메뉴 건너뛰기




Volumn 6, Issue 9, 2011, Pages

Comparative analysis of species-specific ligand recognition in toll-like receptor 8 signaling: A hypothesis

Author keywords

[No Author keywords available]

Indexed keywords

RESIQUIMOD; SINGLE STRANDED RNA; TOLL LIKE RECEPTOR 8; LIGAND;

EID: 80052938022     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025118     Document Type: Article
Times cited : (45)

References (66)
  • 1
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S, Uematsu S, Takeuchi O, (2006) Pathogen recognition and innate immunity. Cell 124: 783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 4
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira S, Takeda K, (2004) Toll-like receptor signalling. Nat Rev Immunol 4: 499-511.
    • (2004) Nat Rev Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 5
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B, Kajava AV, (2001) The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol 11: 725-732.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 6
    • 61849170035 scopus 로고    scopus 로고
    • TLRs and innate immunity
    • Beutler BA, (2009) TLRs and innate immunity. Blood 113: 1399-1407.
    • (2009) Blood , vol.113 , pp. 1399-1407
    • Beutler, B.A.1
  • 7
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors
    • Kawai T, Akira S, (2010) The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat Immunol 11: 373-384.
    • (2010) Nat Immunol , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 8
    • 84904369534 scopus 로고    scopus 로고
    • Pathogen recognition by innate immunity and its signaling
    • Akira S, (2009) Pathogen recognition by innate immunity and its signaling. Proc Jpn Acad Ser B Phys Biol Sci 85: 143-156.
    • (2009) Proc Jpn Acad Ser B Phys Biol Sci , vol.85 , pp. 143-156
    • Akira, S.1
  • 10
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • Park BS, Song DH, Kim HM, Choi BS, Lee H, et al. (2009) The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 458: 1191-1195.
    • (2009) Nature , vol.458 , pp. 1191-1195
    • Park, B.S.1    Song, D.H.2    Kim, H.M.3    Choi, B.S.4    Lee, H.5
  • 11
    • 34548608447 scopus 로고    scopus 로고
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
    • Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, et al. (2007) Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell 130: 1071-1082.
    • (2007) Cell , vol.130 , pp. 1071-1082
    • Jin, M.S.1    Kim, S.E.2    Heo, J.Y.3    Lee, M.E.4    Kim, H.M.5
  • 12
    • 42349090335 scopus 로고    scopus 로고
    • Structural basis of toll-like receptor 3 signaling with double-stranded RNA
    • Liu L, Botos I, Wang Y, Leonard JN, Shiloach J, et al. (2008) Structural basis of toll-like receptor 3 signaling with double-stranded RNA. Science 320: 379-381.
    • (2008) Science , vol.320 , pp. 379-381
    • Liu, L.1    Botos, I.2    Wang, Y.3    Leonard, J.N.4    Shiloach, J.5
  • 13
    • 23044445303 scopus 로고    scopus 로고
    • Crystal structure of human toll-like receptor 3 (TLR3) ectodomain
    • Choe J, Kelker MS, Wilson IA, (2005) Crystal structure of human toll-like receptor 3 (TLR3) ectodomain. Science 309: 581-585.
    • (2005) Science , vol.309 , pp. 581-585
    • Choe, J.1    Kelker, M.S.2    Wilson, I.A.3
  • 14
    • 71749118913 scopus 로고    scopus 로고
    • Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer
    • Kang JY, Nan X, Jin MS, Youn SJ, Ryu YH, et al. (2009) Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer. Immunity 31: 873-884.
    • (2009) Immunity , vol.31 , pp. 873-884
    • Kang, J.Y.1    Nan, X.2    Jin, M.S.3    Youn, S.J.4    Ryu, Y.H.5
  • 15
    • 34548222514 scopus 로고    scopus 로고
    • Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran
    • Kim HM, Park BS, Kim JI, Kim SE, Lee J, et al. (2007) Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Cell 130: 906-917.
    • (2007) Cell , vol.130 , pp. 906-917
    • Kim, H.M.1    Park, B.S.2    Kim, J.I.3    Kim, S.E.4    Lee, J.5
  • 17
    • 61349086647 scopus 로고    scopus 로고
    • Variation matters: TLR structure and species-specific pathogen recognition
    • Werling D, Jann OC, Offord V, Glass EJ, Coffey TJ, (2009) Variation matters: TLR structure and species-specific pathogen recognition. Trends Immunol 30: 124-130.
