparations
    • Muta, T., and Takeshige, K., Essential roles of CD14 and lipopolysaccharide-binding protein for activation of Toll-like receptor (TLR)2 as well as TLR4 reconstitution of TLR2- and TLR4-activation by distinguishable ligands in LPS preparations. Eur J Biochem 2001; 268(16):4580-4589.
    • (2001) Eur J Biochem , vol.268 , Issue.16 , pp. 4580-4589
    • Muta, T.1    Takeshige, K.2
  • 71
    • 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., Takeuchi, O., Kawai, T., Sanjo, H., Ogawa, T., Takeda, Y., Takeda, K., and Akira, S., Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product. J Immunol 1999; 162:3749-3752.
    • (1999) J Immunol , vol.162 , pp. 3749-3752
    • Hoshino, K.1    Takeuchi, O.2    Kawai, T.3    Sanjo, H.4    Ogawa, T.5    Takeda, Y.6    Takeda, K.7    Akira, S.8
  • 72
    • 0035260009 scopus 로고    scopus 로고
    • LPS-hyporesponsiveness of mnd mice is associated with a mutation in Toll-like receptor 4
    • Bihl, F., Lariviere, L., Qureshi, S. T., Flaherty, L., and Malo, D., LPS-hyporesponsiveness of mnd mice is associated with a mutation in Toll-like receptor 4. Genes Immun 2001;2(1):56-59.
    • (2001) Genes Immun , vol.2 , Issue.1 , pp. 56-59
    • Bihl, F.1    Lariviere, L.2    Qureshi, S.T.3    Flaherty, L.4    Malo, D.5
  • 73
    • 0035834135 scopus 로고    scopus 로고
    • Secreted MD-2 is a large polymeric protein that efficiently confers lipopolysaccharide sensitivity to Toll-like receptor 4
    • Visintin, A., Mazzoni, A., Spitzer, J. A., and Segal, D. M., Secreted MD-2 is a large polymeric protein that efficiently confers lipopolysaccharide sensitivity to Toll-like receptor 4. Proc Natl Acad Sci U S A 2001;98(21):12156-12161.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.21 , pp. 12156-12161
    • Visintin, A.1    Mazzoni, A.2    Spitzer, J.A.3    Segal, D.M.4
  • 74
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu, R., Akashi, S., Ogata, H., Nagai, Y., Fukudome, K., Miyake, K., and Kimoto, M., MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J Exp Med 1999; 189:1777-1782.
    • (1999) J Exp Med , vol.189 , pp. 1777-1782
    • Shimazu, R.1    Akashi, S.2    Ogata, H.3    Nagai, Y.4    Fukudome, K.5    Miyake, K.6    Kimoto, M.7
  • 75
    • 0034617274 scopus 로고    scopus 로고
    • Cellular events mediated by lipopolysaccharide-stimulated Toll-like receptor 4. MD-2 is required for activation of mitogen-activated protein kinases and Elk-1
    • Yang, H., Young, D. W., Gusovsky, F., and Chow, J. C., Cellular events mediated by lipopolysaccharide-stimulated Toll-like receptor 4. MD-2 is required for activation of mitogen-activated protein kinases and Elk-1. J Biol Chem 2000; 275:20861-20866.
    • (2000) J Biol Chem , vol.275 , pp. 20861-20866
    • Yang, H.1    Young, D.W.2    Gusovsky, F.3    Chow, J.C.4
  • 79
    • 0037127309 scopus 로고    scopus 로고
    • MD-2 and TLR4 N-linked glycosylations are important for a functional lipopolysaccharide receptor
    • da Silva Correia, J., and Ulevitch, R. J., MD-2 and TLR4 N-linked glycosylations are important for a functional lipopolysaccharide receptor. J Biol Chem 2002; 277(3):1845-1854.
    • (2002) J Biol Chem , vol.277 , Issue.3 , pp. 1845-1854
    • Da Silva Correia, J.1    Ulevitch, R.J.2
  • 80
    • 0034007076 scopus 로고    scopus 로고
    • Physical contact between lipopolysaccharide and Toll-like receptor 4 revealed by genetic complementation
    • Poltorak, A., Ricciardi-Castagnoli, P., Citterio, S., and Beutler, B., Physical contact between lipopolysaccharide and Toll-like receptor 4 revealed by genetic complementation. Proc Natl Acad Sci U S A 2000; 97:2163-2167.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 2163-2167
    • Poltorak, A.1    Ricciardi-Castagnoli, P.2    Citterio, S.3    Beutler, B.4
  • 82
    • 0035877718 scopus 로고    scopus 로고
    • Lipopolysaccharide is in close proximity to each of the proteins in its membrane receptor complex transfer from CD14 to TLR4 and MD-2
    • da Silva Correia, C. J., Soldau, K., Christen, U., Tobias, P. S., and 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 2001; 276(24):21129-21135.
    • (2001) J Biol Chem , vol.276 , Issue.24 , pp. 21129-21135
    • Da Silva Correia, C.J.1    Soldau, K.2    Christen, U.3    Tobias, P.S.4    Ulevitch, R.J.5
  • 83
    • 0033382423 scopus 로고    scopus 로고
    • Analysis ofTlr4-mediated LPS signal transduction in macrophages by mutational modification of the receptor
    • Erratum appears in Blood Cells Mol Dis 2000 Feb; 26(1):9
    • Du, X., Poltorak, A., Silva, M., and Beutler, B., Analysis ofTlr4-mediated LPS signal transduction in macrophages by mutational modification of the receptor. [Erratum appears in Blood Cells Mol Dis 2000 Feb; 26(1):9.] Blood Cells Mol Dis 1999; 25(5-6):328-338.
    • (1999) Blood Cells Mol Dis , vol.25 , Issue.5-6 , pp. 328-338
    • Du, X.1    Poltorak, A.2    Silva, M.3    Beutler, B.4
  • 84
    • 0035253732 scopus 로고    scopus 로고
    • MD-2 enables Toll-like receptor 2 (TLR2)-mediated responses to lipopolysaccharide and enhances TLR2-mediated responses to Gram-positive and Gram-negative bacteria and their cell wall components
    • Dziarski, R., Wang, Q. Miyake, K., Kirschning, C. J., and Gupta, D., MD-2 enables Toll-like receptor 2 (TLR2)-mediated responses to lipopolysaccharide and enhances TLR2-mediated responses to Gram-positive and Gram-negative bacteria and their cell wall components. J Immunol 2001; 166:1938-1944.
    • (2001) J Immunol , vol.166 , pp. 1938-1944
    • Dziarski, R.1    Wang, Q.2    Miyake, K.3    Kirschning, C.J.4    Gupta, D.5
  • 85
    • 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., and Mathison, J. C., CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein. Science 1990; 249:1431-1433.
    • (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
  • 86
    • 0029919991 scopus 로고    scopus 로고
    • Resistance to endotoxin shock and reduced dissemination of Gram-negative bacteria in CD14-deficient mice
    • Haziot, A., Ferrero, E., Kontgen, F., Hijiya, N., Yamamoto, S., Silver, J., Stewart, C. L., and Goyert, S. M., Resistance to endotoxin shock and reduced dissemination of Gram-negative bacteria in CD14-deficient mice. Immunity 1996; 4:407-414.
    • (1996) Immunity , vol.4 , pp. 407-414
    • Haziot, A.1    Ferrero, E.2    Kontgen, F.3    Hijiya, N.4    Yamamoto, S.5    Silver, J.6    Stewart, C.L.7    Goyert, S.M.8
  • 87
    • 0031137733 scopus 로고    scopus 로고
    • CD14-dependent and CD14-independent signaling pathways in murine macrophages from normal and CD14 knockout mice stimulated with lipopolysaccharide or taxol
    • Perera, P. Y., Vogel, S. N., Detore, G. R., Haziot, A., and Goyert, S. M., CD14-dependent and CD14-independent signaling pathways in murine macrophages from normal and CD14 knockout mice stimulated with lipopolysaccharide or taxol. J Immunol 1997; 158(9):4422-4429.
    • (1997) J Immunol , vol.158 , Issue.9 , pp. 4422-4429
    • Perera, P.Y.1    Vogel, S.N.2    Detore, G.R.3    Haziot, A.4    Goyert, S.M.5
  • 89
    • 0034292364 scopus 로고    scopus 로고
    • Lipopolysaccharide induces physical proximity between CD14 and Toll-like receptor 4 (TLR4) prior to nuclear translocation of NF-kappa B
    • Jiang, Q., Akashi, S., Miyake, K., and Petty, H. R., Lipopolysaccharide induces physical proximity between CD14 and Toll-like receptor 4 (TLR4) prior to nuclear translocation of NF-kappa B. J Immunol 2000; 165 (7):3541-3544.
    • (2000) J Immunol , vol.165 , Issue.7 , pp. 3541-3544
    • Jiang, Q.1    Akashi, S.2    Miyake, K.3    Petty, H.R.4
  • 90
    • 0031569527 scopus 로고    scopus 로고
    • Lipopolysaccharide-binding protein and soluble CD14 transfer lipopolysaccharide to phospholipid bilayers: Preferential interaction with particular classes of lipid
    • Wuffel, M. M., and Wright, S. D., Lipopolysaccharide-binding protein and soluble CD14 transfer lipopolysaccharide to phospholipid bilayers: preferential interaction with particular classes of lipid. J Immunol 1997; 158(8):3925-3934.
    • (1997) J Immunol , vol.158 , Issue.8 , pp. 3925-3934
    • Wuffel, M.M.1    Wright, S.D.2
  • 91
    • 0024464813 scopus 로고
    • Lipopolysaccharide (LPS) binding protein opsonizes LPS-bearing particles for recognition by a novel receptor on macrophages
    • Wright, S. D., Tobias, P. S., Ulevitch, R. J., and Ramos, R. A., Lipopolysaccharide (LPS) binding protein opsonizes LPS-bearing particles for recognition by a novel receptor on macrophages. J Exp Med 1989; 170:1231-1242.
    • (1989) J Exp Med , vol.170 , pp. 1231-1242
    • Wright, S.D.1    Tobias, P.S.2    Ulevitch, R.J.3    Ramos, R.A.4
  • 92
    • 0028110048 scopus 로고
    • Lipopolysaccharide (LPS)-binding protein in human serum determines the tumor necrosis factor response of monocytes to LPS
    • Gallay, P., Barras, C., Tobias, P. S., Calandra, T., Glauser, M. P., and Heumann, D., Lipopolysaccharide (LPS)-binding protein in human serum determines the tumor necrosis factor response of monocytes to LPS. J Infect Dis 1994; 170(5):1319-1322.
    • (1994) J Infect Dis , vol.170 , Issue.5 , pp. 1319-1322
    • Gallay, P.1    Barras, C.2    Tobias, P.S.3    Calandra, T.4    Glauser, M.P.5    Heumann, D.6
  • 94
    • 0031440937 scopus 로고    scopus 로고
    • Targeted deletion of the lipopolysaccharide (LPS)-binding protein gene leads to profound suppression of LPS responses ex vivo, whereas in vivo responses remain intact
    • Wurfel, M. M., Monks, B. G., Ingalls, R. R., Dedrick, R. L., Delude, R., Zhou, D., Lamping, N., Schumann, R. R., Thieringer, R., Fenton, M. J., Wright, S. D., and Golenbock, D., Targeted deletion of the lipopolysaccharide (LPS)-binding protein gene leads to profound suppression of LPS responses ex vivo, whereas in vivo responses remain intact. J Exp Med 1997; 186(12):2051-2056.
    • (1997) J Exp Med , vol.186 , Issue.12 , pp. 2051-2056
    • Wurfel, M.M.1    Monks, B.G.2    Ingalls, R.R.3    Dedrick, R.L.4    Delude, R.5    Zhou, D.6    Lamping, N.7    Schumann, R.R.8    Thieringer, R.9    Fenton, M.J.10    Wright, S.D.11    Golenbock, D.12
  • 96
    • 0035423442 scopus 로고    scopus 로고
    • The essential role of lipopolysaccharide-binding protein in protection of mice against a peritoneal Salmonella infection involves the rapid induction of an inflammatory response
    • Heinrich, J. M., Bernheiden, M., Minigo, G., Yang, K. K., Schutt, C., Mannel, D. N., and Jack, R. S., The essential role of lipopolysaccharide-binding protein in protection of mice against a peritoneal Salmonella infection involves the rapid induction of an inflammatory response. J Immunol 2001; 167(3):1624-1628.
    • (2001) J Immunol , vol.167 , Issue.3 , pp. 1624-1628
    • Heinrich, J.M.1    Bernheiden, M.2    Minigo, G.3    Yang, K.K.4    Schutt, C.5    Mannel, D.N.6    Jack, R.S.7
  • 98
    • 0343776167 scopus 로고    scopus 로고
    • Fighting infection: The role of lipopolysaccharide binding proteins CD14 and LBP
    • Schutt, C., Fighting infection: the role of lipopolysaccharide binding proteins CD14 and LBP. Pathobiology 1999; 67(5-6):227-229.
    • (1999) Pathobiology , vol.67 , Issue.5-6 , pp. 227-229
    • Schutt, C.1
  • 99
    • 0035451119 scopus 로고    scopus 로고
    • Critical role of lipopolysaccharide-binding protein and CD14 in immune responses against Gram-negative bacteria
    • Le Roy, D., Di Padova, F., Adachi, Y., Glauser, M. P., Calandra, T., and Heumann, D., Critical role of lipopolysaccharide-binding protein and CD14 in immune responses against Gram-negative bacteria. J Immunol 2001; 167(5):2759-2765.
    • (2001) J Immunol , vol.167 , Issue.5 , pp. 2759-2765
    • Le Roy, D.1    Di Padova, F.2    Adachi, Y.3    Glauser, M.P.4    Calandra, T.5    Heumann, D.6
  • 100
    • 0028935983 scopus 로고
    • Soluble CD14 acts as a shuttle in the neutralization of lipopolysaccharide (LPS) by LPS-binding protein and reconstituted high density lipoprotein
    • Wurfel, M. M., Hallman, E., and Wright, S. D., Soluble CD14 acts as a shuttle in the neutralization of lipopolysaccharide (LPS) by LPS-binding protein and reconstituted high density lipoprotein. J Exp Med 1995; 181(5):1743-1754.
    • (1995) J Exp Med , vol.181 , Issue.5 , pp. 1743-1754
    • Wurfel, M.M.1    Hallman, E.2    Wright, S.D.3
  • 101
    • 0032523815 scopus 로고    scopus 로고
    • LPS-binding protein protects mice from septic shock caused by LPS or Gram-negative bacteria
    • Lamping, N., Dettmer, R., Schroder, N. W., Pfeil, D., Hallatschek, W., Burger, R., and Schumann, R. R., LPS-binding protein protects mice from septic shock caused by LPS or Gram-negative bacteria. J Clin Invest 1998; 101(10):2065-2071.
    • (1998) J Clin Invest , vol.101 , Issue.10 , pp. 2065-2071
    • Lamping, N.1    Dettmer, R.2    Schroder, N.W.3    Pfeil, D.4    Hallatschek, W.5    Burger, R.6    Schumann, R.R.7
  • 102
    • 0036498687 scopus 로고    scopus 로고
    • Does the shape of lipid A determine the interaction of LPS with Toll-like receptors?
    • Netea, M. G., van Deuren, M., Kullberg, B. J., Cavaillon, J. M., and Van der Meer, J. W., Does the shape of lipid A determine the interaction of LPS with Toll-like receptors? Trends Immunol 2002; 23 (3):135-139.
