메뉴 건너뛰기




Volumn 12, Issue 4, 2006, Pages 195-204

Invited review: Roles for accessory molecules in microbial recognition by Toll-like receptors

Author keywords

CD14; LBP; LPS; MD 2; Toll like receptors

Indexed keywords

CD14 ANTIGEN; FLAGELLIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON; LECTIN; LIPID A; LIPOPOLYSACCHARIDE; LIPOPOLYSACCHARIDE BINDING PROTEIN; PACLITAXEL; PROTEIN MD 2; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 7; TOLL LIKE RECEPTOR 8; TOLL LIKE RECEPTOR 9; TUMOR NECROSIS FACTOR ALPHA; ACUTE PHASE PROTEIN; BACTERIAL TOXIN; CARRIER PROTEIN; LIGAND; LIPOPOLYSACCHARIDE-BINDING PROTEIN; MEMBRANE PROTEIN;

EID: 33749065328     PISSN: 09680519     EISSN: None     Source Type: Journal    
DOI: 10.1179/096805106X118807     Document Type: Review
Times cited : (134)

References (86)
  • 1
    • 0034610291 scopus 로고    scopus 로고
    • The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between Toll-like receptors
    • Ozinsky A., Underhill DM, Fontenot JD et al. The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between Toll-like receptors. Proc Natl Acad Sci USA 2000; 97: 13766-13771.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13766-13771
    • Ozinsky, A.1    Underhill, D.M.2    Fontenot, J.D.3
  • 2
    • 0036644042 scopus 로고    scopus 로고
    • Role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins
    • Takeuchi O., Sato S., Horiuchi T. et al. Role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins. J Immunol 2002; 169: 10-14.
    • (2002) J Immunol , vol.169 , pp. 10-14
    • Takeuchi, O.1    Sato, S.2    Horiuchi, T.3
  • 3
    • 0034922923 scopus 로고    scopus 로고
    • Discrimination of bacterial lipoproteins by Toll-like receptor 6
    • Takeuchi O., Kawai T., Muhlradt PF et al. Discrimination of bacterial lipoproteins by Toll-like receptor 6. Int Immunol 2001; 13: 933-940.
    • (2001) Int Immunol , vol.13 , pp. 933-940
    • Takeuchi, O.1    Kawai, T.2    Muhlradt, P.F.3
  • 4
    • 0034619794 scopus 로고    scopus 로고
    • A Toll-like receptor recognizes bacterial DNA
    • Hemmi H., Takeuchi O., Kawai T. et al. A Toll-like receptor recognizes bacterial DNA. Nature 2000; 408: 740-745.
    • (2000) Nature , vol.408 , pp. 740-745
    • Hemmi, H.1    Takeuchi, O.2    Kawai, T.3
  • 5
    • 1542317550 scopus 로고    scopus 로고
    • Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA
    • Diebold SS, Kaisho T., Hemmi H., Akira S., Reis e Sousa C. Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA. Science 2004; 303: 1529-1531.
    • (2004) Science , vol.303 , pp. 1529-1531
    • Diebold, S.S.1    Kaisho, T.2    Hemmi, H.3    Akira, S.4    Reis e Sousa, C.5
  • 6
    • 1542317578 scopus 로고    scopus 로고
    • Species-specific recognition of single-stranded RNA via Toll-like receptor 7 and 8
    • Heil F., Hemmi H., Hochrein H. et al. Species-specific recognition of single-stranded RNA via Toll-like receptor 7 and 8. Science 2004; 303: 1526-1529.
    • (2004) Science , vol.303 , pp. 1526-1529
    • Heil, F.1    Hemmi, H.2    Hochrein, H.3
  • 7
    • 0035909372 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3
    • Alexopoulou L., Holt AC, Medzhitov R., Flavell RA Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3. Nature 2001; 413: 732-738.
    • (2001) Nature , vol.413 , pp. 732-738
    • Alexopoulou, L.1    Holt, A.C.2    Medzhitov, R.3    Flavell, R.A.4
  • 8
    • 23844464444 scopus 로고    scopus 로고
    • Suppression of RNA recognition by Toll-like receptors: The impact of nucleoside modification and the evolutionary origin of RNA
    • Kariko K., Buckstein M., Ni H., Weissman D. Suppression of RNA recognition by Toll-like receptors: The impact of nucleoside modification and the evolutionary origin of RNA. Immunity 2005; 23: 165-175.
    • (2005) Immunity , vol.23 , pp. 165-175
    • Kariko, K.1    Buckstein, M.2    Ni, H.3    Weissman, D.4
  • 9
    • 0035953543 scopus 로고    scopus 로고
    • The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5
    • Hayashi F., Smith KD, Ozinsky A. et al. The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5. Nature 2001; 410: 1099-1103.