    • (2009) Trends Immunol , vol.30 , pp. 124-130
    • Werling, D.1    Jann, O.C.2    Offord, V.3    Glass, E.J.4    Coffey, T.J.5
  • 18
    • 36348962417 scopus 로고    scopus 로고
    • Combinational recognition of bacterial lipoproteins and peptidoglycan by chicken Toll-like receptor 2 subfamily
    • Higuchi M, Matsuo A, Shingai M, Shida K, Ishii A, et al. (2008) Combinational recognition of bacterial lipoproteins and peptidoglycan by chicken Toll-like receptor 2 subfamily. Dev Comp Immunol 32: 147-155.
    • (2008) Dev Comp Immunol , vol.32 , pp. 147-155
    • Higuchi, M.1    Matsuo, A.2    Shingai, M.3    Shida, K.4    Ishii, A.5
  • 19
    • 34249810031 scopus 로고    scopus 로고
    • The central leucine-rich repeat region of chicken TLR16 dictates unique ligand specificity and species-specific interaction with TLR2
    • Keestra AM, de Zoete MR, van Aubel RA, van Putten JP, (2007) The central leucine-rich repeat region of chicken TLR16 dictates unique ligand specificity and species-specific interaction with TLR2. J Immunol 178: 7110-7119.
    • (2007) J Immunol , vol.178 , pp. 7110-7119
    • Keestra, A.M.1    de Zoete, M.R.2    van Aubel, R.A.3    van Putten, J.P.4
  • 20
    • 0034002247 scopus 로고    scopus 로고
    • Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide
    • Lien E, Means TK, Heine H, Yoshimura A, Kusumoto S, et al. (2000) Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide. J Clin Invest 105: 497-504.
    • (2000) J Clin Invest , vol.105 , pp. 497-504
    • Lien, E.1    Means, T.K.2    Heine, H.3    Yoshimura, A.4    Kusumoto, S.5
  • 21
    • 35448968699 scopus 로고    scopus 로고
    • The equine TLR4/MD-2 complex mediates recognition of lipopolysaccharide from Rhodobacter sphaeroides as an agonist
    • Lohmann KL, Vandenplas ML, Barton MH, Bryant CE, Moore JN, (2007) The equine TLR4/MD-2 complex mediates recognition of lipopolysaccharide from Rhodobacter sphaeroides as an agonist. J Endotoxin Res 13: 235-242.
    • (2007) J Endotoxin Res , vol.13 , pp. 235-242
    • Lohmann, K.L.1    Vandenplas, M.L.2    Barton, M.H.3    Bryant, C.E.4    Moore, J.N.5
  • 22
    • 58949092384 scopus 로고    scopus 로고
    • Host species-specific usage of the TLR4-LPS receptor complex
    • Lizundia R, Sauter KS, Taylor G, Werling D, (2008) Host species-specific usage of the TLR4-LPS receptor complex. Innate Immun 14: 223-231.
    • (2008) Innate Immun , vol.14 , pp. 223-231
    • Lizundia, R.1    Sauter, K.S.2    Taylor, G.3    Werling, D.4
  • 23
    • 33847106037 scopus 로고    scopus 로고
    • A conserved surface on Toll-like receptor 5 recognizes bacterial flagellin
    • Andersen-Nissen E, Smith KD, Bonneau R, Strong RK, Aderem A, (2007) A conserved surface on Toll-like receptor 5 recognizes bacterial flagellin. J Exp Med 204: 393-403.
    • (2007) J Exp Med , vol.204 , pp. 393-403
    • Andersen-Nissen, E.1    Smith, K.D.2    Bonneau, R.3    Strong, R.K.4    Aderem, A.5
  • 24
    • 59249095900 scopus 로고    scopus 로고
    • Characterization of bovine Toll-like receptor 8: ligand specificity, signaling essential sites and dimerization
    • Zhu J, Brownlie R, Liu Q, Babiuk LA, Potter A, et al. (2009) Characterization of bovine Toll-like receptor 8: ligand specificity, signaling essential sites and dimerization. Mol Immunol 46: 978-990.