    • (2002) Trends Immunol , vol.23 , Issue.3 , pp. 135-139
    • Netea, M.G.1    Van Deuren, M.2    Kullberg, B.J.3    Cavaillon, J.M.4    Van der Meer, J.W.5
  • 103
    • 0034820507 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharides and innate immunity
    • Alexander, C., and Rietschel, E. T., Bacterial lipopolysaccharides and innate immunity. J Endotoxin Res 2001; 7(3):167-202.
    • (2001) J Endotoxin Res , vol.7 , Issue.3 , pp. 167-202
    • Alexander, C.1    Rietschel, E.T.2
  • 104
    • 0024423590 scopus 로고
    • Human endothelial cell adhesiveness for neutrophils, induced by Escherichia coli lipopolysaccharide in vitro, is inhibited by Bacteroides fragilis lipopolysaccharide
    • Magnuson, D. K., Weintraub, A., Pohlman, T. H., and Maier, R. V., Human endothelial cell adhesiveness for neutrophils, induced by Escherichia coli lipopolysaccharide in vitro, is inhibited by Bacteroides fragilis lipopolysaccharide. J Immunol 1989; 143(9):3025-3030.
    • (1989) J Immunol , vol.143 , Issue.9 , pp. 3025-3030
    • Magnuson, D.K.1    Weintraub, A.2    Pohlman, T.H.3    Maier, R.V.4
  • 105
    • 0028987076 scopus 로고
    • Tumor necrosis factor induction by an aqueous phenol-extracted lipopolysaccharide complex from Bacteroides species
    • Delahooke, D. M., Barclay, G. R., and Poxton, I. R., Tumor necrosis factor induction by an aqueous phenol-extracted lipopolysaccharide complex from Bacteroides species. Infect Immun 1995; 63(3):840-846.
    • (1995) Infect Immun , vol.63 , Issue.3 , pp. 840-846
    • Delahooke, D.M.1    Barclay, G.R.2    Poxton, I.R.3
  • 106
    • 0030984298 scopus 로고    scopus 로고
    • Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ
    • Guo, L., Lim, K. B., Gunn, J. S., Bainbridge, B., Darveau, R. P., Hackett, M., and Miller, S. I., Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science 1997; 276(5310):250-253.
    • (1997) Science , vol.276 , Issue.5310 , pp. 250-253
    • Guo, L.1    Lim, K.B.2    Gunn, J.S.3    Bainbridge, B.4    Darveau, R.P.5    Hackett, M.6    Miller, S.I.7
  • 109
    • 0033014671 scopus 로고    scopus 로고
    • Activation of murine macrophages by lipoprotein and lipooligosaccharide of Treponema denticola
    • Rosen, G., Sela, M. N., Naor, R., Halabi, A., Barak, V., and Shapira, L., Activation of murine macrophages by lipoprotein and lipooligosaccharide of Treponema denticola. Infect Immun 1999; 67(3):1180-1186.
    • (1999) Infect Immun , vol.67 , Issue.3 , pp. 1180-1186
    • Rosen, G.1    Sela, M.N.2    Naor, R.3    Halabi, A.4    Barak, V.5    Shapira, L.6
  • 110
    • 0036672050 scopus 로고    scopus 로고
    • TLR4-dependent recognition of lipopolysaccharide by epithelial cells requires sCD14
    • Backhed, F., Meijer, L., Normark, S., and Richter-Dahlfors, A., TLR4-dependent recognition of lipopolysaccharide by epithelial cells requires sCD14. Cell Microbiol 2002; 4(8):493-501.
    • (2002) Cell Microbiol , vol.4 , Issue.8 , pp. 493-501
    • Backhed, F.1    Meijer, L.2    Normark, S.3    Richter-Dahlfors, A.4
  • 112
    • 0035424901 scopus 로고    scopus 로고
    • Decreased expression of Toll-like receptor-4 and MD-2 correlates with intestinal epithelial cell protection against dysregulated proinflammatory gene expression in response to bacterial lipopolysaccharide
    • Abreu, M. T., Vora, P., Faure, E., Thomas, L. S., Arnold, E. T., and Arditi, M., Decreased expression of Toll-like receptor-4 and MD-2 correlates with intestinal epithelial cell protection against dysregulated proinflammatory gene expression in response to bacterial lipopolysaccharide. J Immunol 2001; 167(3):1609-1616.
    • (2001) J Immunol , vol.167 , Issue.3 , pp. 1609-1616
    • Abreu, M.T.1    Vora, P.2    Faure, E.3    Thomas, L.S.4    Arnold, E.T.5    Arditi, M.6
  • 113
    • 0035000687 scopus 로고    scopus 로고
    • Absence of Toll-like receptor 4 explains endotoxin hyporesponsiveness in human intestinal epithelium
    • Naik, S., Kelly, E. J., Meijer, L., Pettersson, S., and Sanderson, I. R., Absence of Toll-like receptor 4 explains endotoxin hyporesponsiveness in human intestinal epithelium. J Pediatr Gastroenterol Nutr 2001; 32(4):449-453.
    • (2001) J Pediatr Gastroenterol Nutr , vol.32 , Issue.4 , pp. 449-453
    • Naik, S.1    Kelly, E.J.2    Meijer, L.3    Pettersson, S.4    Sanderson, I.R.5
  • 114
    • 0035863909 scopus 로고    scopus 로고
    • Bacterial invasion augments epithelial cytokine responses to Escherichia coli through a lipopolysaccharide-dependent mechanism
    • Schilling, J. D., Mulvey, M. A., Vincent, C. D., Lorenz, R. G., and Hultgren, S. J., Bacterial invasion augments epithelial cytokine responses to Escherichia coli through a lipopolysaccharide-dependent mechanism. J Immunol 2001; 166(2):1148-1155.
    • (2001) J Immunol , vol.166 , Issue.2 , pp. 1148-1155
    • Schilling, J.D.1    Mulvey, M.A.2    Vincent, C.D.3    Lorenz, R.G.4    Hultgren, S.J.5
  • 115
    • 0036144233 scopus 로고    scopus 로고
    • Commensal-associated molecular patterns induce selective Toll-like receptor-trafficking from apical membrane to cytoplasmic compartments in polarized intestinal epithelium
    • Cario, E., Brown, D., McKee, M., Lynch-Devaney, K., Gerken, G., and Podolsky, D. K., Commensal-associated molecular patterns induce selective Toll-like receptor-trafficking from apical membrane to cytoplasmic compartments in polarized intestinal epithelium. Am J Pathol 2002; 160(1):165-173.
    • (2002) Am J Pathol , vol.160 , Issue.1 , pp. 165-173
    • Cario, E.1    Brown, D.2    McKee, M.3    Lynch-Devaney, K.4    Gerken, G.5    Podolsky, D.K.6
  • 116
    • 0034623798 scopus 로고    scopus 로고
    • Structure and function of Toll-like receptor proteins
    • Means, T. K., Golenbock, D. T., and Fenton, M. J., Structure and function of Toll-like receptor proteins. Life Sci 2000; 68:241-258.
    • (2000) Life Sci , vol.68 , pp. 241-258
    • Means, T.K.1    Golenbock, D.T.2    Fenton, M.J.3
  • 118
    • 0034597766 scopus 로고    scopus 로고
    • Structural basis for signal transduction by the Toll/interleukin-1 receptor domains
    • Xu, Y., Tao, X., Shen, B., Horng, T., Medzhitov, R., Manley, J. L., and Tong, L., Structural basis for signal transduction by the Toll/interleukin-1 receptor domains. Nature 2000; 408(6808):111-115.
    • (2000) Nature , vol.408 , Issue.6808 , pp. 111-115
    • Xu, Y.1    Tao, X.2    Shen, B.3    Horng, T.4    Medzhitov, R.5    Manley, J.L.6    Tong, L.7
  • 119
    • 0035555301 scopus 로고    scopus 로고
    • TIRAP: An adapter molecule in the Toll signaling pathway
    • Horng, T., Barton, G. M., and Medzhitov, R., TIRAP: an adapter molecule in the Toll signaling pathway. Nat Immunol 2001; 2:835-841.
    • (2001) Nat Immunol , vol.2 , pp. 835-841
    • Horng, T.1    Barton, G.M.2    Medzhitov, R.3
  • 121
    • 0036709969 scopus 로고    scopus 로고
    • A universal role for MyD88 in TLR/IL-1R-mediated signaling
    • Janssens, S., and Beyaert, R., A universal role for MyD88 in TLR/IL-1R-mediated signaling. Trends Biochem Sci 2002; 27(9):474-482.
    • (2002) Trends Biochem Sci , vol.27 , Issue.9 , pp. 474-482
    • Janssens, S.1    Beyaert, R.2
  • 122
    • 0037114185 scopus 로고    scopus 로고
    • Cutting edge: A novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-beta promoter in the Toll-like receptor signaling
    • Yamamoto, M., Sato, S., Mori, K., Hoshino, K., Takeuchi, O., Takeda, K., and Akira, S., Cutting edge: a novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-beta promoter in the Toll-like receptor signaling. J Immunol 2002; 169(12):6668-6672.
    • (2002) J Immunol , vol.169 , Issue.12 , pp. 6668-6672
    • Yamamoto, M.1    Sato, S.2    Mori, K.3    Hoshino, K.4    Takeuchi, O.5    Takeda, K.6    Akira, S.7
  • 123
    • 0036448929 scopus 로고    scopus 로고
    • MyD88 as a bottle neck in Toll/IL-1 signaling
    • Takeuchi, O., and Akira, S., MyD88 as a bottle neck in Toll/IL-1 signaling. Curr Top Microbiol Immunol 2002; 270:155-167.
    • (2002) Curr Top Microbiol Immunol , vol.270 , pp. 155-167
    • Takeuchi, O.1    Akira, S.2
  • 124
    • 0037153130 scopus 로고    scopus 로고
    • The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors
    • Horng, T., Barton, G. M., Flavell, R. A., and Medzhitov, R., The adaptor molecule TIRAP provides signalling specificity for Toll-like receptors. Nature 2002; 420(6913):329-333.
    • (2002) Nature , vol.420 , Issue.6913 , pp. 329-333
    • Horng, T.1    Barton, G.M.2    Flavell, R.A.3    Medzhitov, R.4
  • 126
    • 0035339861 scopus 로고    scopus 로고
    • Endotoxin-induced maturation of MyD88-deficient dendritic cells
    • Kaisho, T., Takeuchi, O., Kawai, T., Hoshino, K., and Akira, S., Endotoxin-induced maturation of MyD88-deficient dendritic cells. J Immunol 2001; 166:5688-5694.
    • (2001) J Immunol , vol.166 , pp. 5688-5694
    • Kaisho, T.1    Takeuchi, O.2    Kawai, T.3    Hoshino, K.4    Akira, S.5
  • 127
    • 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., Takeuchi, O., Fujita, T., Inoue, J., Muhlradt, P. F., Sato, S., and Hoshino, K., 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 2001; 167(10):5887-5894.
    • (2001) J Immunol , vol.167 , Issue.10 , pp. 5887-5894
    • Kawai, T.1    Takeuchi, O.2    Fujita, T.3    Inoue, J.4    Muhlradt, P.F.5    Sato, S.6    Hoshino, K.7
  • 128
    • 0033563143 scopus 로고    scopus 로고
    • Cutting edge: Functional characterization of the effect of the C3H/HeJ defect in mice that lack an Lpsn gene: In vivo evidence for a dominant negative mutation
    • Vogel, S. N., Johnson, D., Perera, P. Y., Medvedev, A., Lariviere, L., Qureshi, S. T., and Malo, D., Cutting edge: functional characterization of the effect of the C3H/HeJ defect in mice that lack an Lpsn gene: in vivo evidence for a dominant negative mutation. J Immunol 1999; 162(10):5666-5670.
    • (1999) J Immunol , vol.162 , Issue.10 , pp. 5666-5670
    • Vogel, S.N.1    Johnson, D.2    Perera, P.Y.3    Medvedev, A.4    Lariviere, L.5    Qureshi, S.T.6    Malo, D.7
  • 130
    • 0035165287 scopus 로고    scopus 로고
    • Cutting edge: Functional interactions between Toll-like receptor (TLR) 2 and TLR1 or TLR6 in response to phenol-soluble modulin
    • Hajjar, A. M., O'Mahony, D. S., Ozinsky, A., Underhill, D. M., Aderem, A., Klebanoff, S. J., and Wilson, C. B., Cutting edge: functional interactions between Toll-like receptor (TLR) 2 and TLR1 or TLR6 in response to phenol-soluble modulin. J Immunol 2001; 166(1):15-19.
    • (2001) J Immunol , vol.166 , Issue.1 , pp. 15-19
    • Hajjar, A.M.1    O'Mahony, D.S.2    Ozinsky, A.3    Underhill, D.M.4    Aderem, A.5    Klebanoff, S.J.6    Wilson, C.B.7
  • 131
    • 0035879283 scopus 로고    scopus 로고
    • 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
    • Bulut, Y., Faure, E., Thomas, L., Equils, O., and 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 2001; 167(2):987-994.
    • (2001) J Immunol , vol.167 , Issue.2 , pp. 987-994
    • Bulut, Y.1    Faure, E.2    Thomas, L.3    Equils, O.4    Arditi, M.5
  • 133
    • 0034460240 scopus 로고    scopus 로고
    • Innate recognition of lipopolysaccharide by Toll-like receptor 4/MD-2 and RP105/MD-1
    • Miyake, K., Ogata, H., Nagai, Y., Akashi, S., and Kimoto, M., Innate recognition of lipopolysaccharide by Toll-like receptor 4/MD-2 and RP105/MD-1. J Endotoxin Res 2000; 6(5):389-391.
    • (2000) J Endotoxin Res , vol.6 , Issue.5 , pp. 389-391
    • Miyake, K.1    Ogata, H.2    Nagai, Y.3    Akashi, S.4    Kimoto, M.5
  • 134
    • 0028949390 scopus 로고
    • RP105, a novel B cell surface molecule implicated in B cell activation, is a member of the leucine-rich repeat protein family
    • Miyake, K., Yamashita, Y., Ogata, M., Sudo, T., and 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 1995; 154(7):3333-3340.
    • (1995) J Immunol , vol.154 , Issue.7 , pp. 3333-3340
    • Miyake, K.1    Yamashita, Y.2    Ogata, M.3    Sudo, T.4    Kimoto, M.5
  • 135
    • 0030589517 scopus 로고    scopus 로고
    • Molecular cloning of a human RP105 homologue and chromosomal localization of the mouse and human RP105 genes (Ly64 and LY64)
    • Miura, Y., Miyake, K., Yamashita, Y., Shimazu, R., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Inazawa, J., Abe, T., and Kimoto, M., Molecular cloning of a human RP105 homologue and chromosomal localization of the mouse and human RP105 genes (Ly64 and LY64). Genomics 1996; 38(3):299-304.
    • (1996) Genomics , vol.38 , Issue.3 , pp. 299-304
    • Miura, Y.1    Miyake, K.2    Yamashita, Y.3    Shimazu, R.4    Copeland, N.G.5    Gilbert, D.J.6    Jenkins, N.A.7    Inazawa, J.8    Abe, T.9    Kimoto, M.10
  • 136
    • 0028071612 scopus 로고
    • Murine B cell proliferation and protection from apoptosis with an antibody against a 105-kD molecule: Unresponsiveness of X-linked immunodeficient B cells
    • Miyake, K., Yamashita, Y., Hitoshi, Y., Takatsu, K., and Kimoto, M., Murine B cell proliferation and protection from apoptosis with an antibody against a 105-kD molecule: unresponsiveness of X-linked immunodeficient B cells. J Exp Med 1994; 180:1217-1224.