    • (2001) Nature , vol.410 , pp. 1099-1103
    • Hayashi, F.1    Smith, K.D.2    Ozinsky, A.3
  • 10
    • 20644433342 scopus 로고    scopus 로고
    • TLR11 activation of dendritic cells by a protozoan profilin-like protein
    • Yarovinsky F., Zhang D., Andersen JF et al. TLR11 activation of dendritic cells by a protozoan profilin-like protein. Science 2005; 308: 1626-1629.
    • (2005) Science , vol.308 , pp. 1626-1629
    • Yarovinsky, F.1    Zhang, D.2    Andersen, J.F.3
  • 11
    • 1542377424 scopus 로고    scopus 로고
    • A Toll-like receptor that prevents infection by uropathogenic bacteria
    • Zhang D., Zhang G., Hayden MS et al. A Toll-like receptor that prevents infection by uropathogenic bacteria. Science 2004; 303: 1522-1526.
    • (2004) Science , vol.303 , pp. 1522-1526
    • Zhang, D.1    Zhang, G.2    Hayden, M.S.3
  • 12
    • 5944261457 scopus 로고    scopus 로고
    • Pattern recognition receptors TLR4 and CD14 mediate response to respiratory syncytial virus
    • Kurt-Jones EA, Popova L., Kwinn L. et al. Pattern recognition receptors TLR4 and CD14 mediate response to respiratory syncytial virus. Nat Immunol 2000; 1: 398-401.
    • (2000) Nat Immunol , vol.1 , pp. 398-401
    • Kurt-Jones, E.A.1    Popova, L.2    Kwinn, L.3
  • 15
    • 20644469429 scopus 로고    scopus 로고
    • CD14 is required for MyD88-independent LPS signaling
    • Jiang Z., Georgel P., Du X. et al. CD14 is required for MyD88-independent LPS signaling. Nat Immunol 2005; 6: 565-570.
    • (2005) Nat Immunol , vol.6 , pp. 565-570
    • Jiang, Z.1    Georgel, P.2    Du, X.3
  • 16
    • 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., Nishijima M. Involvement of TLR4/MD-2 complex in species-specific lipopolysaccharide-mimetic signal transduction by Taxol. J Endotoxin Res 2001; 7: 232-236.
    • (2001) J Endotoxin Res , vol.7 , pp. 232-236
    • Kawasaki, K.1    Akashi, S.2    Shimazu, R.3    Yoshida, T.4    Miyake, K.5    Nishijima, M.6
  • 18
    • 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. et al. Novel signal transduction pathway utilized by extracellular HSP70: Role of Toll-like receptor (TLR) 2 and TLR4. J Biol Chem 2002; 277: 15028-15034.
    • (2002) J Biol Chem , vol.277 , pp. 15028-15034
    • Asea, A.1    Rehli, M.2    Kabingu, E.3
  • 19
    • 0036467447 scopus 로고    scopus 로고
    • Chlamydial heat shock protein 60 activates macrophages and endothelial cells through Toll-like receptor 4 and MD2 in a MyD88-dependent pathway
    • Bulut Y., Faure E., Thomas L. et al. Chlamydial heat shock protein 60 activates macrophages and endothelial cells through Toll-like receptor 4 and MD2 in a MyD88-dependent pathway. J Immunol 2002; 168: 1435-1440.
    • (2002) J Immunol , vol.168 , pp. 1435-1440
    • Bulut, Y.1    Faure, E.2    Thomas, L.3
  • 20
    • 0035800883 scopus 로고    scopus 로고
    • Chlamydia pneumoniae and chlamydial heat shock protein 60 stimulate proliferation of human vascular smooth muscle cells via Toll-like receptor 4 and p44/p42 mitogen-activated protein kinase activation
    • Sasu S., LaVerda D., Qureshi N., Golenbock DT, Beasley D. Chlamydia pneumoniae and chlamydial heat shock protein 60 stimulate proliferation of human vascular smooth muscle cells via Toll-like receptor 4 and p44/ p42 mitogen-activated protein kinase activation. Circ Res 2001; 89: 244-250.
    • (2001) Circ Res , vol.89 , pp. 244-250
    • Sasu, S.1    LaVerda, D.2    Qureshi, N.3    Golenbock, D.T.4    Beasley, D.5
  • 21
    • 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 RM, Ahmad-Nejad P., da Costa C. et al. 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: 31332-31339.
    • (2001) J Biol Chem , vol.276 , pp. 31332-31339
    • Vabulas, R.M.1    Ahmad-Nejad, P.2    da Costa, C.3
  • 22
    • 0034650427 scopus 로고    scopus 로고
    • Heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex
    • Ohashi K., Burkart V., Flohe S., Kolb H. 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
  • 23
    • 0035971217 scopus 로고    scopus 로고
    • The extra domain A of fibronectin activates Toll-like receptor 4
    • Okamura Y., Watari M., Jerud ES et al. The extra domain A of fibronectin activates Toll-like receptor 4. J Biol Chem 2001; 276: 10229-10233.