    • (2009) Mol Immunol , vol.46 , pp. 978-990
    • Zhu, J.1    Brownlie, R.2    Liu, Q.3    Babiuk, L.A.4    Potter, A.5
  • 25
    • 43449132981 scopus 로고    scopus 로고
    • Porcine TLR8 and TLR7 are both activated by a selective TLR7 ligand, imiquimod
    • Zhu J, Lai K, Brownile R, Babiuk LA, Mutwiri GK, (2008) Porcine TLR8 and TLR7 are both activated by a selective TLR7 ligand, imiquimod. Mol Immunol 45: 3238-3243.
    • (2008) Mol Immunol , vol.45 , pp. 3238-3243
    • Zhu, J.1    Lai, K.2    Brownile, R.3    Babiuk, L.A.4    Mutwiri, G.K.5
  • 26
    • 0036008014 scopus 로고    scopus 로고
    • Small anti-viral compounds activate immune cells via the TLR7 MyD88-dependent signaling pathway
    • Hemmi H, Kaisho T, Takeuchi O, Sato S, Sanjo H, et al. (2002) Small anti-viral compounds activate immune cells via the TLR7 MyD88-dependent signaling pathway. Nat Immunol 3: 196-200.
    • (2002) Nat Immunol , vol.3 , pp. 196-200
    • Hemmi, H.1    Kaisho, T.2    Takeuchi, O.3    Sato, S.4    Sanjo, H.5
  • 27
    • 0036088492 scopus 로고    scopus 로고
    • Human TLR7 or TLR8 independently confer responsiveness to the antiviral compound R-848
    • Jurk M, Heil F, Vollmer J, Schetter C, Krieg AM, et al. (2002) Human TLR7 or TLR8 independently confer responsiveness to the antiviral compound R-848. Nat Immunol 3: 499.
    • (2002) Nat Immunol , vol.3 , pp. 499
    • Jurk, M.1    Heil, F.2    Vollmer, J.3    Schetter, C.4    Krieg, A.M.5
  • 28
    • 0242391997 scopus 로고    scopus 로고
    • The Toll-like receptor 7 (TLR7)-specific stimulus loxoribine uncovers a strong relationship within the TLR7, 8 and 9 subfamily
    • Heil F, Ahmad-Nejad P, Hemmi H, Hochrein H, Ampenberger F, et al. (2003) The Toll-like receptor 7 (TLR7)-specific stimulus loxoribine uncovers a strong relationship within the TLR7, 8 and 9 subfamily. Eur J Immunol 33: 2987-2997.
    • (2003) Eur J Immunol , vol.33 , pp. 2987-2997
    • Heil, F.1    Ahmad-Nejad, P.2    Hemmi, H.3    Hochrein, H.4    Ampenberger, F.5
  • 29
    • 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, Ampenberger F, Kirschning C, et al. (2004) Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8. Science 303: 1526-1529.
    • (2004) Science , vol.303 , pp. 1526-1529
    • Heil, F.1    Hemmi, H.2    Hochrein, H.3    Ampenberger, F.4    Kirschning, C.5
  • 30
    • 33947668943 scopus 로고    scopus 로고
    • Viral recognition by Toll-like receptors
    • Barton GM, (2007) Viral recognition by Toll-like receptors. Semin Immunol 19: 33-40.
    • (2007) Semin Immunol , vol.19 , pp. 33-40
    • Barton, G.M.1
  • 31
    • 0043192812 scopus 로고    scopus 로고
    • The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense
    • Di Matteo A, Federici L, Mattei B, Salvi G, Johnson KA, et al. (2003) The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense. Proc Natl Acad Sci U S A 100: 10124-10128.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10124-10128
    • Di Matteo, A.1    Federici, L.2    Mattei, B.3    Salvi, G.4    Johnson, K.A.5
  • 32
    • 77955093470 scopus 로고    scopus 로고
    • TollML: a database of toll-like receptor structural motifs
    • Gong J, Wei T, Zhang N, Jamitzky F, Heckl WM, et al. (2010) TollML: a database of toll-like receptor structural motifs. J Mol Model 16: 1283-1289.
    • (2010) J Mol Model , vol.16 , pp. 1283-1289
    • Gong, J.1    Wei, T.2    Zhang, N.3    Jamitzky, F.4    Heckl, W.M.5
  • 34
    • 0346882663 scopus 로고    scopus 로고
    • ModLoop: automated modeling of loops in protein structures
    • Fiser A, Sali A, (2003) ModLoop: automated modeling of loops in protein structures. Bioinformatics 19: 2500-2501.