    • (1994) J Exp Med , vol.180 , pp. 1217-1224
    • Miyake, K.1    Yamashita, Y.2    Hitoshi, Y.3    Takatsu, K.4    Kimoto, M.5
  • 137
    • 0032146713 scopus 로고    scopus 로고
    • Mouse MD-1, a molecule that is physically associated with RP105 and positively regulates its expression
    • Miyake, K., Shimazu, R., Kondo, J., Niki,T., Akashi, S., Ogata, H., Yamashita, Y., Miura, Y., and Kimoto, M., Mouse MD-1, a molecule that is physically associated with RP105 and positively regulates its expression. J Immunol 1998; 161:1348-1353.
    • (1998) J Immunol , vol.161 , pp. 1348-1353
    • Miyake, K.1    Shimazu, R.2    Kondo, J.3    Niki, T.4    Akashi, S.5    Ogata, H.6    Yamashita, Y.7    Miura, Y.8    Kimoto, M.9
  • 138
    • 0032532315 scopus 로고    scopus 로고
    • RP105 is associated with MD-1 and transmits an activation signal in human B cells
    • Miura, Y., Shimazu, R., Miyake, K., Akashi, S., Ogata, H., Yamashita, Y., Narisawa, Y., and Kimoto, M., RP105 is associated with MD-1 and transmits an activation signal in human B cells. Blood 1998; 92(8):2815-2822.
    • (1998) Blood , vol.92 , Issue.8 , pp. 2815-2822
    • Miura, Y.1    Shimazu, R.2    Miyake, K.3    Akashi, S.4    Ogata, H.5    Yamashita, Y.6    Narisawa, Y.7    Kimoto, M.8
  • 139
    • 0035173628 scopus 로고    scopus 로고
    • CD11b/CD18 acts in concert with CD14 and Toll-like receptor (TLR) 4 to elicit full lipopolysaccharide and taxol-inducible gene expression
    • Perera, P. Y., Mayadas, T. N., Takeuchi, O., Akira, S., Zaks-Zilberman, M., Goyert, S. M., and Vogel, S. N., CD11b/CD18 acts in concert with CD14 and Toll-like receptor (TLR) 4 to elicit full lipopolysaccharide and taxol-inducible gene expression. J Immunol 2001; 166(1):574-581.
    • (2001) J Immunol , vol.166 , Issue.1 , pp. 574-581
    • Perera, P.Y.1    Mayadas, T.N.2    Takeuchi, O.3    Akira, S.4    Zaks-Zilberman, M.5    Goyert, S.M.6    Vogel, S.N.7
  • 140
    • 0036606913 scopus 로고    scopus 로고
    • Lipopolysaccharide recognition: CD14, TLRs and the LPS-activation cluster
    • Triantafilou, M., and Triantafilou, K., Lipopolysaccharide recognition: CD14, TLRs and the LPS-activation cluster. Trends Immunol 2002; 23(6):301-304.
    • (2002) Trends Immunol , vol.23 , Issue.6 , pp. 301-304
    • Triantafilou, M.1    Triantafilou, K.2
  • 141
    • 0037096172 scopus 로고    scopus 로고
    • Mediators of innate immune recognition of bacteria concentrate in lipid rafts and facilitate Epopolysaccharide-induced cell activation
    • Triantafilou, M., Miyake, K., Golenbock, D. T., and Triantafilou, K., Mediators of innate immune recognition of bacteria concentrate in lipid rafts and facilitate Epopolysaccharide-induced cell activation. J Cell Sci 2002; 115(Pt 12):2603-2611.
    • (2002) J Cell Sci , vol.115 , Issue.PART 12 , pp. 2603-2611
    • Triantafilou, M.1    Miyake, K.2    Golenbock, D.T.3    Triantafilou, K.4
  • 143
    • 0346980722 scopus 로고    scopus 로고
    • Mice genetically hyporesponsive to lipopolysaccharide (LPS) exhibit a defect in endocytic uptake of LPS and ceramide
    • Thieblemont, N., and Wright, S. D., Mice genetically hyporesponsive to lipopolysaccharide (LPS) exhibit a defect in endocytic uptake of LPS and ceramide. J Exp Med 1997; 185(12):2095-2100.
    • (1997) J Exp Med , vol.185 , Issue.12 , pp. 2095-2100
    • Thieblemont, N.1    Wright, S.D.2
  • 144
    • 0037018107 scopus 로고    scopus 로고
    • Toll-like receptor 4 resides in the Golgi apparatus and colocalizes with internalized lipopolysaccharide in intestinal epithehai cells
    • Hornef, M. W., Frisan, T., Vandewalle, A., Normark, S., and Richter-Dahlfors, A., Toll-like receptor 4 resides in the Golgi apparatus and colocalizes with internalized lipopolysaccharide in intestinal epithehai cells. J Exp Med 2002; 195(5):559-570.
    • (2002) J Exp Med , vol.195 , Issue.5 , pp. 559-570
    • Hornef, M.W.1    Frisan, T.2    Vandewalle, A.3    Normark, S.4    Richter-Dahlfors, A.5
  • 145
    • 0032101312 scopus 로고    scopus 로고
    • Innate immune recognition of bacterial lipopolysaccharide: Dependence on interactions with membrane lipids and endocytic movement
    • Thieblemont, N., Thieringer, R., and Wright, S. D., Innate immune recognition of bacterial lipopolysaccharide: dependence on interactions with membrane lipids and endocytic movement. Immunity 1998; 8(6):771-777.
    • (1998) Immunity , vol.8 , Issue.6 , pp. 771-777
    • Thieblemont, N.1    Thieringer, R.2    Wright, S.D.3
  • 146
    • 0033592748 scopus 로고    scopus 로고
    • The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens
    • See comments
    • Underhill, D; M., Ozinsky, A., Hajjar, A. M., Stevens, A., Wilson, C. B., Bassetti, M., and Aderem, A., The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens. [See comments.] Nature 1999; 401(6755):811-815.
    • (1999) Nature , vol.401 , Issue.6755 , pp. 811-815
    • Underhill, D.M.1    Ozinsky, A.2    Hajjar, A.M.3    Stevens, A.4    Wilson, C.B.5    Bassetti, M.6    Aderem, A.7
  • 147
    • 0034672088 scopus 로고    scopus 로고
    • Cutting edge: Naturally occurring soluble form of mouse Toll-like receptor 4 inhibits lipopolysaccharide signaling
    • Iwami, K. I., Matsuguchi, T., Masuda, A., Kikuchi, T., Musikacharoen, T., and Yoshikai, Y., Cutting edge: naturally occurring soluble form of mouse Toll-like receptor 4 inhibits lipopolysaccharide signaling. J Immunol 2000; 165(12):6682-6686.
    • (2000) J Immunol , vol.165 , Issue.12 , pp. 6682-6686
    • Iwami, K.I.1    Matsuguchi, T.2    Masuda, A.3    Kikuchi, T.4    Musikacharoen, T.5    Yoshikai, Y.6
  • 148
    • 0031801957 scopus 로고    scopus 로고
    • Signal transduction pathways activated by the IL-1 receptor family: Ancient signaling machinery in mammals, insects, and plants
    • O'Neill, L. A., and Greene, C., Signal transduction pathways activated by the IL-1 receptor family: ancient signaling machinery in mammals, insects, and plants. J Leukoc Biol 1998; 63(6):650-657.
    • (1998) J Leukoc Biol , vol.63 , Issue.6 , pp. 650-657
    • O'Neill, L.A.1    Greene, C.2
  • 149
    • 0035524488 scopus 로고    scopus 로고
    • Toll-like receptors and innate immunity
    • Medzhitov, R., Toll-like receptors and innate immunity. Nat Rev Immunol 2001;1:135.
    • (2001) Nat Rev Immunol , vol.1 , pp. 135
    • Medzhitov, R.1
  • 150
    • 0035104961 scopus 로고    scopus 로고
    • Toll-like receptors; their physiological role and signal transduction system
    • Takeuchi, O., and Akira, S., Toll-like receptors; their physiological role and signal transduction system. Int Immunopharmacol 2001; 1(4):625-635.
    • (2001) Int Immunopharmacol , vol.1 , Issue.4 , pp. 625-635
    • Takeuchi, O.1    Akira, S.2
  • 151
    • 0037064536 scopus 로고    scopus 로고
    • Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family
    • Martin, M. U., and Wesche, H., Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family. Biochim Biophys Acta 2002; 1592(3):265-280.
    • (2002) Biochim Biophys Acta , vol.1592 , Issue.3 , pp. 265-280
    • Martin, M.U.1    Wesche, H.2
  • 152
    • 0035190972 scopus 로고    scopus 로고
    • Human Toll-like receptor 2 mediates induction of the antimicrobial peptide human beta-defensin 2 in response to bacterial lipoprotein
    • Birchler,T., Seibl,R., Buchner, K., Loeliger, S., Seger, R., Hossle, J. P., Aguzzi, A., and Lauener, R. P., Human Toll-like receptor 2 mediates induction of the antimicrobial peptide human beta-defensin 2 in response to bacterial lipoprotein. Eur J Immunol 2001; 31(11):3131-3137.
    • (2001) Eur J Immunol , vol.31 , Issue.11 , pp. 3131-3137
    • Birchler, T.1    Seibl, R.2    Buchner, K.3    Loeliger, S.4    Seger, R.5    Hossle, J.P.6    Aguzzi, A.7    Lauener, R.P.8
  • 154
    • 0033591428 scopus 로고    scopus 로고
    • Phylogenetic perspectives in innate immunity
    • Hoffmann, J. A., Kafatos, F. C., Janeway, C. A., and Ezekowitz, R. A., Phylogenetic perspectives in innate immunity. Science 1999; 284(5418):1313-1318.
    • (1999) Science , vol.284 , Issue.5418 , pp. 1313-1318
    • Hoffmann, J.A.1    Kafatos, F.C.2    Janeway, C.A.3    Ezekowitz, R.A.4
  • 155
    • 0032191163 scopus 로고    scopus 로고
    • Innate immune recognition and control of adaptive immune responses
    • Medzhitov, R., and Janeway, C. A., Jr., Innate immune recognition and control of adaptive immune responses. Semin Immunol 1998; 10:351-353.
    • (1998) Semin Immunol , vol.10 , pp. 351-353
    • Medzhitov, R.1    Janeway C.A., Jr.2
  • 156
    • 0036832351 scopus 로고    scopus 로고
    • Opinion: Interpretation of the complexity of innate immune responses by functional genomics
    • Ricciardi-Castagnoli, P., and Granucci, F., Opinion: interpretation of
    • (2002) Nat Rev Immunol , vol.2 , Issue.11 , pp. 881-889
    • Ricciardi-Castagnoli, P.1    Granucci, F.2
  • 157
    • 0023912875 scopus 로고
    • Induction of tolerance to lipopolysaccharide (LPS)-D-galactosamine lethality by pretreatment with LPS is mediated by macrophages
    • Freudenberg, M. A., and Galanos, C., Induction of tolerance to lipopolysaccharide (LPS)-D-galactosamine lethality by pretreatment with LPS is mediated by macrophages. Infect Immun 1988; 56(5):1352-1357.
    • (1988) Infect Immun , vol.56 , Issue.5 , pp. 1352-1357
    • Freudenberg, M.A.1    Galanos, C.2
  • 158
    • 0037008716 scopus 로고    scopus 로고
    • Gamma interferon and granulocyte/monocyte colony-stimulating factor prevent endotoxin tolerance in human monocytes by promoting interleukin-1 receptor-associated kinase expression and its association to MyD88 and not by modulating TLR4 expression
    • Adib-Conquy, M., and Cavaillon, J. M., Gamma interferon and granulocyte/monocyte colony-stimulating factor prevent endotoxin tolerance in human monocytes by promoting interleukin-1 receptor-associated kinase expression and its association to MyD88 and not by modulating TLR4 expression. J Biol Chem 2002; 277(31):27927-27934.
    • (2002) J Biol Chem , vol.277 , Issue.31 , pp. 27927-27934
    • Adib-Conquy, M.1    Cavaillon, J.M.2
  • 162
    • 0035881949 scopus 로고    scopus 로고
    • Induction of tolerance to lipopolysaccharide and mycobacterial components in Chinese hamster ovary/CD14 cells is not affected by overexpression of Toll-like receptors 2 or 4
    • Medvedev, A. E., Henneke, P., Schromm, A., Lien, E., Ingalls, R., Fenton, M. J., Golenbock, D. T., and Vogel, S. N., Induction of tolerance to lipopolysaccharide and mycobacterial components in Chinese hamster ovary/CD14 cells is not affected by overexpression of Toll-like receptors 2 or 4. J Immunol 2001; 167(4):2257-2267.
    • (2001) J Immunol , vol.167 , Issue.4 , pp. 2257-2267
    • Medvedev, A.E.1    Henneke, P.2    Schromm, A.3    Lien, E.4    Ingalls, R.5    Fenton, M.J.6    Golenbock, D.T.7    Vogel, S.N.8
  • 163
    • 0036510366 scopus 로고    scopus 로고
    • Negative regulation of Toll-like receptor-mediated signaling by Tollip
    • Zhang, G., and Ghosh, S., Negative regulation of Toll-like receptor-mediated signaling by Tollip. J Biol Chem 2002; 277(9):7059-7065.
    • (2002) J Biol Chem , vol.277 , Issue.9 , pp. 7059-7065
    • Zhang, G.1    Ghosh, S.2
  • 164
    • 20244384395 scopus 로고    scopus 로고
    • Cutting edge: Endotoxin tolerance in mouse peritoneal macrophages correlates with down-regulation of surface Toll-like receptor 4 expression
    • Nomura, F., Akashi, S., Sakao, Y., Sato, S., Kawai, T., Matsumoto, M., Nakanishi, K., Kimoto, M., Miyake, K., Takeda, K., and Akira, S., Cutting edge: endotoxin tolerance in mouse peritoneal macrophages correlates with down-regulation of surface Toll-like receptor 4 expression. J Immunol 2000; 164:3476-3479.
    • (2000) J Immunol , vol.164 , pp. 3476-3479
    • Nomura, F.1    Akashi, S.2    Sakao, Y.3    Sato, S.4    Kawai, T.5    Matsumoto, M.6    Nakanishi, K.7    Kimoto, M.8    Miyake, K.9    Takeda, K.10    Akira, S.11
  • 165
    • 0036838930 scopus 로고    scopus 로고
    • Dysregulation of LPS-induced Toll-like receptor 4-MyD88 complex formation and IL-1 receptor-associated kinase 1 activation in endotoxin-tolerant cells
    • Medvedev, A. E., Lentschat, A., Wahl, L. M., Golenbock, D. T., and Vogel, S. N., Dysregulation of LPS-induced Toll-like receptor 4-MyD88 complex formation and IL-1 receptor-associated kinase 1 activation in endotoxin-tolerant cells. J Immunol 2002; 169(9):5209-5016.
    • (2002) J Immunol , vol.169 , Issue.9 , pp. 5209-5016
    • Medvedev, A.E.1    Lentschat, A.2    Wahl, L.M.3    Golenbock, D.T.4    Vogel, S.N.5
  • 166
    • 0036067659 scopus 로고    scopus 로고
    • Toll receptors, CD14, and macrophage activation and deactivation by LPS
    • Dobrovolskaia, M. A., and Vogel, S. N., Toll receptors, CD14, and macrophage activation and deactivation by LPS. Microbes Infect 2002; 4(9):903-914.
    • (2002) Microbes Infect , vol.4 , Issue.9 , pp. 903-914
    • Dobrovolskaia, M.A.1    Vogel, S.N.2
  • 167
    • 0034043956 scopus 로고    scopus 로고
    • Inhibition of lipopolysaccharide-induced signal transduction in endotoxin-tolerized mouse macrophages: Dysregulation of cytokine, chemokine, and Toll-like receptor 2 and 4 gene expression
    • Medvedev, A. E., Kopydlowski, K. M., and Vogel, S. N., Inhibition of lipopolysaccharide-induced signal transduction in endotoxin-tolerized mouse macrophages: dysregulation of cytokine, chemokine, and Toll-like receptor 2 and 4 gene expression. J Immunol 2000; 164(11):5564-5574.