    • (2001) J Biol Chem , vol.276 , pp. 10229-10233
    • Okamura, Y.1    Watari, M.2    Jerud, E.S.3
  • 24
    • 0037097672 scopus 로고    scopus 로고
    • The immunostimulatory activity of the lung surfactant protein-A involves Toll-like receptor 4
    • Guillot L., Balloy V., McCormack FX, Golenbock DT, Chignard M., Si-Tahar M. The immunostimulatory activity of the lung surfactant protein-A involves Toll-like receptor 4. J Immunol 2002; 168: 5989-5992.
    • (2002) J Immunol , vol.168 , pp. 5989-5992
    • Guillot, L.1    Balloy, V.2    McCormack, F.X.3    Golenbock, D.T.4    Chignard, M.5    Si-Tahar, M.6
  • 25
    • 0037033364 scopus 로고    scopus 로고
    • Oligosaccharides of Hyaluronan activate dendritic cells via Toll-like receptor 4
    • Termeer C., Benedix F., Sleeman J. et al. Oligosaccharides of Hyaluronan activate dendritic cells via Toll-like receptor 4. J Exp Med 2002; 195: 99-111.
    • (2002) J Exp Med , vol.195 , pp. 99-111
    • Termeer, C.1    Benedix, F.2    Sleeman, J.3
  • 26
    • 0033580949 scopus 로고    scopus 로고
    • Peptidoglycan- and lipoteichoic acid-induced cell activation is mediated by Toll-like receptor 2
    • Schwandner R., Dziarski R., Wesche H., Rothe M., Kirschning CJ Peptidoglycan- and lipoteichoic acid-induced cell activation is mediated by Toll-like receptor 2. J Biol Chem 1999; 274: 17406-17409.
    • (1999) J Biol Chem , vol.274 , pp. 17406-17409
    • Schwandner, R.1    Dziarski, R.2    Wesche, H.3    Rothe, M.4    Kirschning, C.J.5
  • 27
    • 0037124358 scopus 로고    scopus 로고
    • Synthetic lipoteichoic acid from Staphylococcus aureus is a potent stimulus of cytokine release
    • Morath S., Stadelmaier A., Geyer A., Schmidt RR, Hartung T. Synthetic lipoteichoic acid from Staphylococcus aureus is a potent stimulus of cytokine release. J Exp Med 2002; 195: 1635-1640.
    • (2002) J Exp Med , vol.195 , pp. 1635-1640
    • Morath, S.1    Stadelmaier, A.2    Geyer, A.3    Schmidt, R.R.4    Hartung, T.5
  • 28
    • 0033592748 scopus 로고    scopus 로고
    • The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens
    • Underhill DM, Ozinsky A., Hajjar AM et al. The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens. Nature 1999; 401: 811-815.
    • (1999) Nature , vol.401 , pp. 811-815
    • Underhill, D.M.1    Ozinsky, A.2    Hajjar, A.M.3
  • 29
    • 0034933019 scopus 로고    scopus 로고
    • Identification of CpG oligonucleotide sequences with high induction of IFN-alpha/beta in plasmacytoid dendritic cells
    • Krug A., Rothenfusser S., Hornung V. et al. Identification of CpG oligonucleotide sequences with high induction of IFN-alpha/beta in plasmacytoid dendritic cells. Eur J Immunol 2001; 31: 2154-2163.
    • (2001) Eur J Immunol , vol.31 , pp. 2154-2163
    • Krug, A.1    Rothenfusser, S.2    Hornung, V.3
  • 30
    • 0035865054 scopus 로고    scopus 로고
    • Human peripheral blood cells differentially recognize and respond to two distinct CPG motifs
    • Verthelyi D., Ishii KJ., Gursel M., Takeshita F., Klinman DM Human peripheral blood cells differentially recognize and respond to two distinct CPG motifs. J Immunol 2001; 166: 2372-2377.
    • (2001) J Immunol , vol.166 , pp. 2372-2377
    • Verthelyi, D.1    Ishii, K.J.2    Gursel, M.3    Takeshita, F.4    Klinman, D.M.5
  • 31
    • 17844380477 scopus 로고    scopus 로고
    • Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction
    • Honda K., Ohba Y., Yanai H. et al. Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction. Nature 2005; 434: 1035-1040.
    • (2005) Nature , vol.434 , pp. 1035-1040
    • Honda, K.1    Ohba, Y.2    Yanai, H.3
  • 32
    • 10744219675 scopus 로고    scopus 로고
    • TLR9 signals after translocating from the ER to CpG DNA in the lysosome
    • Latz E., Schoenemeyer A., Visintin A. et al. TLR9 signals after translocating from the ER to CpG DNA in the lysosome. Nat Immunol 2004; 5: 190-198.