    • (2003) Bioinformatics , vol.19 , pp. 2500-2501
    • Fiser, A.1    Sali, A.2
  • 35
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang J, Cieplak P, Kollman PA, (2000) How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? Journal of Computational Chemistry 21: 1049-1074.
    • (2000) Journal of Computational Chemistry , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 37
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM, (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8: 477-486.
    • (1996) J Biomol NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 38
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: assessment of protein models with three-dimensional profiles
    • Eisenberg D, Luthy R, Bowie JU, (1997) VERIFY3D: assessment of protein models with three-dimensional profiles. Methods Enzymol 277: 396-404.
    • (1997) Methods Enzymol , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.U.3
  • 39
    • 0027180507 scopus 로고
    • Verification of protein structures: patterns of nonbonded atomic interactions
    • Colovos C, Yeates TO, (1993) Verification of protein structures: patterns of nonbonded atomic interactions. Protein Sci 2: 1511-1519.
    • (1993) Protein Sci , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 40
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins
    • Wiederstein M, Sippl MJ, (2007) ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res 35: W407-410.
    • (2007) Nucleic Acids Res , vol.35 , pp. 407-410
    • Wiederstein, M.1    Sippl, M.J.2
  • 41
    • 33747840389 scopus 로고    scopus 로고
    • GRAMM-X public web server for protein-protein docking
    • Tovchigrechko A, Vakser IA, (2006) GRAMM-X public web server for protein-protein docking. Nucleic Acids Res 34: W310-314.
    • (2006) Nucleic Acids Res , vol.34 , pp. 310-314
    • Tovchigrechko, A.1    Vakser, I.A.2
  • 43
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: an automated docking and discrimination method for the prediction of protein complexes
    • Comeau SR, Gatchell DW, Vajda S, Camacho CJ, (2004) ClusPro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20: 45-50.
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 44
    • 74049093947 scopus 로고    scopus 로고
    • Application of the PM6 semi-empirical method to modeling proteins enhances docking accuracy of AutoDock
    • Bikadi Z, Hazai E, (2009) Application of the PM6 semi-empirical method to modeling proteins enhances docking accuracy of AutoDock. J Cheminform 1: 15.
    • (2009) J Cheminform , vol.1 , pp. 15
    • Bikadi, Z.1    Hazai, E.2
  • 45
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
    • Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, et al. (2009) AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. J Comput Chem 30: 2785-2791.
    • (2009) J Comput Chem , vol.30 , pp. 2785-2791
    • Morris, G.M.1    Huey, R.2    Lindstrom, W.3    Sanner, M.F.4    Belew, R.K.5
  • 47
    • 45549086115 scopus 로고    scopus 로고
    • The crystal structure of the human toll-like receptor 10 cytoplasmic domain reveals a putative signaling dimer
    • Nyman T, Stenmark P, Flodin S, Johansson I, Hammarstrom M, et al. (2008) The crystal structure of the human toll-like receptor 10 cytoplasmic domain reveals a putative signaling dimer. J Biol Chem 283: 11861-11865.
    • (2008) J Biol Chem , vol.283 , pp. 11861-11865
    • Nyman, T.1    Stenmark, P.2    Flodin, S.3    Johansson, I.4    Hammarstrom, M.5
  • 49
    • 33748065439 scopus 로고    scopus 로고
    • Conserved features in the extracellular domain of human toll-like receptor 8 are essential for pH-dependent signaling
    • Gibbard RJ, Morley PJ, Gay NJ, (2006) Conserved features in the extracellular domain of human toll-like receptor 8 are essential for pH-dependent signaling. J Biol Chem 281: 27503-27511.
    • (2006) J Biol Chem , vol.281 , pp. 27503-27511
    • Gibbard, R.J.1    Morley, P.J.2    Gay, N.J.3
  • 50
    • 34347209992 scopus 로고    scopus 로고
    • Comparative sequence analysis of leucine-rich repeats (LRRs) within vertebrate toll-like receptors
    • Matsushima N, Tanaka T, Enkhbayar P, Mikami T, Taga M, et al. (2007) Comparative sequence analysis of leucine-rich repeats (LRRs) within vertebrate toll-like receptors. BMC Genomics 8: 124.
    • (2007) BMC Genomics , vol.8 , pp. 124
    • Matsushima, N.1    Tanaka, T.2    Enkhbayar, P.3    Mikami, T.4    Taga, M.5
  • 51
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL, Mizuguchi K, (2001) FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 310: 243-257.