    • (2000) J Immunol , vol.164 , Issue.11 , pp. 5564-5574
    • Medvedev, A.E.1    Kopydlowski, K.M.2    Vogel, S.N.3
  • 168
    • 0034671772 scopus 로고    scopus 로고
    • Synergy and cross-tolerance between Toll-like receptor (TLR) 2- and TLR4-mediated signaling pathways
    • Sato, S., Nomura, F., Kawai, T., Takeuchi, O., Muhlradt, P. F., Takeda, K., and Akira, S., Synergy and cross-tolerance between Toll-like receptor (TLR) 2- and TLR4-mediated signaling pathways. J Immunol 2000; 165(12):7096-7101.
    • (2000) J Immunol , vol.165 , Issue.12 , pp. 7096-7101
    • Sato, S.1    Nomura, F.2    Kawai, T.3    Takeuchi, O.4    Muhlradt, P.F.5    Takeda, K.6    Akira, S.7
  • 169
    • 0036232737 scopus 로고    scopus 로고
    • Toll-like receptor I inhibits Toll-like receptor 4 signaling in endothelial cells
    • Spitzer, J. H., Visintin, A., Mazzoni, A., Kennedy, M. N., and Segal, D. M., Toll-like receptor I inhibits Toll-like receptor 4 signaling in endothelial cells. Eur J Immunol 2002; 32(4):1182-1187.
    • (2002) Eur J Immunol , vol.32 , Issue.4 , pp. 1182-1187
    • Spitzer, J.H.1    Visintin, A.2    Mazzoni, A.3    Kennedy, M.N.4    Segal, D.M.5
  • 171
    • 0034597711 scopus 로고    scopus 로고
    • Tolerance and sensitization to endotoxin in Kupffer cells caused by acute ethanol involve interleukin-1 receptor-associated kinase
    • Yamashina, S., Wheeler, M. D., Rusyn, I., Ikejima, K., Sato, N., and Thurman, R. G., Tolerance and sensitization to endotoxin in Kupffer cells caused by acute ethanol involve interleukin-1 receptor-associated kinase. Biochem Biophys Res Commun 2000; 277(3):686-690.
    • (2000) Biochem Biophys Res Commun , vol.277 , Issue.3 , pp. 686-690
    • Yamashina, S.1    Wheeler, M.D.2    Rusyn, I.3    Ikejima, K.4    Sato, N.5    Thurman, R.G.6
  • 172
    • 0035997382 scopus 로고    scopus 로고
    • Lipopolysaccharide endotoxins
    • Raetz, C. R., and Whitfield, C., Lipopolysaccharide endotoxins. Annu Rev Biochem 2002; 71:635-700.
    • (2002) Annu Rev Biochem , vol.71 , pp. 635-700
    • Raetz, C.R.1    Whitfield, C.2
  • 173
    • 0035542869 scopus 로고    scopus 로고
    • Towards a rational development of antiendotoxin agents: Novel approaches to sequestration of bacterial endotoxins with small molecules
    • David, S. A., Towards a rational development of antiendotoxin agents: novel approaches to sequestration of bacterial endotoxins with small molecules. J Mol Recognit 2001; 14(6):370-387.
    • (2001) J Mol Recognit , vol.14 , Issue.6 , pp. 370-387
    • David, S.A.1
  • 174
    • 0036780681 scopus 로고    scopus 로고
    • Toll-like receptors as potential therapeutic targets for multiple diseases
    • Zuany-Amorim, C., Hastewell, J., and Walker, C., Toll-like receptors as potential therapeutic targets for multiple diseases. Nat Rev Drug Discov 2002; 1(10):797-807.
    • (2002) Nat Rev Drug Discov , vol.1 , Issue.10 , pp. 797-807
    • Zuany-Amorim, C.1    Hastewell, J.2    Walker, C.3
  • 175
    • 0037071251 scopus 로고    scopus 로고
    • Relevance of mutations in the TLR4 receptor in patients with Gram-negative septic shock
    • Lorenz, E., Mira, J. P., Frees, K. L., and Schwartz, D. A., Relevance of mutations in the TLR4 receptor in patients with Gram-negative septic shock. Arch Intern Med 2002; 162(9):1028-1032.
    • (2002) Arch Intern Med , vol.162 , Issue.9 , pp. 1028-1032
    • Lorenz, E.1    Mira, J.P.2    Frees, K.L.3    Schwartz, D.A.4
  • 177
    • 0036160150 scopus 로고    scopus 로고
    • Nods: A family of cytosolic proteins that regulate the host response to pathogens
    • Inohara, N., Ogura, Y., and Nunez, G., Nods: a family of cytosolic proteins that regulate the host response to pathogens. Curr Opin Microbiol 2002; 5(1):76-80.
    • (2002) Curr Opin Microbiol , vol.5 , Issue.1 , pp. 76-80
    • Inohara, N.1    Ogura, Y.2    Nunez, G.3
  • 178
    • 0036532316 scopus 로고    scopus 로고
    • Intracellular vs extracellular recognition of pathogens-common concepts in mammals and flies
    • Girardin, S. E., Sansonetti, P. J., and Philpott, D. J., Intracellular vs extracellular recognition of pathogens-common concepts in mammals and flies. Trends Microbiol 2002; 10(4):193-199.
    • (2002) Trends Microbiol , vol.10 , Issue.4 , pp. 193-199
    • Girardin, S.E.1    Sansonetti, P.J.2    Philpott, D.J.3
  • 179
    • 0033231647 scopus 로고    scopus 로고
    • The Arabidopsis RPS4 bacterial-resistance gene is a member of the TIR-NBS-LRR family of disease-resistance genes
    • Gassmann,W., Hinsch,M. E., and Staskawicz, B.J., The Arabidopsis RPS4 bacterial-resistance gene is a member of the TIR-NBS-LRR family of disease-resistance genes. Plant J 1999; 20(3):265-277.
    • (1999) Plant J , vol.20 , Issue.3 , pp. 265-277
    • Gassmann, W.1    Hinsch, M.E.2    Staskawicz, B.J.3
  • 180
    • 0036212554 scopus 로고    scopus 로고
    • Diversity, distribution, and ancient taxonomic relationships within the TIR and non-TIR NBS-LRR resistance gene subfamilies
    • Cannon, S. B., Zhu, H., Baumgarten, A. M., Spangler, R., May, G., Cook, D. R., and Young, N. D., Diversity, distribution, and ancient taxonomic relationships within the TIR and non-TIR NBS-LRR resistance gene subfamilies. J Mol Evol 2002; 54(4):548-562.
    • (2002) J Mol Evol , vol.54 , Issue.4 , pp. 548-562
    • Cannon, S.B.1    Zhu, H.2    Baumgarten, A.M.3    Spangler, R.4    May, G.5    Cook, D.R.6    Young, N.D.7
  • 181
    • 0035951792 scopus 로고    scopus 로고
    • Human Nodl confers responsiveness to bacterial lipopolysaccharides
    • Inohara, N., Ogura, Y., Chen, F. F., Muto, A., and Nunez, G., Human Nodl confers responsiveness to bacterial lipopolysaccharides. J Biol Chem 2001; 276:2551-2554.
    • (2001) J Biol Chem , vol.276 , pp. 2551-2554
    • Inohara, N.1    Ogura, Y.2    Chen, F.F.3    Muto, A.4    Nunez, G.5
  • 184
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defence responses to infection
    • Dangl, J. L., and Jones, J. D., Plant pathogens and integrated defence responses to infection. Nature 2001; 411(6839):826-833.
    • (2001) Nature , vol.411 , Issue.6839 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.2
  • 185
    • 0034789068 scopus 로고    scopus 로고
    • Resistance gene complexes: Evolution and utilization
    • Hulbert, S. H., Webb, C. A., Smith, S. M., and Sun, Q., Resistance gene complexes: evolution and utilization. Annu Rev Phytopathol 2001; 39:285-312.
    • (2001) Annu Rev Phytopathol , vol.39 , pp. 285-312
    • Hulbert, S.H.1    Webb, C.A.2    Smith, S.M.3    Sun, Q.4
  • 187
    • 0035933536 scopus 로고    scopus 로고
    • Common and contrasting themes of plant and animal diseases
    • Staskawicz, B. J., Mudgett, M. B., Dangl, J. L., and Galan, J. E., Common and contrasting themes of plant and animal diseases. Science 2001; 292:2285-2289.
    • (2001) Science , vol.292 , pp. 2285-2289
    • Staskawicz, B.J.1    Mudgett, M.B.2    Dangl, J.L.3    Galan, J.E.4
  • 188
    • 0036479659 scopus 로고    scopus 로고
    • Balancing selection favors guarding resistance proteins
    • Van der Hoorn, R. A., De Wit, P. J., and Joosten, M. H., Balancing selection favors guarding resistance proteins. Trends Plant Sci 2002; 7(2):67-71.
    • (2002) Trends Plant Sci , vol.7 , Issue.2 , pp. 67-71
    • Van der Hoorn, R.A.1    De Wit, P.J.2    Joosten, M.H.3
  • 189
    • 0032422882 scopus 로고    scopus 로고
    • Plant disease-resistance proteins and the gene-for-gene concept
    • Van der Biezen, E. A., and Jones, J. D., Plant disease-resistance proteins and the gene-for-gene concept. Trends Biochem Sci 1998; 23(12):454-456.
    • (1998) Trends Biochem Sci , vol.23 , Issue.12 , pp. 454-456
    • Van der Biezen, E.A.1    Jones, J.D.2
  • 190
    • 0022556791 scopus 로고
    • Structure and function of heparan sulfate proteoglycans
    • Gallagher, J. T., Lyon, M., and Steward, W. P., Structure and function of heparan sulfate proteoglycans. Biochem J 1986; 236:313-325.
    • (1986) Biochem J , vol.236 , pp. 313-325
    • Gallagher, J.T.1    Lyon, M.2    Steward, W.P.3
  • 191
    • 0026744148 scopus 로고
    • Cell surface heparan sulfate proteoglycans
    • Yanagishita, M., and Hascall, V. C., Cell surface heparan sulfate proteoglycans. J Biol Chem 1992; 267:9451-9454.
    • (1992) J Biol Chem , vol.267 , pp. 9451-9454
    • Yanagishita, M.1    Hascall, V.C.2
  • 192
    • 0033959545 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans on the cell surface: Versatile coordinators of cellular functions
    • Tumova, S., Woods, A., and Couchman, J. R., Heparan sulfate proteoglycans on the cell surface: versatile coordinators of cellular functions. Int J Biochem Cell Biol. 2000; 32(3):269-288.
    • (2000) Int J Biochem Cell Biol , vol.32 , Issue.3 , pp. 269-288
    • Tumova, S.1    Woods, A.2    Couchman, J.R.3
  • 193
    • 0026758187 scopus 로고
    • Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG-2/perlecan)
    • Murdoch, A. D., Dodge, G. R., Cohen, I., Tuan, R. S., and Iozzo, R. V., Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG-2/perlecan). J Biol Chem 1992; 267:8544-8557.
    • (1992) J Biol Chem , vol.267 , pp. 8544-8557
    • Murdoch, A.D.1    Dodge, G.R.2    Cohen, I.3    Tuan, R.S.4    Iozzo, R.V.5
  • 195
    • 0022892749 scopus 로고
    • William Henry Howell and Jay McLean: The experimental context for the discovery of heparin
    • Marcum, J. A., Fritze, L. M., Nawroth, P., Stem, D., and Rosenberg, R. D., William Henry Howell and Jay McLean: the experimental context for the discovery of heparin. J Biol Chem 1986; 261:7507-7517.
    • (1986) J Biol Chem , vol.261 , pp. 7507-7517
    • Marcum, J.A.1    Fritze, L.M.2    Nawroth, P.3    Stem, D.4    Rosenberg, R.D.5
  • 196
    • 0022322564 scopus 로고
    • Structure and biological activity of heparin
    • New York: Academic Press
    • Casu, B. Structure and biological activity of heparin. Advances in Carbohydrate Chemistry and Biochemistry, Vol. 43. New York: Academic Press, 1985:51-134.
    • (1985) Advances in Carbohydrate Chemistry and Biochemistry , vol.43 , pp. 51-134
    • Casu, B.1
  • 197
    • 0029989042 scopus 로고    scopus 로고
    • The structure and function of hyaluronan: An overview
    • Laurent, T. C., Laurent, U. B., and Fraser, J. R., The structure and function of hyaluronan: an overview, Immunol Cell Biol 1996; 74(2):A1-7.
    • (1996) Immunol Cell Biol , vol.74 , Issue.2
    • Laurent, T.C.1    Laurent, U.B.2    Fraser, J.R.3
  • 198
    • 0036154206 scopus 로고    scopus 로고
    • Hyaluronan and its catabolic products in tissue injury and repair
    • Noble, P. W., Hyaluronan and its catabolic products in tissue injury and repair. Matrix Biol 2002; 21(1):25-29.
    • (2002) Matrix Biol , vol.21 , Issue.1 , pp. 25-29
    • Noble, P.W.1
  • 199
    • 0031749471 scopus 로고    scopus 로고
    • Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2
    • Kato, M., Wang, H., Kainulainen, V., Fitzgerald, M. L., Ledbetter, S., Ornitz, D. M., and Bernfield, M., Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2. Nat Med 1998; 4:691-697.
    • (1998) Nat Med , vol.4 , pp. 691-697
    • Kato, M.1    Wang, H.2    Kainulainen, V.3    Fitzgerald, M.L.4    Ledbetter, S.5    Ornitz, D.M.6    Bernfield, M.7
  • 200
    • 0030967612 scopus 로고    scopus 로고
    • Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor receptor activation
    • Subramanian, S. V., Fitzgerald, M. L., and Bernfield, M., Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor receptor activation. J Biol Chem 1997; 272:14713-14720.
    • (1997) J Biol Chem , vol.272 , pp. 14713-14720
    • Subramanian, S.V.1    Fitzgerald, M.L.2    Bernfield, M.3
  • 201
    • 0037094084 scopus 로고    scopus 로고
    • Receptor-mediated monitoring of tissue well-being via detection of soluble heparan sulfate by Toll-like receptor 4
    • Johnson, G. B., Brunn, G.J., Kodaira, Y., and Platt, J. L., Receptor-mediated monitoring of tissue well-being via detection of soluble heparan sulfate by Toll-like receptor 4. J Immunol 2002; 168(10):5233-5239.
    • (2002) J Immunol , vol.168 , Issue.10 , pp. 5233-5239
    • Johnson, G.B.1    Brunn, G.J.2    Kodaira, Y.3    Platt, J.L.4
  • 203
    • 0034937208 scopus 로고    scopus 로고
    • Heparanases: Endoglycosidases that derade heparan sulfate proteoglycans
    • Bame, K. J., Heparanases: endoglycosidases that derade heparan sulfate proteoglycans. Glycobiol 2001; 11(6):91R-98R.
    • (2001) Glycobiol , vol.11 , Issue.6
    • Bame, K.J.1
  • 204
    • 0031966911 scopus 로고    scopus 로고
    • Regulation of platelet heparanase during inflammation: Role of pH and proteinases
    • Ihrcke, N. S., Parker, W., Reissner, K. J., and Platt, J. L., Regulation of platelet heparanase during inflammation: role of pH and proteinases. J Cell Physiol 1998; 175:255-267.
    • (1998) J Cell Physiol , vol.175 , pp. 255-267
    • Ihrcke, N.S.1    Parker, W.2    Reissner, K.J.3    Platt, J.L.4
  • 205
    • 0036283527 scopus 로고    scopus 로고
    • Regional manifestations and control of the immune system
    • Saadi, S., Wrenshall, L. E., and Platt, J. L., Regional manifestations and control of the immune system. FASEB J 2002; 16(8):849-856.