    • (2004) Nat Immunol , vol.5 , pp. 190-198
    • Latz, E.1    Schoenemeyer, A.2    Visintin, A.3
  • 34
    • 0037025399 scopus 로고    scopus 로고
    • The extracellular Toll-like receptor 2 domain directly binds peptidoglycan derived from Staphylococcus aureus
    • Iwaki D., Mitsuzawa H., Murakami S. et al. The extracellular Toll-like receptor 2 domain directly binds peptidoglycan derived from Staphylococcus aureus. J Biol Chem 2002; 277: 24315-24320.
    • (2002) J Biol Chem , vol.277 , pp. 24315-24320
    • Iwaki, D.1    Mitsuzawa, H.2    Murakami, S.3
  • 35
    • 2442450672 scopus 로고    scopus 로고
    • Direct evidence that Toll-like receptor 9 (TLR9) functionally binds plasmid DNA by specific cytosine-phosphate-guanine motif recognition
    • Cornelie S., Hoebeke J., Schacht AM et al. Direct evidence that Toll-like receptor 9 (TLR9) functionally binds plasmid DNA by specific cytosine-phosphate-guanine motif recognition. J Biol Chem 2004; 279: 15124-15129.
    • (2004) J Biol Chem , vol.279 , pp. 15124-15129
    • Cornelie, S.1    Hoebeke, J.2    Schacht, A.M.3
  • 36
    • 4644330955 scopus 로고    scopus 로고
    • Toll-like receptor 9 binds single-stranded CpG-DNA in a sequence- and pH-dependent manner
    • Rutz M., Metzger J., Gellert T. et al. Toll-like receptor 9 binds single-stranded CpG-DNA in a sequence- and pH-dependent manner. Eur J Immunol 2004; 34: 2541-2550.
    • (2004) Eur J Immunol , vol.34 , pp. 2541-2550
    • Rutz, M.1    Metzger, J.2    Gellert, T.3
  • 37
    • 23044445303 scopus 로고    scopus 로고
    • Crystal structure of human Toll-like receptor 3 (TLR3) ectodomain
    • Choe J., Kelker MS, Wilson IA Crystal structure of human Toll-like receptor 3 (TLR3) ectodomain. Science 2005; 309: 581-585.
    • (2005) Science , vol.309 , pp. 581-585
    • Choe, J.1    Kelker, M.S.2    Wilson, I.A.3
  • 38
    • 31344476404 scopus 로고    scopus 로고
    • Recognition of double stranded RNA by human Toll like receptor 3 and downstream receptor signaling requires multimerisation and an acidic pH
    • de Bouteiller O., Merck E., Hasan UA et al. Recognition of double stranded RNA by human Toll like receptor 3 and downstream receptor signaling requires multimerisation and an acidic pH. J Biol Chem 2005; 280: 38173-38152.
    • (2005) J Biol Chem , vol.280 , pp. 38152-38173
    • de Bouteiller, O.1    Merck, E.2    Hasan, U.A.3
  • 39
    • 23344431978 scopus 로고    scopus 로고
    • The molecular structure of the Toll-like receptor 3 ligand-binding domain
    • Bell JK, Botos I., Hall PR et al. The molecular structure of the Toll-like receptor 3 ligand-binding domain. Proc Natl Acad Sci USA 2005; 102: 10976-10980.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10976-10980
    • Bell, J.K.1    Botos, I.2    Hall, P.R.3
  • 40
    • 13444280215 scopus 로고    scopus 로고
    • CD36 is a sensor of diacylglycerides
    • Hoebe K., Georgel P., Rutschmann S. et al. CD36 is a sensor of diacylglycerides. Nature 2005; 433: 523-527.
    • (2005) Nature , vol.433 , pp. 523-527
    • Hoebe, K.1    Georgel, P.2    Rutschmann, S.3
  • 41
    • 0035817818 scopus 로고    scopus 로고
    • Immune recognition. A new receptor for beta-glucans
    • Brown GD, Gordon S. Immune recognition. A new receptor for beta-glucans. Nature 2001; 413: 36-37.
    • (2001) Nature , vol.413 , pp. 36-37
    • Brown, G.D.1    Gordon, S.2
  • 42
    • 0038558249 scopus 로고    scopus 로고
    • Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2
    • Gantner BN, Simmons RM, Canavera SJ, Akira S., Underhill DM Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2. J Exp Med 2003; 197: 1107-1117.
    • (2003) J Exp Med , vol.197 , pp. 1107-1117
    • Gantner, B.N.1    Simmons, R.M.2    Canavera, S.J.3    Akira, S.4    Underhill, D.M.5
  • 43
    • 20244363662 scopus 로고    scopus 로고
    • Syk-dependent cytokine induction by Dectin-1 reveals a novel pattern recognition pathway for C type lectins
    • Rogers NC, Slack EC, Edwards AD et al. Syk-dependent cytokine induction by Dectin-1 reveals a novel pattern recognition pathway for C type lectins. Immunity 2005; 22: 507-517.
