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Volumn 11, Issue 5, 2005, Pages 294-298

Conserved mechanisms of signal transduction by toll and toll-like receptors

Author keywords

Modelling; TLR4 MD 2 complex; Toll receptor signalling

Indexed keywords

CD14 ANTIGEN; ENDOTOXIN; LIPID A; LIPOPOLYSACCHARIDE; LIPOPOLYSACCHARIDE BINDING PROTEIN; MEMBRANE PROTEIN; PROTEIN MD 2; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 4;

EID: 27644578690     PISSN: 09680519     EISSN: None     Source Type: Journal    
DOI: 10.1179/096805105X67274     Document Type: Article
Times cited : (9)

References (33)
  • 1
    • 0024464813 scopus 로고
    • Lipopolysaccharide (LPS) binding protein opsonizes LPS-bearing particles for recognition by a novel receptor on macrophages
    • Wright SD, Tobias PS, Ulevitch RJ, Ramos RA. Lipopolysaccharide (LPS) binding protein opsonizes LPS-bearing particles for recognition by a novel receptor on macrophages. J Exp Med 1989; 170: 1231-1241.
    • (1989) J. Exp. Med. , vol.170 , pp. 1231-1241
    • Wright, S.D.1    Tobias, P.S.2    Ulevitch, R.J.3    Ramos, R.A.4
  • 2
    • 0030685133 scopus 로고    scopus 로고
    • Lipopolysaccharide-binding protein is required to combat a murine Gram-negative bacterial infection
    • Jack RS, Fan XL, Bernheiden M et al. Lipopolysaccharide-binding protein is required to combat a murine Gram-negative bacterial infection. Nature 1997; 389: 742-745.
    • (1997) Nature , vol.389 , pp. 742-745
    • Jack, R.S.1    Fan, X.L.2    Bernheiden, M.3
  • 3
    • 0034674059 scopus 로고    scopus 로고
    • The 1.7 Angstrom crystal structure of BPI: A study of how two dissimilar amino acid sequences can adopt the same fold
    • Kleiger G, Beamer LJ, Grothe R, Mallick P, Eisenberg D. The 1.7 Angstrom crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold. J Mol Biol 2000; 299: 1019-1034.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1019-1034
    • Kleiger, G.1    Beamer, L.J.2    Grothe, R.3    Mallick, P.4    Eisenberg, D.5
  • 4
    • 0027955127 scopus 로고
    • Lipopolysaccharide (Lps)-binding protein accelerates the binding of LPS to CD14
    • Hailman E, Lichenstein HS, Wurfel MM et al. Lipopolysaccharide (Lps)-binding protein accelerates the binding of LPS to CD14. J Exp Med 1994; 179: 269-277.
    • (1994) J. Exp. Med. , vol.179 , pp. 269-277
    • Hailman, E.1    Lichenstein, H.S.2    Wurfel, M.M.3
  • 5
    • 0032509295 scopus 로고    scopus 로고
    • Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: Mutations in Tlr4 gene
    • Poltorak A, He XL, 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.L.2    Smirnova, I.3
  • 6
    • 0030437795 scopus 로고    scopus 로고
    • Structural and functional diversity in the leucine rich repeat family of proteins
    • Buchanan SGS, Gay NJ. Structural and functional diversity in the leucine rich repeat family of proteins. Prog Biophys Mol Biol 1996; 65: 1-44.
    • (1996) Prog. Biophys. Mol. Biol. , vol.65 , pp. 1-44
    • Buchanan, S.G.S.1    Gay, N.J.2
  • 8
    • 0029730738 scopus 로고    scopus 로고
    • A conserved signaling pathway: The Drosophila Toll-dorsal pathway
    • Belvin MP, Anderson KV. 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
  • 9
    • 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 JM, Hoffmann JA. 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.M.4    Hoffmann, J.A.5
  • 11
    • 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, DeLotto R. Proteolytic processing of the Drosophila Spatzle protein by Easter generates a dimeric NGF-like molecule with ventralising activity. Mech Dev 1998; 72: 141-148.
    • (1998) Mech. Dev. , vol.72 , pp. 141-148
    • DeLotto, Y.1    DeLotto, R.2
  • 12
    • 0037025213 scopus 로고    scopus 로고
    • Activation of Drosophila Toll during fungal infection by a blood serine protease
    • Ligoxygakis P, Pelte N, Hoffmann JA, Reichhart JM. Activation of Drosophila Toll during fungal infection by a blood serine protease. Science 2002; 297: 114-116.
    • (2002) Science , vol.297 , pp. 114-116
    • Ligoxygakis, P.1    Pelte, N.2    Hoffmann, J.A.3    Reichhart, J.M.4
  • 13
    • 0041989575 scopus 로고    scopus 로고
    • Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling
    • Weber A, Tauszig-Delamasure S, Hoffmann J et al. Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling. Nat Immunol 2003; 4: 794-800.
    • (2003) Nat. Immunol. , vol.4 , pp. 794-800
    • Weber, A.1    Tauszig-Delamasure, S.2    Hoffmann, J.3
  • 14
    • 0035479747 scopus 로고    scopus 로고
    • A family of proteins related to Spatzle, the Toll receptor ligand, are encoded in the Drosophila genome
    • Parker JS, Mizuguchi K, Gay NJ. A family of proteins related to Spatzle, the Toll receptor ligand, are encoded in the Drosophila genome. Proteins 2001; 45: 71-80.
    • (2001) Proteins , vol.45 , pp. 71-80
    • Parker, J.S.1    Mizuguchi, K.2    Gay, N.J.3
  • 15
    • 1642384019 scopus 로고    scopus 로고
    • Innate recognition of lipopolysaccharide by Toll-like receptor 4-MD-2
    • Miyake K. Innate recognition of lipopolysaccharide by Toll-like receptor 4-MD-2. Trends Microbiol 2004; 12: 186-192.
    • (2004) Trends Microbiol. , vol.12 , pp. 186-192
    • Miyake, K.1
  • 16
    • 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
  • 17