    • (2002) FASEB J , vol.16 , Issue.8 , pp. 849-856
    • Saadi, S.1    Wrenshall, L.E.2    Platt, J.L.3
  • 206
    • 0012030796 scopus 로고
    • Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase
    • Thompson, R. C., and Ohlsson, K., Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proc Natl Acad Sci U S A 1986; 83(18):6692-6696.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , Issue.18 , pp. 6692-6696
    • Thompson, R.C.1    Ohlsson, K.2
  • 207
    • 0020078928 scopus 로고
    • Solubilization and degradation of subendothelial matrix glycoproteins and proteoglycans by metastatic tumor cells
    • Kramer, R. H., Vogel, K. G., and Nicolson, G. L., Solubilization and degradation of subendothelial matrix glycoproteins and proteoglycans by metastatic tumor cells. J Biol Chem 1982; 257:2678-2686.
    • (1982) J Biol Chem , vol.257 , pp. 2678-2686
    • Kramer, R.H.1    Vogel, K.G.2    Nicolson, G.L.3
  • 208
    • 0021822245 scopus 로고
    • Sequential degradation of heparan sulfate in the subendothelial extracellular matrix by highly metastatic lymphoma cells
    • Bar-Ner, M., Kramer, M. D., Schirrmacher, V., Ishai-Michaeli, R., Fuks, Z., and Vlodavsky, I., Sequential degradation of heparan sulfate in the subendothelial extracellular matrix by highly metastatic lymphoma cells. Int J Cancer 1985; 35:483-491.
    • (1985) Int J Cancer , vol.35 , pp. 483-491
    • Bar-Ner, M.1    Kramer, M.D.2    Schirrmacher, V.3    Ishai-Michaeli, R.4    Fuks, Z.5    Vlodavsky, I.6
  • 209
    • 0040446013 scopus 로고    scopus 로고
    • Hyaluronidases in tissue invasion
    • Csoka, T. B., Frost, G. I., and Stern, R., Hyaluronidases in tissue invasion. Invasion Metastasis 1997; 17(6):297-311.
    • (1997) Invasion Metastasis , vol.17 , Issue.6 , pp. 297-311
    • Csoka, T.B.1    Frost, G.I.2    Stern, R.3
  • 210
    • 0034212445 scopus 로고    scopus 로고
    • Action pattern and substrate specificity of the hyaluronan lyase from group B streptococci
    • Baker, J. R., and Pritchard, D. G., Action pattern and substrate specificity of the hyaluronan lyase from group B streptococci. Biochem J 2000; 348(Pt 2):465-467.
    • (2000) Biochem J , vol.348 , Issue.PART 2 , pp. 465-467
    • Baker, J.R.1    Pritchard, D.G.2
  • 211
    • 0031627221 scopus 로고    scopus 로고
    • Oligosaccharide elicitors in host-pathogen interactions. Generation, perception, and signal transduction
    • Cote, F., Ham, K. S., Hahn, M. G., and Bergmann, C. W., Oligosaccharide elicitors in host-pathogen interactions. Generation, perception, and signal transduction. Subcell Biochem 1998; 29:385-432.
    • (1998) Subcell Biochem , vol.29 , pp. 385-432
    • Cote, F.1    Ham, K.S.2    Hahn, M.G.3    Bergmann, C.W.4
  • 214
    • 0022382680 scopus 로고
    • Degradation of heparan sulfate in the subendothelial extracellular matrix by a readily released heparanase from human neutrophils: Possible role in invasion through basement membranes
    • Matzner,Y.,Bar-Ner,M., Yahalom, J., Ishai-Michaeli, R., Fuks, Z., and Vlodavsky, I., Degradation of heparan sulfate in the subendothelial extracellular matrix by a readily released heparanase from human neutrophils: possible role in invasion through basement membranes. J Clin Invest 1985; 76:1306-1313.
    • (1985) J Clin Invest , vol.76 , pp. 1306-1313
    • Matzner, Y.1    Bar-Ner, M.2    Yahalom, J.3    Ishai-Michaeli, R.4    Fuks, Z.5    Vlodavsky, I.6
  • 215
    • 0025370901 scopus 로고
    • Degranulating mast cells secrete an endoglycosidase that degrades heparan sulfate in subendothelial extracellular matrix
    • Bashkin, P., Razin, E., Eldor, A., and Vlodavsky, I., Degranulating mast cells secrete an endoglycosidase that degrades heparan sulfate in subendothelial extracellular matrix. Blood 1990; 75:2204-2212.
    • (1990) Blood , vol.75 , pp. 2204-2212
    • Bashkin, P.1    Razin, E.2    Eldor, A.3    Vlodavsky, I.4
  • 216
    • 0021249299 scopus 로고
    • Activated T-lymphocytes produce a matrix-degrading heparan sulfate endoglycosidase
    • Naparstek, Y., Cohen, I. R., Fuks, Z., and Vlodavsky, I., Activated T-lymphocytes produce a matrix-degrading heparan sulfate endoglycosidase. Nature 1984; 310:241-244.
    • (1984) Nature , vol.310 , pp. 241-244
    • Naparstek, Y.1    Cohen, I.R.2    Fuks, Z.3    Vlodavsky, I.4
  • 217
    • 0038583352 scopus 로고
    • Neutrophil proteases cleave endothelial proteoglycan core protein: Potential role in inflammatory thrombosis
    • Vercellotti, G. M., Key, N. S., Platt, J. L., and Jacob, H. S., Neutrophil proteases cleave endothelial proteoglycan core protein: potential role in inflammatory thrombosis. J Cell Biochem Suppl 1990; 14E:217.
    • (1990) J Cell Biochem Suppl , vol.14 E , pp. 217
    • Vercellotti, G.M.1    Key, N.S.2    Platt, J.L.3    Jacob, H.S.4
  • 219
    • 0025993863 scopus 로고
    • The role of CSa and antibody in the release of heparan sulfate from endothelial cells
    • Platt, J. L., Dalmasso, A. P., Lindman, B. J., Ihrcke, N. S., and Bach, F. H., The role of CSa and antibody in the release of heparan sulfate from endothelial cells. Eur J Immunol 1991; 21:2887-2890.
    • (1991) Eur J Immunol , vol.21 , pp. 2887-2890
    • Platt, J.L.1    Dalmasso, A.P.2    Lindman, B.J.3    Ihrcke, N.S.4    Bach, F.H.5
  • 220
    • 0025911987 scopus 로고
    • Regulation of murine splenocyte responses by heparan sulfate
    • Wrenshall, L. E., Cerra, F. B., Carlson, A., Bach, F. H., and Platt, J. L., Regulation of murine splenocyte responses by heparan sulfate. J Immunol 1991; 147:455-459. 219.
    • (1991) J Immunol , vol.147 , pp. 455-459
    • Wrenshall, L.E.1    Cerra, F.B.2    Carlson, A.3    Bach, F.H.4    Platt, J.L.5
  • 221
    • 0025349483 scopus 로고
    • Release of heparan sulfate from endothelial cells: Implications for the pathogenesis of hyperacute rejection
    • Platt, J. L., Vercellotti, G. M., Lindman, B. J., Oegema, T. R., Jr., Bach, F. H., and Dalmasso, A. P., Release of heparan sulfate from endothelial cells: implications for the pathogenesis of hyperacute rejection. J Exp Med 1990; 171:1363-1368.
    • (1990) J Exp Med , vol.171 , pp. 1363-1368
    • Platt, J.L.1    Vercellotti, G.M.2    Lindman, B.J.3    Oegema T.R., Jr.4    Bach, F.H.5    Dalmasso, A.P.6
  • 222
    • 4244052656 scopus 로고
    • Antibody and complement activated endothelial cells release partially degraded heparan sulfate
    • Ihrcke, N. S., and Platt, J. L., Antibody and complement activated endothelial cells release partially degraded heparan sulfate. FASEB J 1992; 14:500-505.
    • (1992) FASEB J , vol.14 , pp. 500-505
    • Ihrcke, N.S.1    Platt, J.L.2
  • 223
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellen, L., and Lindahl, U., Proteoglycans: structures and interactions. Annu Rev Biochem 1991; 60:443-475.
    • (1991) Annu Rev Biochem , vol.60 , pp. 443-475
    • Kjellen, L.1    Lindahl, U.2
  • 224
    • 0028302391 scopus 로고
    • Cartilage proteoglycans: Structure and potential functions
    • Roughley, P. J., and Lee, E. R., Cartilage proteoglycans: structure and potential functions. Microsc Res Tech 1994; 28(5):385-397.
    • (1994) Microsc Res Tech , vol.28 , Issue.5 , pp. 385-397
    • Roughley, P.J.1    Lee, E.R.2
  • 225
    • 0035984272 scopus 로고    scopus 로고
    • Heparin and heparan sulfate: Structure and function
    • Rabenstein, D. L., Heparin and heparan sulfate: structure and function. Nat Prod Rep 2002; 19(3):312-31.
    • (2002) Nat Prod Rep , vol.19 , Issue.3 , pp. 312-331
    • Rabenstein, D.L.1
  • 227
    • 0037022804 scopus 로고    scopus 로고
    • Structural requirements for high-affinity heparin binding: Alanine scanning analysis of charged residues in the C-terminal domain of human extracellular superoxide dismutase
    • Stenlund, P., Lindberg, M. J., and Tibell, L. A., Structural requirements for high-affinity heparin binding: alanine scanning analysis of charged residues in the C-terminal domain of human extracellular superoxide dismutase. Biochemistry 2002; 41(9):3168-3175.
    • (2002) Biochemistry , vol.41 , Issue.9 , pp. 3168-3175
    • Stenlund, P.1    Lindberg, M.J.2    Tibell, L.A.3
  • 229
    • 0032496145 scopus 로고    scopus 로고
    • Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids
    • Kainulainen, V.,Wang, H., Schick, C., and Bernfield, M., Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids. J Biol Chem 1998; 273:11563-11569.
    • (1998) J Biol Chem , vol.273 , pp. 11563-11569
    • Kainulainen, V.1    Wang, H.2    Schick, C.3    Bernfield, M.4
  • 230
    • 0034254204 scopus 로고    scopus 로고
    • Phenotypic and functional maturation of dendritic cells modulated by heparan sulfate
    • Kodaira, Y., Nair, S. K., Wrenshall, L. E., Gilboa, E., and Platt, J. L., Phenotypic and functional maturation of dendritic cells modulated by heparan sulfate. J Immunol 2000; 165:1599-1604.
    • (2000) J Immunol , vol.165 , pp. 1599-1604
    • Kodaira, Y.1    Nair, S.K.2    Wrenshall, L.E.3    Gilboa, E.4    Platt, J.L.5
  • 231
    • 0025282411 scopus 로고
    • CD44 is the principal cell surface receptor for hyaluronate
    • Aruffo, A., Stamenkovic, I., Melnick, M., Underhill, C. B., and Seed, B., CD44 is the principal cell surface receptor for hyaluronate. Cell 1990; 61:1303-1313.
    • (1990) Cell , vol.61 , pp. 1303-1313
    • Aruffo, A.1    Stamenkovic, I.2    Melnick, M.3    Underhill, C.B.4    Seed, B.5
  • 232
    • 0027491845 scopus 로고
    • CD44 and its interaction with extracellular matrix
    • Lesley, J., Hyman, R., and Kincade, P. W., CD44 and its interaction with extracellular matrix. Adv Immunol 1993; 54:271-335.
    • (1993) Adv Immunol , vol.54 , pp. 271-335
    • Lesley, J.1    Hyman, R.2    Kincade, P.W.3
  • 233
    • 0033179160 scopus 로고    scopus 로고
    • Hyaluronate-enhanced hematopoiesis: Two different receptors trigger the release of interleukin-1beta and interleukin-6 from bone marrow macrophages
    • Khaldoyanidi, S., Moll, J., Karakhanova, S., Herrlich, P., and Ponta, H., Hyaluronate-enhanced hematopoiesis: two different receptors trigger the release of interleukin-1beta and interleukin-6 from bone marrow macrophages. Blood 1999; 94(3):940-949.
    • (1999) Blood , vol.94 , Issue.3 , pp. 940-949
    • Khaldoyanidi, S.1    Moll, J.2    Karakhanova, S.3    Herrlich, P.4    Ponta, H.5
  • 234
    • 0028816517 scopus 로고
    • Heparan sulfate initiates signals in murine macrophages leading to divergent biological outcomes
    • Wrenshall, L. E., Cerra, F. B., Singh, R. K., and Platt, J. L., Heparan sulfate initiates signals in murine macrophages leading to divergent biological outcomes. J Immunol 1995; 154:871-880.
    • (1995) J Immunol , vol.154 , pp. 871-880
    • Wrenshall, L.E.1    Cerra, F.B.2    Singh, R.K.3    Platt, J.L.4
  • 235
    • 0036883487 scopus 로고    scopus 로고
    • Biosynthesis and properties of the plant cell wall
    • Reiter, W. D.,Biosynthesis and properties of the plant cell wall. Curr Opin Plant Biol 2002; 5(6):536-542.
    • (2002) Curr Opin Plant Biol , vol.5 , Issue.6 , pp. 536-542
    • Reiter, W.D.1
  • 236
    • 0028721071 scopus 로고
    • Oligosaccharins: Structures and signal transduction
    • Cote, F., and Hahn, M. G., Oligosaccharins: structures and signal transduction. Plant Mol Biol 1994; 26:1379-1411.
    • (1994) Plant Mol Biol , vol.26 , pp. 1379-1411
    • Cote, F.1    Hahn, M.G.2
  • 237
    • 0028923697 scopus 로고
    • Diphosphoryl lipid A from Rbodobacter sphaeroides transiently activates NF-kappa B but inhibits lipopolysaccharide induction of kappa light chain and Oct-2 in the B-cell lymphoma line 70Z/3
    • Lawrence, O., Rachie, N., Qureshi, N., Bomsztyk, K., and Sibley, C. H., Diphosphoryl lipid A from Rbodobacter sphaeroides transiently activates NF-kappa B but inhibits lipopolysaccharide induction of kappa light chain and Oct-2 in the B-cell lymphoma line 70Z/3. Infect Immun 1995; 63:1040-1046.
    • (1995) Infect Immun , vol.63 , pp. 1040-1046
    • Lawrence, O.1    Rachie, N.2    Qureshi, N.3    Bomsztyk, K.4    Sibley, C.H.5
  • 238
    • 0030857849 scopus 로고    scopus 로고
    • Diphosphoryl lipid A from Rhodobacter sphaeroides inhibits complexes that form in vitro between lipopolysaccharide (LPS)-binding protein, soluble CD14, and spectrally pure LPS
    • Jarvis, B. W., Lichenstein, H., and Qureshi, N., Diphosphoryl lipid A from Rhodobacter sphaeroides inhibits complexes that form in vitro between lipopolysaccharide (LPS)-binding protein, soluble CD14, and spectrally pure LPS. Infect Immun 1997; 65:3011-3016.
    • (1997) Infect Immun , vol.65 , pp. 3011-3016
    • Jarvis, B.W.1    Lichenstein, H.2    Qureshi, N.3
  • 239
    • 0034610291 scopus 로고    scopus 로고
    • The repertoire for partern recognition of pathogens by the innate immune system is defined by cooperation between Toll-like receptors
    • Ozinsky, A., Underhill, D. M., Fontenot, J. D., Hajjar, A. M., Smith, K. D., Wilson, C. B., Schroeder, L., and Aderem, A.,The repertoire for partern recognition of pathogens by the innate immune system is defined by cooperation between Toll-like receptors. Proc Natl Acad Sci U S A 2000; 97(25):13766-13771.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.25 , pp. 13766-13771
    • Ozinsky, A.1    Underhill, D.M.2    Fontenot, J.D.3    Hajjar, A.M.4    Smith, K.D.5    Wilson, C.B.6    Schroeder, L.7    Aderem, A.8
  • 240
  • 241
    • 0036644042 scopus 로고    scopus 로고
    • Cutting edge: Role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins
    • Takeuchi, O., Sato, S., Horiuchi, T., Hoshino, K., Takeda, K., Dong, Z., Modlin, R. L., and Akira, S., Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins. J Immunol 2002; 169(1):10-14.