    • (2005) Immunity , vol.22 , pp. 507-517
    • Rogers, N.C.1    Slack, E.C.2    Edwards, A.D.3
  • 44
    • 0032509295 scopus 로고    scopus 로고
    • Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: Mutations in Tlr4 gene
    • Poltorak A., He X., Smirnova I. et al. Defective LPS signaling in C3H/ HeJ and C57BL/10ScCr mice: Mutations in Tlr4 gene. Science 1998; 282: 2085-2088.
    • (1998) Science , vol.282 , pp. 2085-2088
    • Poltorak, A.1    He, X.2    Smirnova, I.3
  • 45
    • 0345561540 scopus 로고    scopus 로고
    • Endotoxin-tolerant mice have mutations in Toll-like receptor 4 (Tlr4)
    • Qureshi ST, Lariviere L., Leveque G. et al. Endotoxin-tolerant mice have mutations in Toll-like receptor 4 (Tlr4). J Exp Med 1999; 189: 615-625.
    • (1999) J Exp Med , vol.189 , pp. 615-625
    • Qureshi, S.T.1    Lariviere, L.2    Leveque, G.3
  • 46
    • 0028924539 scopus 로고
    • Lipopolysaccharide binding protein-mediated complexation of lipopolysaccharide with soluble CD14
    • Tobias PS, Soldau K., Gegner JA, Mintz D., Ulevitch RJ Lipopolysaccharide binding protein-mediated complexation of lipopolysaccharide with soluble CD14. J Biol Chem 1995; 270: 10482-10488.
    • (1995) J Biol Chem , vol.270 , pp. 10482-10488
    • Tobias, P.S.1    Soldau, K.2    Gegner, J.A.3    Mintz, D.4    Ulevitch, R.J.5
  • 47
    • 0025107568 scopus 로고
    • Structure and function of lipopolysaccharide binding protein
    • Schumann RR, Leong SR, Flaggs GW et al. Structure and function of lipopolysaccharide binding protein. Science 1990; 249: 1429-1431.
    • (1990) Science , vol.249 , pp. 1429-1431
    • Schumann, R.R.1    Leong, S.R.2    Flaggs, G.W.3
  • 48
    • 0025166114 scopus 로고
    • CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein
    • Wright SD, Ramos RA, Tobias PS, Ulevitch RJ, Mathison JC 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
  • 49
    • 0030760314 scopus 로고    scopus 로고
    • Crystal structure of human BPI and two bound phospholipids at 2.4 Angstrom resolution
    • Beamer LJ, Carroll SF, Eisenberg D. Crystal structure of human BPI and two bound phospholipids at 2.4 Angstrom resolution. Science 1997; 276: 1861-1864.
    • (1997) Science , vol.276 , pp. 1861-1864
    • Beamer, L.J.1    Carroll, S.F.2    Eisenberg, D.3
  • 50
    • 33646336635 scopus 로고    scopus 로고
    • Localization of the lipopolysaccharide-binding protein (LBP) in phospholipid membranes by a atomic force microscopy
    • Roes S., Mumm F., Seydel U., Gutsmann T. Localization of the lipopolysaccharide-binding protein (LBP) in phospholipid membranes by a atomic force microscopy. J Biol Chem 2006; 281: 2757-2819.
    • (2006) J Biol Chem , vol.281 , pp. 2757-2819
    • Roes, S.1    Mumm, F.2    Seydel, U.3    Gutsmann, T.4
  • 51
    • 15744396047 scopus 로고    scopus 로고
    • Crystal structure of CD14 and its implications for lipopolysaccharide signaling
    • Kim JI, Lee CJ, Jin MS et al. Crystal structure of CD14 and its implications for lipopolysaccharide signaling. J Biol Chem 2005; 280: 11347-11351.
    • (2005) J Biol Chem , vol.280 , pp. 11347-11351
    • Kim, J.I.1    Lee, C.J.2    Jin, M.S.3
  • 52
    • 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 J., Soldau K., Christen U., Tobias PS, Ulevitch RJ 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: 21129-21135.
    • (2001) J Biol Chem , vol.276 , pp. 21129-21135
    • da Silva Correia, J.1    Soldau, K.2    Christen, U.3    Tobias, P.S.4    Ulevitch, R.J.5
  • 53
    • 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., 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: 42372-42379.
    • (2002) J Biol Chem , vol.277 , pp. 42372-42379
    • Muroi, M.1    Ohnishi, T.2    Tanamoto, K.3
  • 54
    • 0029117709 scopus 로고
    • Identification of a domain in soluble CD14 essential for lipopolysaccharide (LPS) signaling but not LPS binding
    • Juan TS, Hailman E., Kelley MJ, Wright SD, Lichenstein HS Identification of a domain in soluble CD14 essential for lipopolysaccharide (LPS) signaling but not LPS binding. J Biol Chem 1995; 270: 17237-17242.