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 52
    • 77958589003 scopus 로고    scopus 로고
    • Molecular modeling-based evaluation of hTLR10 and identification of potential ligands in Toll-like receptor signaling
    • Govindaraj RG, Manavalan B, Lee G, Choi S, (2010) Molecular modeling-based evaluation of hTLR10 and identification of potential ligands in Toll-like receptor signaling. PloS one 5: e12713.
    • (2010) PloS One , vol.5
    • Govindaraj, R.G.1    Manavalan, B.2    Lee, G.3    Choi, S.4
  • 53
    • 80052294520 scopus 로고    scopus 로고
    • In silico approach to inhibition of signaling pathways of toll-like receptors 2 and 4 by ST2L
    • Basith S, Manavalan B, Govindaraj RG, Choi S, (2011) In silico approach to inhibition of signaling pathways of toll-like receptors 2 and 4 by ST2L. PloS one 6: e23989.
    • (2011) PloS One , vol.6
    • Basith, S.1    Manavalan, B.2    Govindaraj, R.G.3    Choi, S.4
  • 54
    • 34250698370 scopus 로고    scopus 로고
    • Ligand-induced conformational changes allosterically activate Toll-like receptor 9
    • Latz E, Verma A, Visintin A, Gong M, Sirois CM, et al. (2007) Ligand-induced conformational changes allosterically activate Toll-like receptor 9. Nat Immunol 8: 772-779.
    • (2007) Nat Immunol , vol.8 , pp. 772-779
    • Latz, E.1    Verma, A.2    Visintin, A.3    Gong, M.4    Sirois, C.M.5
  • 55
    • 0031282514 scopus 로고    scopus 로고
    • Induction of cytokines in cynomolgus monkeys by the immune response modifiers, imiquimod, S-27609 and S-28463
    • Wagner TL, Horton VL, Carlson GL, Myhre PE, Gibson SJ, et al. (1997) Induction of cytokines in cynomolgus monkeys by the immune response modifiers, imiquimod, S-27609 and S-28463. Cytokine 9: 837-845.
    • (1997) Cytokine , vol.9 , pp. 837-845
    • Wagner, T.L.1    Horton, V.L.2    Carlson, G.L.3    Myhre, P.E.4    Gibson, S.J.5
  • 56
    • 0031900829 scopus 로고    scopus 로고
    • Cytokine induction in hairless mouse and rat skin after topical application of the immune response modifiers imiquimod and S-28463
    • Imbertson LM, Beaurline JM, Couture AM, Gibson SJ, Smith RM, et al. (1998) Cytokine induction in hairless mouse and rat skin after topical application of the immune response modifiers imiquimod and S-28463. J Invest Dermatol 110: 734-739.
    • (1998) J Invest Dermatol , vol.110 , pp. 734-739
    • Imbertson, L.M.1    Beaurline, J.M.2    Couture, A.M.3    Gibson, S.J.4    Smith, R.M.5
  • 57
    • 0035869132 scopus 로고    scopus 로고
    • Daily or weekly therapy with resiquimod (R-848) reduces genital recurrences in herpes simplex virus-infected guinea pigs during and after treatment
    • Bernstein DI, Harrison CJ, Tomai MA, Miller RL, (2001) Daily or weekly therapy with resiquimod (R-848) reduces genital recurrences in herpes simplex virus-infected guinea pigs during and after treatment. J Infect Dis 183: 844-849.
    • (2001) J Infect Dis , vol.183 , pp. 844-849
    • Bernstein, D.I.1    Harrison, C.J.2    Tomai, M.A.3    Miller, R.L.4
  • 58
    • 0343485063 scopus 로고    scopus 로고
    • The imidazoquinolines, imiquimod and R-848, induce functional, but not phenotypic, maturation of human epidermal Langerhans' cells
    • Burns RP Jr, Ferbel B, Tomai M, Miller R, Gaspari AA, (2000) The imidazoquinolines, imiquimod and R-848, induce functional, but not phenotypic, maturation of human epidermal Langerhans' cells. Clin Immunol 94: 13-23.
    • (2000) Clin Immunol , vol.94 , pp. 13-23
    • Burns Jr., R.P.1    Ferbel, B.2    Tomai, M.3    Miller, R.4    Gaspari, A.A.5
  • 59
    • 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, Luppa P, Lipford GB, et al. (2004) Toll-like receptor 9 binds single-stranded CpG-DNA in a sequence- and pH-dependent manner. Eur J Immunol 34: 2541-2550.