    • (2002) J Immunol , vol.169 , Issue.1 , pp. 10-14
    • Takeuchi, O.1    Sato, S.2    Horiuchi, T.3    Hoshino, K.4    Takeda, K.5    Dong, Z.6    Modlin, R.L.7    Akira, S.8
  • 243
    • 0036828922 scopus 로고    scopus 로고
    • Regions of the mouse CD14 molecule required for Toll-like receptor 2- and 4-mediated activation of NF-kappa B
    • Muroi, M., Ohnishi, T., and Tanamoto, K., Regions of the mouse CD14 molecule required for Toll-like receptor 2- and 4-mediated activation of NF-kappa B. J Biol Chem 2002; 277(44):42372-42379.
    • (2002) J Biol Chem , vol.277 , Issue.44 , pp. 42372-42379
    • Muroi, M.1    Ohnishi, T.2    Tanamoto, K.3
  • 244
    • 0015211527 scopus 로고
    • Plant antitumor agents. VI. Isolation and structure of taxol, a novel antileukemic and antitumor agen from Taxus brevifolia
    • Wani, M. C., Taylor, H. L., Wall, M. E., Coggon, P., and McPhail, A. T., Plant antitumor agents. VI. Isolation and structure of taxol, a novel antileukemic and antitumor agen from Taxus brevifolia. J Am Chem Soc 1971; 93(9):2325-2327.
    • (1971) J Am Chem Soc , vol.93 , Issue.9 , pp. 2325-2327
    • Wani, M.C.1    Taylor, H.L.2    Wall, M.E.3    Coggon, P.4    McPhail, A.T.5
  • 247
    • 0030761974 scopus 로고    scopus 로고
    • Epothilone B stabilizes microtubuli of macrophages like taxol without showing taxol-like endotoxin activity
    • Muhlradt, P. F., and Sasse, F., Epothilone B stabilizes microtubuli of macrophages like taxol without showing taxol-like endotoxin activity. Cancer Res 1997; 57(16):3344-3346.
    • (1997) Cancer Res , vol.57 , Issue.16 , pp. 3344-3346
    • Muhlradt, P.F.1    Sasse, F.2
  • 248
    • 0034723186 scopus 로고    scopus 로고
    • Mouse Toll-like receptor 4. MD-2 complex mediates lipopolysaccharidemimetic signal transduction by Taxol
    • Kawasaki, K., Akashi, S., Shimazu, R., Yoshida, T., Miyake, K., and Nishijima, M., Mouse Toll-like receptor 4. MD-2 complex mediates lipopolysaccharidemimetic signal transduction by Taxol. J Biol Chem 2000; 275:2251-2254.
    • (2000) J Biol Chem , vol.275 , pp. 2251-2254
    • Kawasaki, K.1    Akashi, S.2    Shimazu, R.3    Yoshida, T.4    Miyake, K.5    Nishijima, M.6
  • 249
    • 0028906579 scopus 로고
    • CD14 is not involved in Rhodobacter sphaeroides diphosphoryl lipid A inhibition of tumor necrosis factor alpha and nitric oxide induction by taxol in murine macrophages
    • Kirikae, F., Kirikae, T., Qureshi, N., Takayama, K., Morrison, D. C., and Nakano, M., CD14 is not involved in Rhodobacter sphaeroides diphosphoryl lipid A inhibition of tumor necrosis factor alpha and nitric oxide induction by taxol in murine macrophages. Infect Immun 1995; 63:486-497.
    • (1995) Infect Immun , vol.63 , pp. 486-497
    • Kirikae, F.1    Kirikae, T.2    Qureshi, N.3    Takayama, K.4    Morrison, D.C.5    Nakano, M.6
  • 250
    • 0033564270 scopus 로고    scopus 로고
    • Use of a photoactivatable taxol analogue to identify unique cellular targets in murine macrophages: Identification of murine CD18 as a major taxol-binding protein and a role for Mac-1 in taxol-induced gene expression
    • Bhat, N., Perera, P. Y., Carboni, J. M., Blanco, J., Golenbock, D. T., Mayadas, T. N., and Vogel, S. N., Use of a photoactivatable taxol analogue to identify unique cellular targets in murine macrophages: identification of murine CD18 as a major taxol-binding protein and a role for Mac-1 in taxol-induced gene expression. J Immunol 1999; 162(12):7335-7342.
    • (1999) J Immunol , vol.162 , Issue.12 , pp. 7335-7342
    • Bhat, N.1    Perera, P.Y.2    Carboni, J.M.3    Blanco, J.4    Golenbock, D.T.5    Mayadas, T.N.6    Vogel, S.N.7
  • 251
    • 0034746813 scopus 로고    scopus 로고
    • Cutting edge: Gln22 of mouse MD-2 is essential for species-specific lipopolysaccharide mimetic action of taxol
    • Kawasaki, K., Gomi, K., and Nishijima, M., Cutting edge: Gln22 of mouse MD-2 is essential for species-specific lipopolysaccharide mimetic action of taxol. J Immunol 2001; 166:11-14.
    • (2001) J Immunol , vol.166 , pp. 11-14
    • Kawasaki, K.1    Gomi, K.2    Nishijima, M.3
  • 252
    • 0034834474 scopus 로고    scopus 로고
    • Involvement of TLR4/MD-2 complex in species-specific lipopolysaccharide mimetic signal transduction by Taxol
    • Kawasaki, K., Akashi, S., Shimazu, R., Yoshida, T., Miyake, K., and Nishijima, M., Involvement of TLR4/MD-2 complex in species-specific lipopolysaccharide mimetic signal transduction by Taxol. J Endotoxin Res 2001; 7(3):232-236.
    • (2001) J Endotoxin Res , vol.7 , Issue.3 , pp. 232-236
    • Kawasaki, K.1    Akashi, S.2    Shimazu, R.3    Yoshida, T.4    Miyake, K.5    Nishijima, M.6
  • 253
    • 0037087255 scopus 로고    scopus 로고
    • Toll-like receptor 4-M.D-2 complex mediates the signal transduction induced by flavoepin, an amino acid-containing lipid unique to Flavobacterium meningosepticum
    • Gomi, K., Kawasaki, K., Kawai, Y., Shiozaki, M., and Nishijima, M., Toll-like receptor 4-M.D-2 complex mediates the signal transduction induced by flavoepin, an amino acid-containing lipid unique to Flavobacterium meningosepticum. J Immunol 2002; 168(6):2939-2943.
    • (2002) J Immunol , vol.168 , Issue.6 , pp. 2939-2943
    • Gomi, K.1    Kawasaki, K.2    Kawai, Y.3    Shiozaki, M.4    Nishijima, M.5
  • 254
    • 0031713365 scopus 로고    scopus 로고
    • Fibronectin-structure, assembly, and cardiovasular implications
    • Magnusson, M. K., and Mosher, D. F., Fibronectin-structure, assembly, and cardiovasular implications. Arteriosder Thromb Vasc Biol 1998; 18:1363-1370.
    • (1998) Arteriosder Thromb Vasc Biol , vol.18 , pp. 1363-1370
    • Magnusson, M.K.1    Mosher, D.F.2
  • 255
    • 0034681420 scopus 로고    scopus 로고
    • Elucidation of the structural features of heparan sulfate important for interaction with the Hep-2 domain of fibronectin
    • Lyon, M., Rushton, G., Askari, J. A., Humphries, M.J., and Gallagher, J. T., Elucidation of the structural features of heparan sulfate important for interaction with the Hep-2 domain of fibronectin. J Biol Chem 2000; 275(7):4599-4606.
    • (2000) J Biol Chem , vol.275 , Issue.7 , pp. 4599-4606
    • Lyon, M.1    Rushton, G.2    Askari, J.A.3    Humphries, M.J.4    Gallagher, J.T.5
  • 258
    • 0037290892 scopus 로고    scopus 로고
    • Drosophila immunity: Paths and patterns
    • Hultmark, D., Drosophila immunity: paths and patterns. Curr Opin Immunol 2003; 15(1):12-19.
    • (2003) Curr Opin Immunol , vol.15 , Issue.1 , pp. 12-19
    • Hultmark, D.1
  • 259
    • 0032033030 scopus 로고    scopus 로고
    • Proteolytic processing of the Drosophila Spatzle protein by easter generates a dimeric NGF-like molecule with ventralising activity
    • DeLotto, Y., and DeLotto, R., Proteolytic processing of the Drosophila Spatzle protein by easter generates a dimeric NGF-like molecule with ventralising activity. Mech Dev 1998; 72(1-2):141-148.
    • (1998) Mech Dev , vol.72 , Issue.1-2 , pp. 141-148
    • DeLotto, Y.1    DeLotto, R.2
  • 260
    • 0033973826 scopus 로고    scopus 로고
    • Signaling mechanisms in the antimicrobial host defense of Drosophila
    • Imler, J. L., and Hoffmann, J. A., Signaling mechanisms in the antimicrobial host defense of Drosophila. Curr Opin Microbiol 2000; 3(1):16-22.
    • (2000) Curr Opin Microbiol , vol.3 , Issue.1 , pp. 16-22
    • Imler, J.L.1    Hoffmann, J.A.2
  • 261
    • 0033578917 scopus 로고    scopus 로고
    • Constitutive activation of Toll-mediated antifungal defense in serpin-deficient Drosophila
    • Levashina, E. A., Langley, E., Green, C., Gubb, D., Ashburner, M., Hoffmann, J. A., and Reichhart, J. M., Constitutive activation of Toll-mediated antifungal defense in serpin-deficient Drosophila. Science 1999; 285(5435):1917-1919.
    • (1999) Science , vol.285 , Issue.5435 , pp. 1917-1919
    • Levashina, E.A.1    Langley, E.2    Green, C.3    Gubb, D.4    Ashburner, M.5    Hoffmann, J.A.6    Reichhart, J.M.7
  • 262
    • 0037458713 scopus 로고    scopus 로고
    • Characterization of the necrotic protein that regulates the Toll-mediated immune response in Drosophila
    • Robertson, A. S., Belorgey, D., Lilley, K. S., Lomas, D. A., Gubb, D., and Daffom, T. R., Characterization of the necrotic protein that regulates the Toll-mediated immune response in Drosophila. J Biol Chem 2002; 278:6175-6180.
    • (2002) J Biol Chem , vol.278 , pp. 6175-6180
    • Robertson, A.S.1    Belorgey, D.2    Lilley, K.S.3    Lomas, D.A.4    Gubb, D.5    Daffom, T.R.6
  • 263
    • 0033762437 scopus 로고    scopus 로고
    • The necrotic gene in Drosophila corresponds to one of a cluster of three serpin transcripts mapping at 43A1.2
    • Green, C., Levashina, E., McKimmie, C., Dafforn, T., Reichhart, J. M., and Gubb, D., The necrotic gene in Drosophila corresponds to one of a cluster of three serpin transcripts mapping at 43A1.2. Genetics 2000; 156(3):1117-1127.
    • (2000) Genetics , vol.156 , Issue.3 , pp. 1117-1127
    • Green, C.1    Levashina, E.2    McKimmie, C.3    Dafforn, T.4    Reichhart, J.M.5    Gubb, D.6
  • 264
    • 0034523345 scopus 로고    scopus 로고
    • Phylogeny of the serpin superfamily: Implications of patterns of amino acid conservation for structure and function
    • Irving, J. A., Pike, R. N., Lesk, A. M., and Whisstock, J. C., Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. Genome Res 2000; 10(12):1845-1864.
    • (2000) Genome Res , vol.10 , Issue.12 , pp. 1845-1864
    • Irving, J.A.1    Pike, R.N.2    Lesk, A.M.3    Whisstock, J.C.4
  • 265
    • 0037025213 scopus 로고    scopus 로고
    • Activation of Drosophila Toll during fungal infection by a blood serine protease
    • Ligoxygakis, P., Pelte, N., Hoffmann, J. A., and Reichhart, J. M., Activation of Drosophila Toll during fungal infection by a blood serine protease. Science 2002; 297(5578):114-116.
    • (2002) Science , vol.297 , Issue.5578 , pp. 114-116
    • Ligoxygakis, P.1    Pelte, N.2    Hoffmann, J.A.3    Reichhart, J.M.4
  • 266
    • 0035856990 scopus 로고    scopus 로고
    • Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein
    • Michel, T., Reichhart, J. M., Hoffmann, J. A., and Royet, J., Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein. Nature 2001; 414(6865):756-759.
    • (2001) Nature , vol.414 , Issue.6865 , pp. 756-759
    • Michel, T.1    Reichhart, J.M.2    Hoffmann, J.A.3    Royet, J.4
  • 267
    • 0028785577 scopus 로고
    • Role of the integument in insect defense: Pro-phenol oxidase cascade in the cuticular matrix
    • Ashida, M., and Brey, P. T., Role of the integument in insect defense: pro-phenol oxidase cascade in the cuticular matrix. Proc Nad Acad Sci U S A 1995; 92(23):10698-10702.
    • (1995) Proc Nad Acad Sci U S A , vol.92 , Issue.23 , pp. 10698-10702
    • Ashida, M.1    Brey, P.T.2
  • 268
    • 0034019343 scopus 로고    scopus 로고
    • Cytotoxicity and cytotoxic molecules in invertebrates
    • Nappi, A. J., and Ottaviani, E., Cytotoxicity and cytotoxic molecules in invertebrates. Bioessays 2000; 22(5):469-480.
    • (2000) Bioessays , vol.22 , Issue.5 , pp. 469-480
    • Nappi, A.J.1    Ottaviani, E.2
  • 269
    • 0029884417 scopus 로고    scopus 로고
    • Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori
    • Yoshida, H., Kinoshita, K., and Ashida, M., Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori. J Biol Chem 1996; 271(23):13854-13860.
    • (1996) J Biol Chem , vol.271 , Issue.23 , pp. 13854-13860
    • Yoshida, H.1    Kinoshita, K.2    Ashida, M.3
  • 270
    • 0033166017 scopus 로고    scopus 로고
    • Immulectin, an inducible C-type lectin from an insect, Manduca sexta, stimulates activation of plasma prophenol oxidase
    • Yu, X. Q:., Gan, H., and Kanost, M. R., Immulectin, an inducible C-type lectin from an insect, Manduca sexta, stimulates activation of plasma prophenol oxidase. Insect Biochem Mol Biol 1999; 29(7):585-597.
    • (1999) Insect Biochem Mol Biol , vol.29 , Issue.7 , pp. 585-597
    • Yu, X.Q.1    Gan, H.2    Kanost, M.R.3
  • 271
    • 0034677596 scopus 로고    scopus 로고
    • A beta1,3-glucan recognition protein from an insect, Manduca sexta, agglutinates microorganisms and activates the phenoloxidase cascade
    • Ma, C., and Kanost, M. R., A beta1,3-glucan recognition protein from an insect, Manduca sexta, agglutinates microorganisms and activates the phenoloxidase cascade. J Biol Chem 2000; 275(11):7505-7514.