    • 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 T, 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: 4186-4190.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4186-4190
    • Gioannini, T.1    Teghanemt, A.2    Zhang, D.3
  • 18
    • 0035796406 scopus 로고    scopus 로고
    • Molecular genetic analysis of an endotoxin nonresponder mutant cell Line: A point mutation in a conserved region of MD-2 abolishes endotoxin-induced signaling
    • Schromm AB, Lien E, Henneke P et al. Molecular genetic analysis of an endotoxin nonresponder mutant cell Line: a point mutation in a conserved region of MD-2 abolishes endotoxin-induced signaling. J Exp Med 2001; 194: 79-88.
    • (2001) J. Exp. Med. , vol.194 , pp. 79-88
    • Schromm, A.B.1    Lien, E.2    Henneke, P.3
  • 19
    • 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
  • 20
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol 1993; 234: 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 21
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi JY, Blundell TL, Mizuguchi K. FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 2001; 310: 243-257.
    • (2001) J. Mol. Biol. , vol.310 , pp. 243-257
    • Shi, J.Y.1    Blundell, T.L.2    Mizuguchi, K.3
  • 22
    • 0025804653 scopus 로고
    • Dominant and recessive mutations define functional domains of Toll, a transmembrane protein required for dorsal ventral polarity in the Drosophila embryo
    • Schneider DS, Hudson KL, Lin TY, Anderson KV. Dominant and recessive mutations define functional domains of Toll, a transmembrane protein required for dorsal ventral polarity in the Drosophila embryo. Gene Dev 1991; 5: 797-807.
    • (1991) Gene Dev. , vol.5 , pp. 797-807
    • Schneider, D.S.1    Hudson, K.L.2    Lin, T.Y.3    Anderson, K.V.4
  • 23
    • 20744451399 scopus 로고    scopus 로고
    • Ligand-receptor and receptor-receptor interactions act in concert to activate signalling in the Drosophila Toll pathway
    • Weber AN, Moncrieffe MC, Gangloff M, Imler JL, Gay NJ. Ligand-receptor and receptor-receptor interactions act in concert to activate signalling in the Drosophila Toll pathway. J Biol Chem 2005; 280: 22793-22799.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22793-22799
    • Weber, A.N.1    Moncrieffe, M.C.2    Gangloff, M.3    Imler, J.L.4    Gay, N.J.5
  • 24
    • 2442434770 scopus 로고    scopus 로고
    • Structure of nerve growth factor complexed with the shared neurotrophin receptor p75
    • He XL, Garcia KC. Structure of nerve growth factor complexed with the shared neurotrophin receptor p75. Science 2004; 304: 870-875.
    • (2004) Science , vol.304 , pp. 870-875
    • He, X.L.1    Garcia, K.C.2
  • 25
    • 0037292275 scopus 로고    scopus 로고
    • Functional diversity and regulation of different interleukin-1 receptor-associated kinase (IRAK) family members
    • Janssens S, Beyaert R. Functional diversity and regulation of different interleukin-1 receptor-associated kinase (IRAK) family members. Mol Cell 2003; 11: 293-302.
    • (2003) Mol. Cell. , vol.11 , pp. 293-302
    • Janssens, S.1    Beyaert, R.2
  • 26
    • 0036510366 scopus 로고    scopus 로고
    • Negative regulation of Toll-like receptor-mediated signaling by Tollip
    • Zhang G, Ghosh S. Negative regulation of Toll-like receptor-mediated signaling by Tollip. J Biol Chem 2002; 277: 7059-7065.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7059-7065
    • Zhang, G.1    Ghosh, S.2
  • 27
    • 3042645409 scopus 로고    scopus 로고
    • Multimerization and interaction of Toll and Spatzle in Drosophila
    • Hu X, Yagi Y, Tanji T, Zhou S, Ip YT. Multimerization and interaction of Toll and Spatzle in Drosophila. Proc Natl Acad Sci USA 2004; 101: 9369-9374.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9369-9374
    • Hu, X.1    Yagi, Y.2    Tanji, T.3    Zhou, S.4    Ip, Y.T.5
  • 28
    • 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
  • 29
    • 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
  • 30
    • 0037418188 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease
    • Friedland N, Liou HL, Lobel P, Stock AM. Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease. Proc Natl Acad Sci USA 2003; 100: 2512-2517.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2512-2517
    • Friedland, N.1    Liou, H.L.2    Lobel, P.3    Stock, A.M.4
  • 31
    • 9244251126 scopus 로고    scopus 로고
    • Function of the Drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria
    • Bischoff V, Vignal C, Boneca IG et al. Function of the Drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria. Nat Immunol 2004; 5: 1175-1180.
    • (2004) Nat. Immunol. , vol.5 , pp. 1175-1180
    • Bischoff, V.1    Vignal, C.2    Boneca, I.G.3
  • 32
    • 2442456719 scopus 로고    scopus 로고
    • Monomeric and polymeric Gram-negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway
    • Kaneko T, Goldman WE, Mellroth P et al. Monomeric and polymeric Gram-negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway. Immunity 2004; 20: 637-649.
    • (2004) Immunity , vol.20 , pp. 637-649
    • Kaneko, T.1    Goldman, W.E.2    Mellroth, P.3
  • 33
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson AD, Hofmann E, Coulton JW, Diederichs K, Welte W. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 1998; 282: 2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.