    • (2004) Eur J Immunol , vol.34 , pp. 2541-2550
    • Rutz, M.1    Metzger, J.2    Gellert, T.3    Luppa, P.4    Lipford, G.B.5
  • 60
    • 74449089424 scopus 로고    scopus 로고
    • A five-amino-acid motif in the undefined region of the TLR8 ectodomain is required for species-specific ligand recognition
    • Liu J, Xu C, Hsu LC, Luo Y, Xiang R, et al. (2010) A five-amino-acid motif in the undefined region of the TLR8 ectodomain is required for species-specific ligand recognition. Mol Immunol 47: 1083-1090.
    • (2010) Mol Immunol , vol.47 , pp. 1083-1090
    • Liu, J.1    Xu, C.2    Hsu, L.C.3    Luo, Y.4    Xiang, R.5
  • 61
    • 67749108047 scopus 로고    scopus 로고
    • Homology modeling of human Toll-like receptors TLR7, 8, and 9 ligand-binding domains
    • Wei T, Gong J, Jamitzky F, Heckl WM, Stark RW, et al. (2009) Homology modeling of human Toll-like receptors TLR7, 8, and 9 ligand-binding domains. Protein Sci 18: 1684-1691.
    • (2009) Protein Sci , vol.18 , pp. 1684-1691
    • Wei, T.1    Gong, J.2    Jamitzky, F.3    Heckl, W.M.4    Stark, R.W.5
  • 62
    • 33750823681 scopus 로고    scopus 로고
    • Cutting edge: activation of murine TLR8 by a combination of imidazoquinoline immune response modifiers and polyT oligodeoxynucleotides
    • Gorden KK, Qiu XX, Binsfeld CC, Vasilakos JP, Alkan SS, (2006) Cutting edge: activation of murine TLR8 by a combination of imidazoquinoline immune response modifiers and polyT oligodeoxynucleotides. Journal of immunology 177: 6584-6587.
    • (2006) Journal of Immunology , vol.177 , pp. 6584-6587
    • Gorden, K.K.1    Qiu, X.X.2    Binsfeld, C.C.3    Vasilakos, J.P.4    Alkan, S.S.5
  • 63
    • 0036088519 scopus 로고    scopus 로고
    • Selective allosteric enhancement of agonist binding and function at human A3 adenosine receptors by a series of imidazoquinoline derivatives
    • Gao ZG, Kim SG, Soltysiak KA, Melman N, AP IJ, et al. (2002) Selective allosteric enhancement of agonist binding and function at human A3 adenosine receptors by a series of imidazoquinoline derivatives. Molecular pharmacology 62: 81-89.
    • (2002) Molecular Pharmacology , vol.62 , pp. 81-89
    • Gao, Z.G.1    Kim, S.G.2    Soltysiak, K.A.3    Melman, N.4    Ap, I.J.5
  • 64
    • 33746266273 scopus 로고    scopus 로고
    • Modulating responsiveness of human TLR7 and 8 to small molecule ligands with T-rich phosphorothiate oligodeoxynucleotides
    • Jurk M, Kritzler A, Schulte B, Tluk S, Schetter C, et al. (2006) Modulating responsiveness of human TLR7 and 8 to small molecule ligands with T-rich phosphorothiate oligodeoxynucleotides. European journal of immunology 36: 1815-1826.
    • (2006) European Journal of Immunology , vol.36 , pp. 1815-1826
    • Jurk, M.1    Kritzler, A.2    Schulte, B.3    Tluk, S.4    Schetter, C.5
  • 65
    • 0036570169 scopus 로고    scopus 로고
    • Quantitative expression of toll-like receptor 1-10 mRNA in cellular subsets of human peripheral blood mononuclear cells and sensitivity to CpG oligodeoxynucleotides
    • Hornung V, Rothenfusser S, Britsch S, Krug A, Jahrsdorfer B, et al. (2002) Quantitative expression of toll-like receptor 1-10 mRNA in cellular subsets of human peripheral blood mononuclear cells and sensitivity to CpG oligodeoxynucleotides. Journal of immunology 168: 4531-4537.
    • (2002) Journal of Immunology , vol.168 , pp. 4531-4537
    • Hornung, V.1    Rothenfusser, S.2    Britsch, S.3    Krug, A.4    Jahrsdorfer, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.