    • (2000) J Biol Chem , vol.275 , Issue.11 , pp. 7505-7514
    • Ma, C.1    Kanost, M.R.2
  • 272
    • 0033597134 scopus 로고    scopus 로고
    • A pattern recognition protein for peptidoglycan. Cloning the cDNA and the gene of the silkworm, Bombyx mori
    • Ochiai, M., and Ashida, M., A pattern recognition protein for peptidoglycan. Cloning the cDNA and the gene of the silkworm, Bombyx mori. J Biol Chem 1999; 274(17):11854-11858.
    • (1999) J Biol Chem , vol.274 , Issue.17 , pp. 11854-11858
    • Ochiai, M.1    Ashida, M.2
  • 275
    • 0034913274 scopus 로고    scopus 로고
    • Drosophila immunity: Two paths to NF-kappaB
    • Khush, R. S., Leulier, F., and Lemaitre, B., Drosophila immunity: two paths to NF-kappaB. Trends Immunol 2001; 22(5):260-264.
    • (2001) Trends Immunol , vol.22 , Issue.5 , pp. 260-264
    • Khush, R.S.1    Leulier, F.2    Lemaitre, B.3
  • 278
    • 0037061450 scopus 로고    scopus 로고
    • The Drosophila immune response against Gramnegative bacteria is mediated by a peptidoglycan recognition protein
    • Gottar, M., Gobert, V., Michel, T., Belvin, M., Duyk, G., Hoffmann, J. A., Ferrandon, D., and Royet, J., The Drosophila immune response against Gramnegative bacteria is mediated by a peptidoglycan recognition protein. Nature 2002; 416(6881):640-644.
    • (2002) Nature , vol.416 , Issue.6881 , pp. 640-644
    • Gottar, M.1    Gobert, V.2    Michel, T.3    Belvin, M.4    Duyk, G.5    Hoffmann, J.A.6    Ferrandon, D.7    Royet, J.8
  • 279
    • 0037066464 scopus 로고    scopus 로고
    • Requirement for a peptidoglycan recognition protein (PGRP) in relish activation and antibacterial immune responses in Drosophila
    • Choe, K. M., Werner, T., Stoven, S., Hultmark, D., and Anderson, K. V., Requirement for a peptidoglycan recognition protein (PGRP) in relish activation and antibacterial immune responses in Drosophila. Science 2002; 296(5566):359-362.
    • (2002) Science , vol.296 , Issue.5566 , pp. 359-362
    • Choe, K.M.1    Werner, T.2    Stoven, S.3    Hultmark, D.4    Anderson, K.V.5
  • 280
    • 0037061482 scopus 로고    scopus 로고
    • Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli
    • Ramet, M., Manfruelli, P., Pearson,A., Mathey-Prevot, B., and Ezekowitz, R. A., Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature 2002; 416(6881):644-648.
    • (2002) Nature , vol.416 , Issue.6881 , pp. 644-648
    • Ramet, M.1    Manfruelli, P.2    Pearson, A.3    Mathey-Prevot, B.4    Ezekowitz, R.A.5
  • 281
    • 0031281940 scopus 로고    scopus 로고
    • Antimicrobial peptide defense in Drosophila
    • Meister, M., Lemaitre, B., and Hoffmann, J. A., Antimicrobial peptide defense in Drosophila. Bioessays 1997; 19(11):1019-1026.
    • (1997) Bioessays , vol.19 , Issue.11 , pp. 1019-1026
    • Meister, M.1    Lemaitre, B.2    Hoffmann, J.A.3
  • 282
    • 0037133259 scopus 로고    scopus 로고
    • Constitutive expression of a single antimicrobial peptide can restore wild-type resistance to infection in immunodeficient Drosophila mutants
    • Tzou, P., Reichhart, J. M., and Lemaitre, B., Constitutive expression of a single antimicrobial peptide can restore wild-type resistance to infection in immunodeficient Drosophila mutants. Proc Natl Acad Sci U S A 2002; 99(4):2152-2157.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.4 , pp. 2152-2157
    • Tzou, P.1    Reichhart, J.M.2    Lemaitre, B.3
  • 283
    • 0028278901 scopus 로고
    • Ventralizing signal determined by protease activation in Drosophila embryogenesis
    • Smith, C. L., and DeLotto, R., Ventralizing signal determined by protease activation in Drosophila embryogenesis. Nature 1994; 368(6471):548-551.
    • (1994) Nature , vol.368 , Issue.6471 , pp. 548-551
    • Smith, C.L.1    DeLotto, R.2
  • 284
    • 0032515119 scopus 로고    scopus 로고
    • Pinning down positional information: Dorsal-ventral polarity in the Drosophila embryo
    • Anderson, K. V., Pinning down positional information: dorsal-ventral polarity in the Drosophila embryo. Cell 1998; 95(4):439-442.
    • (1998) Cell , vol.95 , Issue.4 , pp. 439-442
    • Anderson, K.V.1
  • 285
    • 0028182623 scopus 로고
    • A processed form of the Spatzle protein defines dorsal-ventral polarity in the Drosophila embryo
    • Schneider, D. S., Jin, Y., Morisato, D., and Anderson, K. V., A processed form of the Spatzle protein defines dorsal-ventral polarity in the Drosophila embryo. Development 1994; 120(5):1243-1250.
    • (1994) Development , vol.120 , Issue.5 , pp. 1243-1250
    • Schneider, D.S.1    Jin, Y.2    Morisato, D.3    Anderson, K.V.4
  • 286
    • 0028167111 scopus 로고
    • The spatzle gene encodes a component of the extracellular signaling pathway establishing the dorsal-ventral pattern of the Drosophila embryo
    • Morisato, D., and Anderson, K. V., The spatzle gene encodes a component of the extracellular signaling pathway establishing the dorsal-ventral pattern of the Drosophila embryo. Cell 1994; 76(4):677-688.
    • (1994) Cell , vol.76 , Issue.4 , pp. 677-688
    • Morisato, D.1    Anderson, K.V.2
  • 287
    • 0033106265 scopus 로고    scopus 로고
    • Signal transduction by a protease cascade
    • LeMosy, E. K., Hong, C. C., and Hashimoto, C., Signal transduction by a protease cascade. Trends Cell Biol 1999; 9(3):102-107.
    • (1999) Trends Cell Biol , vol.9 , Issue.3 , pp. 102-107
    • LeMosy, E.K.1    Hong, C.C.2    Hashimoto, C.3
  • 288
    • 0034641738 scopus 로고    scopus 로고
    • From the cover: Toll-related receptors and the control of antimicrobial peptide expression in Drosophila
    • Tauszig, S., Jouanguy, E., Hoffmann, J. A., and Imler, J. L., From the cover: Toll-related receptors and the control of antimicrobial peptide expression in Drosophila, Proc Natl Acad Sci U S A 2000; 97 (19):10520-10525.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.19 , pp. 10520-10525
    • Tauszig, S.1    Jouanguy, E.2    Hoffmann, J.A.3    Imler, J.L.4
  • 289
    • 0030663332 scopus 로고    scopus 로고
    • The 18-wheeler mutation reveals complex antibacterial gene regulation in Drosophila host defense
    • Williams, M. J., Rodriguez, A., Kimbrell, D. A., and Eldon, E. D., The 18-wheeler mutation reveals complex antibacterial gene regulation in Drosophila host defense. EMBO J 1997; 16:6120-6130.
    • (1997) EMBO J , vol.16 , pp. 6120-6130
    • Williams, M.J.1    Rodriguez, A.2    Kimbrell, D.A.3    Eldon, E.D.4
  • 290
    • 0023024217 scopus 로고
    • A gene required for the specification of dorsal-ventral pattern in Drosophila appears to encode a serine protease
    • DeLotto, R., and Spierer, P., A gene required for the specification of dorsal-ventral pattern in Drosophila appears to encode a serine protease. Nature 1986; 323 (6090):688-692.
    • (1986) Nature , vol.323 , Issue.6090 , pp. 688-692
    • DeLotto, R.1    Spierer, P.2
  • 291
    • 0024965999 scopus 로고
    • The role of easter, an apparent serine protease, in organizing the dorsalventral pattern of the Drosophila embryo
    • Chasan, R., and Anderson, K. V., The role of easter, an apparent serine protease, in organizing the dorsalventral pattern of the Drosophila embryo. Cell 1989; 56(3):391-400.
    • (1989) Cell , vol.56 , Issue.3 , pp. 391-400
    • Chasan, R.1    Anderson, K.V.2
  • 292
    • 0032499717 scopus 로고    scopus 로고
    • The gastrulation defective gene of Drosophila melanogaster is a member of the serine protease superfamily
    • Konrad, K. D., Goralski, T. J., Mahowald, A. P., and Marsh, J. L., The gastrulation defective gene of Drosophila melanogaster is a member of the serine protease superfamily. Proc Natl Acad Sci U S A 1998; 95(12):6819-6824.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.12 , pp. 6819-6824
    • Konrad, K.D.1    Goralski, T.J.2    Mahowald, A.P.3    Marsh, J.L.4
  • 293
    • 0024292694 scopus 로고
    • The molecular basis of blood coagulation
    • Furie, B., and Furie, B. C., The molecular basis of blood coagulation. Cell 1988; 53(4):505-518.
    • (1988) Cell , vol.53 , Issue.4 , pp. 505-518
    • Furie, B.1    Furie, B.C.2
  • 294
    • 0028109290 scopus 로고
    • Membrane-dependent reactions in blood coagulation: Role of the vitamin K-dependent enzyme complexes
    • Kalafatis, M., Swords, N. A., Rand, M. D., and Mann, K. G., Membrane-dependent reactions in blood coagulation: role of the vitamin K-dependent enzyme complexes, Biochim Biophys Acta 1994; 1227(3):113-129.
    • (1994) Biochim Biophys Acta , vol.1227 , Issue.3 , pp. 113-129
    • Kalafatis, M.1    Swords, N.A.2    Rand, M.D.3    Mann, K.G.4
  • 295
    • 0027509462 scopus 로고
    • Glycosaminoglycans and the regulation of blood coagulation
    • Bourin, M. C., and Lindahl, U., Glycosaminoglycans and the regulation of blood coagulation. Biochem J 1993; 289(Pt 2):313-330.
    • (1993) Biochem J , vol.289 , Issue.PART 2 , pp. 313-330
    • Bourin, M.C.1    Lindahl, U.2
  • 296
    • 0031924060 scopus 로고    scopus 로고
    • Positive and negative regulation of Easter, a member of the serine protease family that controls dorsal-ventral patterningin the Drosophila embryo
    • Misra, S., Hecht, P., Maeda, R., and Anderson, K. V., Positive and negative regulation of Easter, a member of the serine protease family that controls dorsal-ventral patterningin the Drosophila embryo. Development 1998; 125(7):1261-1267.
    • (1998) Development , vol.125 , Issue.7 , pp. 1261-1267
    • Misra, S.1    Hecht, P.2    Maeda, R.3    Anderson, K.V.4
  • 297
    • 0035941066 scopus 로고    scopus 로고
    • The serine protease inhibitor antithrombin III inhibits LPS-mediated NF-kappaB activation by TLR-4
    • Mansell, A., Reinicke, A., Worrall, D. M., and O'Neill, L. A., The serine protease inhibitor antithrombin III inhibits LPS-mediated NF-kappaB activation by TLR-4. FEBS Lett 2001; 508(3):313-317.
    • (2001) FEBS Lett , vol.508 , Issue.3 , pp. 313-317
    • Mansell, A.1    Reinicke, A.2    Worrall, D.M.3    O'Neill, L.A.4
  • 298
    • 0035451118 scopus 로고    scopus 로고
    • Fibrinogen stimulates macrophage chemokine secretion through Toll-like receptor 4
    • Smiley, S. T., King, J. A., and Hancock, W. W., Fibrinogen stimulates macrophage chemokine secretion through Toll-like receptor 4. J Immunol 2001; 167:2887-2894.
    • (2001) J Immunol , vol.167 , pp. 2887-2894
    • Smiley, S.T.1    King, J.A.2    Hancock, W.W.3
  • 299
    • 0036138426 scopus 로고    scopus 로고
    • Coagulation inhibitors in the treatment of sepsis
    • Freeman, B. D., and Buchman, T. G., Coagulation inhibitors in the treatment of sepsis. Exp Opin Invest Drugs 2002; 11(1):69-74.
    • (2002) Exp Opin Invest Drugs , vol.11 , Issue.1 , pp. 69-74
    • Freeman, B.D.1    Buchman, T.G.2
  • 300
    • 0036266019 scopus 로고    scopus 로고
    • TLR4-dependent lipopolysaccharide signalling in epithelial cells is independent of extracellular protease activity
    • Backhed, F., Normark, S., and Richter-Dahlfors, A., TLR4-dependent lipopolysaccharide signalling in epithelial cells is independent of extracellular protease activity. Cell Microbiol 2002; 4(5):297-303.
    • (2002) Cell Microbiol , vol.4 , Issue.5 , pp. 297-303
    • Backhed, F.1    Normark, S.2    Richter-Dahlfors, A.3
  • 301
    • 0035877013 scopus 로고    scopus 로고
    • An essential role of the NF-kappa B/Toll-like receptor pathway in induction of inflammatory and tissue-repair gene expression by necrotic cells
    • Li, M., Carpio, D. F., Zheng, Y., Bruzzo, P., Singh, V., Ouaaz, F., Medzhitov, R. M., and Beg, A. A., An essential role of the NF-kappa B/Toll-like receptor pathway in induction of inflammatory and tissue-repair gene expression by necrotic cells. J Immunol 2001; 166:7128-7135.
    • (2001) J Immunol , vol.166 , pp. 7128-7135
    • Li, M.1    Carpio, D.F.2    Zheng, Y.3    Bruzzo, P.4    Singh, V.5    Ouaaz, F.6    Medzhitov, R.M.7    Beg, A.A.8
  • 302
    • 0036453356 scopus 로고    scopus 로고
    • TLR2: Cellular sensor for microbial and endogenous molecular patterns
    • Kirschning, C. J., and Schumann, R. R., TLR2: cellular sensor for microbial and endogenous molecular patterns. Curr Top Microbiol Immunol 2002; 270:121-144.
    • (2002) Curr Top Microbiol Immunol , vol.270 , pp. 121-144
    • Kirschning, C.J.1    Schumann, R.R.2
  • 303
    • 0034650427 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex
    • Ohashi, K., Burkart, V., Flohe, S., and Kolb, H., Cutting edge: heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex. J Immunol 2000; 164:558-561.
    • (2000) J Immunol , vol.164 , pp. 558-561
    • Ohashi, K.1    Burkart, V.2    Flohe, S.3    Kolb, H.4
  • 304
    • 0035903158 scopus 로고    scopus 로고
    • Endocytosed HSP60s use Toll-like receptor 2 (TLR2) and TLR4 to activate the Toll/interleukin-1 receptor signaling pathway in innate immune cells
    • Vabulas, R. M., Ahmad-Nejad, P., da Costa, C., Miethke, T., Kirschning, C. J., Hacker, H., and Wagner, H., Endocytosed HSP60s use Toll-like receptor 2 (TLR2) and TLR4 to activate the Toll/interleukin-1 receptor signaling pathway in innate immune cells. J Biol Chem 2001; 276(33):31332-31339.
    • (2001) J Biol Chem , vol.276 , Issue.33 , pp. 31332-31339
    • Vabulas, R.M.1    Ahmad-Nejad, P.2    Da Costa, C.3    Miethke, T.4    Kirschning, C.J.5    Hacker, H.6    Wagner, H.7
  • 306
    • 0037177825 scopus 로고    scopus 로고
    • Novel signal transduction pathway utilized by extracellular HSP70: Role of Toll-like receptor (TLR) 2 and TLR4
    • Asea, A., Rehli, M., Kabingu, E., Boch, J. A., Bare, O., Auron, P. E., Stevenson, M. A., and Calderwood, S. K., Novel signal transduction pathway utilized by extracellular HSP70: role of Toll-like receptor (TLR) 2 and TLR4. J Biol Chem 2002; 277(17):15028-15034.