    • (1995) J Biol Chem , vol.270 , pp. 17237-17242
    • Juan, T.S.1    Hailman, E.2    Kelley, M.J.3    Wright, S.D.4    Lichenstein, H.S.5
  • 55
    • 0033485433 scopus 로고    scopus 로고
    • Differential impact of substitution of amino acids 9-13 and 91-101 of human CD14 on soluble CD14-dependent activation of cells by lipopolysaccharide
    • Stelter F., Loppnow H., Menzel R. et al. Differential impact of substitution of amino acids 9-13 and 91-101 of human CD14 on soluble CD14-dependent activation of cells by lipopolysaccharide. J Immunol 1999; 163: 6035-6044.
    • (1999) J Immunol , vol.163 , pp. 6035-6044
    • Stelter, F.1    Loppnow, H.2    Menzel, R.3
  • 56
    • 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 JA, Segal DM Secreted MD-2 is a large polymeric protein that efficiently confers lipopolysaccharide sensitivity to Toll-like receptor 4. Proc Natl Acad Sci USA 2001; 98: 12156-12161.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12156-12161
    • Visintin, A.1    Mazzoni, A.2    Spitzer, J.A.3    Segal, D.M.4
  • 57
    • 0036558018 scopus 로고    scopus 로고
    • ML - A conserved domain involved in innate immunity and lipid metabolism
    • Inohara N., Nunez G. ML - a conserved domain involved in innate immunity and lipid metabolism. Trends Biochem Sci 2002; 27: 219-221.
    • (2002) Trends Biochem Sci , vol.27 , pp. 219-221
    • Inohara, N.1    Nunez, G.2
  • 58
    • 0036307905 scopus 로고    scopus 로고
    • The crystal structure of a major dust mite allergen Der p 2, and its biological implications
    • Derewenda U., Li J., Derewenda Z. et al. The crystal structure of a major dust mite allergen Der p 2, and its biological implications. J Mol Biol 2002; 318: 189-197.
    • (2002) J Mol Biol , vol.318 , pp. 189-197
    • Derewenda, U.1    Li, J.2    Derewenda, Z.3
  • 59
    • 3242776258 scopus 로고    scopus 로고
    • MD-2: The Toll 'gatekeeper' in endotoxin signalling
    • Gangloff M., Gay NJ MD-2: The Toll 'gatekeeper' in endotoxin signalling. Trends Biochem Sci 2004; 29: 294-300.
    • (2004) Trends Biochem Sci , vol.29 , pp. 294-300
    • Gangloff, M.1    Gay, N.J.2
  • 61
    • 0037080024 scopus 로고    scopus 로고
    • Tissue expression of human Toll-like receptors and differential regulation of Toll-like receptor mRNAs in leukocytes in response to microbes, their products, and cytokines
    • Zarember KA, Godowski PJ Tissue expression of human Toll-like receptors and differential regulation of Toll-like receptor mRNAs in leukocytes in response to microbes, their products, and cytokines. J Immunol 2002; 168: 554-561.
    • (2002) J Immunol , vol.168 , pp. 554-561
    • Zarember, K.A.1    Godowski, P.J.2
  • 62
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu R., Akashi S., Ogata H. et al. 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
  • 63
    • 0035885127 scopus 로고    scopus 로고
    • N-linked glycosylations at Asn26 and Asn114 of human MD-2 are required for Toll-like receptor 4-mediated activation of NF-κB by lipopolysaccharide
    • Ohnishi T., Muroi M., Tanamoto K-I. N-linked glycosylations at Asn26 and Asn114 of human MD-2 are required for Toll-like receptor 4-mediated activation of NF-κB by lipopolysaccharide. J Immunol 2001; 167: 3354-3359.
    • (2001) J Immunol , vol.167 , pp. 3354-3359
    • Ohnishi, T.1    Muroi, M.2    Tanamoto, K.-I.3
  • 64
    • 0034795208 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
    • Randow F., Seed B. Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. Nat Cell Biol 2001; 3: 891-896.
    • (2001) Nat Cell Biol , vol.3 , pp. 891-896
    • Randow, F.1    Seed, B.2
  • 65
    • 0036301797 scopus 로고    scopus 로고
    • Essential role of MD-2 in LPS responsiveness and TLR4 distribution
    • Nagai Y., Akashi S., Nagafuku M. et al. Essential role of MD-2 in LPS responsiveness and TLR4 distribution. Nat Immunol 2002; 3: 667-672.
    • (2002) Nat Immunol , vol.3 , pp. 667-672
    • Nagai, Y.1    Akashi, S.2    Nagafuku, M.3
  • 66
    • 29244450802 scopus 로고    scopus 로고
    • Intracellular localization of Toll-like receptor 9 prevents recognition of self DNA but facilitates access to viral DNA
    • Barton GM, Kagan JC, Medzhitov R. Intracellular localization of Toll-like receptor 9 prevents recognition of self DNA but facilitates access to viral DNA. Nat Immunol 2006; 7: 49-56.