    • (2002) J Biol Chem , vol.277 , Issue.17 , pp. 15028-15034
    • Asea, A.1    Rehli, M.2    Kabingu, E.3    Boch, J.A.4    Bare, O.5    Auron, P.E.6    Stevenson, M.A.7    Calderwood, S.K.8
  • 307
    • 0034795208 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
    • Randow, F., and Seed, B., Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. Nat Cell Biol 2001; 3(10):891-896.
    • (2001) Nat Cell Biol , vol.3 , Issue.10 , pp. 891-896
    • Randow, F.1    Seed, B.2
  • 308
    • 0036512501 scopus 로고    scopus 로고
    • An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response
    • Li, Z., Dai, J., Zheng, H., Liu, B., and Caudill, M., An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response. Front Biosci 2002; 7:731-751.
    • (2002) Front Biosci , vol.7 , pp. 731-751
    • Li, Z.1    Dai, J.2    Zheng, H.3    Liu, B.4    Caudill, M.5
  • 309
    • 0036452764 scopus 로고    scopus 로고
    • Heat shock proteins as ligands of Toll-like receptors
    • Vabulas, R. M., Wagner, H., and Schild, H., Heat shock proteins as ligands of Toll-like receptors. Curr Top Microbiol Immunol 2002; 270:169-184.
    • (2002) Curr Top Microbiol Immunol , vol.270 , pp. 169-184
    • Vabulas, R.M.1    Wagner, H.2    Schild, H.3
  • 310
    • 0035113012 scopus 로고    scopus 로고
    • Unraveling the mechanisms by which heat shock proteins activate the immune system
    • Palliser, D., Unraveling the mechanisms by which heat shock proteins activate the immune system. Curr Opin Mol Ther 2001; 3(1):25-30.
    • (2001) Curr Opin Mol Ther , vol.3 , Issue.1 , pp. 25-30
    • Palliser, D.1
  • 312
    • 0037414787 scopus 로고    scopus 로고
    • Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor alpha release by murine macrophages
    • Gao, B., and Tsan, M. F., Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor alpha release by murine macrophages, J Biol Chem 2003; 278(1):174-179.
    • (2003) J Biol Chem , vol.278 , Issue.1 , pp. 174-179
    • Gao, B.1    Tsan, M.F.2
  • 314
    • 0032734313 scopus 로고    scopus 로고
    • Expression and regulation of the human beta-defensins hBD-1 and hBD-2 in intestinal epithelium
    • O'Neil, D. A., Porter, E. M., Elewaut, D., Anderson, G. M., Eckmann, L., Ganz, T., and Kagnoff, M. F., Expression and regulation of the human beta-defensins hBD-1 and hBD-2 in intestinal epithelium. J Immunol 1999; 163(12):6718-6724.
    • (1999) J Immunol , vol.163 , Issue.12 , pp. 6718-6724
    • O'Neil, D.A.1    Porter, E.M.2    Elewaut, D.3    Anderson, G.M.4    Eckmann, L.5    Ganz, T.6    Kagnoff, M.F.7
  • 315
    • 0027474382 scopus 로고
    • Defensins: Antimicrobial and cytotoxic peptides of mammalian cells
    • Lehrer, R. I., Lichtenstein, A. K., and Ganz, T., Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu Rev Immunol 1993; 11:105-128.
    • (1993) Annu Rev Immunol , vol.11 , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 316
    • 0036467390 scopus 로고    scopus 로고
    • Defensins of vertebrate animals
    • Lehrer, R. I., and Ganz, T., Defensins of vertebrate animals. Curr Opin Immunol 2002; 14(1):96-102.
    • (2002) Curr Opin Immunol , vol.14 , Issue.1 , pp. 96-102
    • Lehrer, R.I.1    Ganz, T.2
  • 320
    • 0037097672 scopus 로고    scopus 로고
    • Cutting edge: The immunostimulatory activity of the lung surfactant protein-A involves Toll-like receptor 4
    • Guillot, L., Balloy V., McCorrnack, F.X., Golenbock, D. T., Chignard, M., and Si-Tahar, M., Cutting edge: the immunostimulatory activity of the lung surfactant protein-A involves Toll-like receptor 4. J Immunol 2002; 168(12):5989-5992.
    • (2002) J Immunol , vol.168 , Issue.12 , pp. 5989-5992
    • Guillot, L.1    Balloy, V.2    McCorrnack, F.X.3    Golenbock, D.T.4    Chignard, M.5    Si-Tahar, M.6
  • 321
    • 0034979340 scopus 로고    scopus 로고
    • The role of surfactant-associated protein A in pulmonary host defense
    • Shepherd, V. L., and Lopez, J. P., The role of surfactant-associated protein A in pulmonary host defense. Immunol Res 2001; 23(2-3):111-120.
    • (2001) Immunol Res , vol.23 , Issue.2-3 , pp. 111-120
    • Shepherd, V.L.1    Lopez, J.P.2
  • 322
    • 0034973011 scopus 로고    scopus 로고
    • Surfactant regulation of host defense function in the lung: A question of balance
    • Phelps, D. S., Surfactant regulation of host defense function in the lung: a question of balance. Pediatr Pathol Mol Med 2001; 20(4):269-292.
    • (2001) Pediatr Pathol Mol Med , vol.20 , Issue.4 , pp. 269-292
    • Phelps, D.S.1
  • 323
    • 0033168699 scopus 로고    scopus 로고
    • Pulmonary surfactant protein A modulates the cellular response to smooth and rough lipopolysaccharides by interaction with CD14
    • Sano, H., Sohma, H.,Muta,T., Nomura, S.,Voelker, D. R., and Kuroki, Y., Pulmonary surfactant protein A modulates the cellular response to smooth and rough lipopolysaccharides by interaction with CD14. J Immunol 1999; 163(1):387-395.
    • (1999) J Immunol , vol.163 , Issue.1 , pp. 387-395
    • Sano, H.1    Sohma, H.2    Muta, T.3    Nomura, S.4    Voelker, D.R.5    Kuroki, Y.6
  • 324
    • 0034698127 scopus 로고    scopus 로고
    • Surfactant proteins A and D bind CD14 by different mechanisms
    • Sano, H., Chiba, H., Iwaki, D., Sohma, H., Voelker, D. R., and Kuroki, Y., Surfactant proteins A and D bind CD14 by different mechanisms. J Biol Chem 2000; 275(29):22442-22451.
    • (2000) J Biol Chem , vol.275 , Issue.29 , pp. 22442-22451
    • Sano, H.1    Chiba, H.2    Iwaki, D.3    Sohma, H.4    Voelker, D.R.5    Kuroki, Y.6
  • 325
    • 0034892207 scopus 로고    scopus 로고
    • Evolution of effectors and receptors of innate immunity
    • Magor, B. G., and Magor, K. E., Evolution of effectors and receptors of innate immunity. Dev Comp Immunol 2001; 25:651-682.
    • (2001) Dev Comp Immunol , vol.25 , pp. 651-682
    • Magor, B.G.1    Magor, K.E.2
  • 326
    • 0036453721 scopus 로고    scopus 로고
    • Evolution of the TIR, Tolls and TLRs: Functional inferences from computational biology
    • Beutler, B., and Rehli, M., Evolution of the TIR, Tolls and TLRs: functional inferences from computational biology. Curr Top Microbiol Immunol 2002; 270:1-21.
    • (2002) Curr Top Microbiol Immunol , vol.270 , pp. 1-21
    • Beutler, B.1    Rehli, M.2
  • 327
    • 0035811018 scopus 로고    scopus 로고
    • A reverse genetic analysis of components of the Toll signaling pathway in Caenorhabditis elegans
    • Pujol, N., Link, E. M., Liu, L. X., Kurz, C. L., Alloing, G., Tan, M. W., Ray, K. P., Solari, R., Johnson, C. D., and Ewbank, J. J., A reverse genetic analysis of components of the Toll signaling pathway in Caenorhabditis elegans. Curr Biol 2001; 11 (11):809-821.
    • (2001) Curr Biol , vol.11 , Issue.11 , pp. 809-821
    • Pujol, N.1    Link, E.M.2    Liu, L.X.3    Kurz, C.L.4    Alloing, G.5    Tan, M.W.6    Ray7
  • 328
    • 0035139983 scopus 로고    scopus 로고
    • Danger signals: SOS to the immune system
    • Gallucci, S., and Matzinger, P., Danger signals: SOS to the immune system. Curr Opin Immunol 2001; 13 (1):114-119.
    • (2001) Curr Opin Immunol , vol.13 , Issue.1 , pp. 114-119
    • Gallucci, S.1    Matzinger, P.2
  • 329
    • 0036790571 scopus 로고    scopus 로고
    • Role of heat shock proteins in atherosclerosis
    • Xu, Q., Role of heat shock proteins in atherosclerosis. Arterioscler Thromb Vasc Biol 2002; 22(10):1547-1559.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , Issue.10 , pp. 1547-1559
    • Xu, Q.1
  • 331
    • 0024320881 scopus 로고
    • Cytomegalovirus infection is associated with cardiac allograft rejection and atherosclerosis
    • Gratten, M. T., Moreno-Cabral, C. E., Starnes, V. A., Oyer, P. E., Stinson, E. B., and Shumway, N. E., Cytomegalovirus infection is associated with cardiac allograft rejection and atherosclerosis. JAMA 1989; 261:3561.
    • (1989) JAMA , vol.261 , pp. 3561
    • Gratten, M.T.1    Moreno-Cabral, C.E.2    Starnes, V.A.3    Oyer, P.E.4    Stinson, E.B.5    Shumway, N.E.6
  • 332
    • 0036015025 scopus 로고    scopus 로고
    • Review of evidence for a connection between Chlamydia pneumoniae and atherosclerotic disease
    • Dugan, J. P., Feuge, R. R., and Burgess, D. S., Review of evidence for a connection between Chlamydia pneumoniae and atherosclerotic disease. Clin Ther 2002; 24(5):719-735.
    • (2002) Clin Ther , vol.24 , Issue.5 , pp. 719-735
    • Dugan, J.P.1    Feuge, R.R.2    Burgess, D.S.3
  • 333
    • 0036329427 scopus 로고    scopus 로고
    • Role of infection in atherosclerosis and coronary artery disease: A new therapeutic target?
    • Frishman, W. H., and Ismail, A. A., Role of infection in atherosclerosis and coronary artery disease: a new therapeutic target? Cardiol Rev 2002; 10(4):199-210.
    • (2002) Cardiol Rev , vol.10 , Issue.4 , pp. 199-210
    • Frishman, W.H.1    Ismail, A.A.2
  • 334
    • 0037024326 scopus 로고    scopus 로고
    • Roxithromycin treatment prevents progression of peripheral arterial occlusive disease in Chlamydia pneumoniae seropositive men: A randomized, double-blind, placebo-controlled trial
    • Wiesli, P., Czerwenka, W., Meniconi, A., Maly, F. E., Hoffmann, U., Vetter, W., and Schulthess, G., Roxithromycin treatment prevents progression of peripheral arterial occlusive disease in Chlamydia pneumoniae seropositive men: a randomized, double-blind, placebo-controlled trial. Circulation 2002; 105 (22):2646-2652.
    • (2002) Circulation , vol.105 , Issue.22 , pp. 2646-2652
    • Wiesli, P.1    Czerwenka, W.2    Meniconi, A.3    Maly, F.E.4    Hoffmann, U.5    Vetter, W.6    Schulthess, G.7
  • 335
    • 0037027478 scopus 로고    scopus 로고
    • Reduced progression of early carotid atherosclerosis after antibiotic treatment and Chlamydia pneumoniae seropositivity
    • Sander, D.,Winbeck, K., Klingelhofer, J., Etgen, T., and Conrad, B., Reduced progression of early carotid atherosclerosis after antibiotic treatment and Chlamydia pneumoniae seropositivity. Circulation 2002; 106 (19):2428-2433.
    • (2002) Circulation , vol.106 , Issue.19 , pp. 2428-2433
    • Sander, D.1    Winbeck, K.2    Klingelhofer, J.3    Etgen, T.4    Conrad, B.5
  • 336
    • 0036888669 scopus 로고    scopus 로고
    • Making and breaking tolerance
    • Ohashi, P. S., and DeFranco, A. L., Making and breaking tolerance. Curr Opin Immunol 2002; 14(6):744-759.
    • (2002) Curr Opin Immunol , vol.14 , Issue.6 , pp. 744-759
    • Ohashi, P.S.1    DeFranco, A.L.2
  • 337
    • 0036093704 scopus 로고    scopus 로고
    • A role for Toll in autoimmunity
    • Krieg, A. M., A role for Toll in autoimmunity. Nat Immunol 2002; 3(5):423-424.
    • (2002) Nat Immunol , vol.3 , Issue.5 , pp. 423-424
    • Krieg, A.M.1
  • 338
    • 0036093704 scopus 로고    scopus 로고
    • A role for Toll in autoimmunity
    • Krieg, A. M., A role for Toll in autoimmunity. Nat Immunol 2002; 3(5):423-424.
    • (2002) Nat Immunol , vol.3 , Issue.5 , pp. 423-424
    • Krieg, A.M.1
  • 339
    • 0036204061 scopus 로고    scopus 로고
    • Cardiac inflammation and innate immunity in septic shock: Is there a role for Toll-like receptors?
    • Knuefermann, P.,Nemoto, S., Baumgarten, G., Misra, A., Sivasubramanian, N., Carabello, B. A., and Vallejo, J. G., Cardiac inflammation and innate immunity in septic shock: is there a role for Toll-like receptors? Chest 2002; 121(4):1329-1336.
    • (2002) Chest , vol.121 , Issue.4 , pp. 1329-1336
    • Knuefermann, P.1    Nemoto, S.2    Baumgarten, G.3    Misra, A.4    Sivasubramanian, N.5    Carabello, B.A.6    Vallejo, J.G.7
  • 341
    • 0036521467 scopus 로고    scopus 로고
    • Emerging evidence that molecules expressed by mammalian tissue grafts are recognized by the innate immune system
    • Fox-Marsh, A., and Harrison, L. C., Emerging evidence that molecules expressed by mammalian tissue grafts are recognized by the innate immune system. J Leukoc Biol 2002; 71(3):401-409.
    • (2002) J Leukoc Biol , vol.71 , Issue.3 , pp. 401-409
    • Fox-Marsh, A.1    Harrison, L.C.2
  • 343
    • 0036569813 scopus 로고    scopus 로고
    • Toll-like receptor 4 is required for optimal development of Th2 immune responses: Role of dendritic cells
    • Dabbagh, K., Dahl, M. E., Stepick-Biek, P., and Lewis, D. B., Toll-like receptor 4 is required for optimal development of Th2 immune responses: role of dendritic cells. J Immunol 2002; 168(9):4524-4530.
    • (2002) J Immunol , vol.168 , Issue.9 , pp. 4524-4530
    • Dabbagh, K.1    Dahl, M.E.2    Stepick-Biek, P.3    Lewis, D.B.4
  • 344
    • 0036105543 scopus 로고    scopus 로고
    • Differential responses of mast cell Toll-like receptors 2 and 4 in allergy and innate immunity
    • Supajatura, V., Ushio, H., Nakao, A., Akira, S., Okumura, K., Ra, C., and Ogawa, H., Differential responses of mast cell Toll-like receptors 2 and 4 in allergy and innate immunity. J Clin Invest 2002; 109(10):1351-1359.
    • (2002) J Clin Invest , vol.109 , Issue.10 , pp. 1351-1359
    • Supajatura, V.1    Ushio, H.2    Nakao, A.3    Akira, S.4    Okumura, K.5    Ra, C.6    Ogawa, H.7


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