    • (2006) Nat Immunol , vol.7 , pp. 49-56
    • Barton, G.M.1    Kagan, J.C.2    Medzhitov, R.3
  • 67
    • 0037018107 scopus 로고    scopus 로고
    • Toll-like receptor 4 resides in the Golgi apparatus and colocalizes with internalized lipopolysaccharide in intestinal epithelial cells
    • Hornef MW, Frisan T., Vandewalle A., Normark S., Richter-Dahlfors A. Toll-like receptor 4 resides in the Golgi apparatus and colocalizes with internalized lipopolysaccharide in intestinal epithelial cells. J Exp Med 2002; 195: 559-570.
    • (2002) J Exp Med , vol.195 , pp. 559-570
    • Hornef, M.W.1    Frisan, T.2    Vandewalle, A.3    Normark, S.4    Richter-Dahlfors, A.5
  • 68
    • 0037036469 scopus 로고    scopus 로고
    • TLR4 and MD-2 expression are regulated by immune-mediated signals in human intestinal epithelial cells
    • Abreu MT, Arnold ET, Thomas LS et al. TLR4 and MD-2 expression are regulated by immune-mediated signals in human intestinal epithelial cells. J Biol Chem 2002; 277: 20431-20437.
    • (2002) J Biol Chem , vol.277 , pp. 20431-20437
    • Abreu, M.T.1    Arnold, E.T.2    Thomas, L.S.3
  • 69
    • 3242708716 scopus 로고    scopus 로고
    • Endotoxin responsiveness of human airway epithelia is limited by low expression of MD-2
    • Jia HP, Kline JN, Penisten A. et al. Endotoxin responsiveness of human airway epithelia is limited by low expression of MD-2. Am J Physiol 2004; 287: L428-L437.
    • (2004) Am J Physiol , vol.287
    • Jia, H.P.1    Kline, J.N.2    Penisten, A.3
  • 70
    • 9144271703 scopus 로고    scopus 로고
    • Interaction of soluble form of recombinant extracellular TLR4 domain with MD-2 enables lipopolysaccharide binding and attenuates TLR4-mediated signaling
    • Hyakushima N., Mitsuzawa H., Nishitani C. et al. Interaction of soluble form of recombinant extracellular TLR4 domain with MD-2 enables lipopolysaccharide binding and attenuates TLR4-mediated signaling. J Immunol 2004; 173: 6949-6954.
    • (2004) J Immunol , vol.173 , pp. 6949-6954
    • Hyakushima, N.1    Mitsuzawa, H.2    Nishitani, C.3
  • 71
    • 1642529500 scopus 로고    scopus 로고
    • Isolation of an endotoxin-MD-2 complex that produces Toll-like receptor 4-dependent cell activation at picomolar concentrations
    • Gioannini TL, Teghanemt A., Zhang D. et al. Isolation of an endotoxin-MD-2 complex that produces Toll-like receptor 4-dependent cell activation at picomolar concentrations. Proc Natl Acad Sci USA 2004; 101: 4186-4191.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4186-4191
    • Gioannini, T.L.1    Teghanemt, A.2    Zhang, D.3
  • 73
    • 0141890200 scopus 로고    scopus 로고
    • Lipopolysaccharide interaction with cell surface Toll-like receptor 4-MD-2: Higher affinity than that with MD-2 or CD14
    • Akashi S., Saitoh S., Wakabayashi Y. et al. Lipopolysaccharide interaction with cell surface Toll-like receptor 4-MD-2: Higher affinity than that with MD-2 or CD14. J Exp Med 2003; 198: 1035-1042.
    • (2003) J Exp Med , vol.198 , pp. 1035-1042
    • Akashi, S.1    Saitoh, S.2    Wakabayashi, Y.3
  • 74
    • 0346850824 scopus 로고    scopus 로고
    • Lysines 128 and 132 enable lipopolysaccharide binding to MD-2, leading to Toll-like receptor-4 aggregation and signal transduction
    • Visintin A., Latz E., Monks BG, Espevik T., Golenbock DT Lysines 128 and 132 enable lipopolysaccharide binding to MD-2, leading to Toll-like receptor-4 aggregation and signal transduction. J Biol Chem 2003; 278: 48313-48320.
    • (2003) J Biol Chem , vol.278 , pp. 48313-48320
    • Visintin, A.1    Latz, E.2    Monks, B.G.3    Espevik, T.4    Golenbock, D.T.5
  • 75
    • 0037189544 scopus 로고    scopus 로고
    • Monomeric recombinant MD-2 binds Toll-like receptor 4 tightly and confers lipopolysaccharide responsiveness
    • Re F., Strominger JL Monomeric recombinant MD-2 binds Toll-like receptor 4 tightly and confers lipopolysaccharide responsiveness. J Biol Chem 2002; 277: 23427-23432.
    • (2002) J Biol Chem , vol.277 , pp. 23427-23432
    • Re, F.1    Strominger, J.L.2
  • 76
    • 0242495481 scopus 로고    scopus 로고
    • Separate functional domains of human MD-2 mediate Toll-like receptor 4-binding and lipopolysaccharide responsiveness
    • Re F., Strominger JL Separate functional domains of human MD-2 mediate Toll-like receptor 4-binding and lipopolysaccharide responsiveness. J Immunol 2003; 171: 5272-5276.
    • (2003) J Immunol , vol.171 , pp. 5272-5276
    • Re, F.1    Strominger, J.L.2
  • 77
    • 0036289969 scopus 로고    scopus 로고
    • Identification of LPS-binding peptide fragment of MD-2, a Toll-receptor accessory protein
    • Mancek M., Pristovsek P., Jerala R. Identification of LPS-binding peptide fragment of MD-2, a Toll-receptor accessory protein. Biochem Biophys Res Commun 2002; 292: 880-885.
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 880-885
    • Mancek, M.1    Pristovsek, P.2    Jerala, R.3
  • 78
    • 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., Beutler B. Physical contact between lipopolysaccharide and Toll-like receptor 4 revealed by genetic complementation. Proc Natl Acad Sci USA 2000; 97: 2163-2167.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2163-2167
    • Poltorak, A.1    Ricciardi-Castagnoli, P.2    Citterio, S.3    Beutler, B.4
  • 79
    • 0034002247 scopus 로고    scopus 로고
    • Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide
    • Lien E., Means TK, Heine H. et al. Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide. J Clin Invest 2000; 105: 497-504.
    • (2000) J Clin Invest , vol.105 , pp. 497-504
    • Lien, E.1    Means, T.K.2    Heine, H.3
  • 80
    • 3242690772 scopus 로고    scopus 로고
    • Lipid A antagonist, lipid IVa, is distinct from lipid A in interaction with Toll-like receptor 4 (TLR4)-MD-2 and ligand-induced TLR4 oligomerization
    • Saitoh S., Akashi S., Yamada T. et al. Lipid A antagonist, lipid IVa, is distinct from lipid A in interaction with Toll-like receptor 4 (TLR4)-MD-2 and ligand-induced TLR4 oligomerization. Int Immunol 2004; 16: 961-969.
    • (2004) Int Immunol , vol.16 , pp. 961-969
    • Saitoh, S.1    Akashi, S.2    Yamada, T.3
  • 81
    • 1642358911 scopus 로고    scopus 로고
    • Cytoplasmic domain-mediated dimerizations of Toll-like receptor 4 observed by beta-lactamase enzyme fragment complementation
    • Lee HK, Dunzendorfer S., Tobias PS Cytoplasmic domain-mediated dimerizations of Toll-like receptor 4 observed by beta-lactamase enzyme fragment complementation. J Biol Chem 2004; 279: 10564-10574.
    • (2004) J Biol Chem , vol.279 , pp. 10564-10574
    • Lee, H.K.1    Dunzendorfer, S.2    Tobias, P.S.3
  • 82
    • 0038448236 scopus 로고    scopus 로고
    • Lps2: A new locus required for responses to lipopolysaccharide, revealed by germline mutagenesis and phenotypic screening
    • Hoebe K., Du X., Goode J., Mann N., Beutler B. Lps2: A new locus required for responses to lipopolysaccharide, revealed by germline mutagenesis and phenotypic screening. J Endotoxin Res 2003; 9: 250-255.
    • (2003) J Endotoxin Res , vol.9 , pp. 250-255
    • Hoebe, K.1    Du, X.2    Goode, J.3    Mann, N.4    Beutler, B.5
  • 83
    • 0043176281 scopus 로고    scopus 로고
    • Role of adaptor TRIF in the MyD88-independent Toll-like receptor signaling pathway
    • Yamamoto M., Sato S., Hemmi H. et al. Role of adaptor TRIF in the MyD88-independent Toll-like receptor signaling pathway. Science 2003; 301: 640-643.
    • (2003) Science , vol.301 , pp. 640-643
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3
  • 85
    • 2442465798 scopus 로고    scopus 로고
    • Lipopolysaccharide-binding protein critically regulates lipopolysaccharide-induced IFN-beta signaling pathway in human monocytes
    • Kato A., Ogasawara T., Homma T., Saito H., Matsumoto K. Lipopolysaccharide-binding protein critically regulates lipopolysaccharide-induced IFN-beta signaling pathway in human monocytes. J Immunol 2004; 172: 6185-6194.
    • (2004) J Immunol , vol.172 , pp. 6185-6194
    • Kato, A.1    Ogasawara, T.2    Homma, T.3    Saito, H.4    Matsumoto, K.5
  • 86
    • 0242624622 scopus 로고    scopus 로고
    • TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway
    • Yamamoto M., Sato S., Hemmi H. et al. TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway. Nat Immunol 2003; 4: 1144-1150.
    • (2003) Nat Immunol , vol.4 , pp. 1144-1150
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.