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Volumn 21, Issue 8, 2016, Pages

Computational Approaches to Toll-Like Receptor 4 Modulation

Author keywords

Computational chemistry; Docking; Drug design; Homology modeling; Md simulations; Molecular recognition; Tlr4 md 2 modulators; Toll like receptor 4; Virtual screening

Indexed keywords

LIPOPOLYSACCHARIDE; LY96 PROTEIN, HUMAN; MOLECULAR LIBRARY; PROTEIN MD 2; TLR4 PROTEIN, HUMAN; TOLL LIKE RECEPTOR 4;

EID: 84982732343     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules21080994     Document Type: Review
Times cited : (67)

References (87)
  • 1
    • 0036451206 scopus 로고    scopus 로고
    • TLR4 as the mammalian endotoxin sensor
    • Beutler, B. TLR4 as the mammalian endotoxin sensor. Curr. Top. Microbiol. Immunol. 2002, 270, 109-120.
    • (2002) Curr. Top. Microbiol. Immunol , vol.270 , pp. 109-120
    • Beutler, B.1
  • 2
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira, S.; Takeda, K. Toll-like receptor signalling. Nat. Rev. Immunol. 2004, 4, 499-511.
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 5
    • 77950591965 scopus 로고    scopus 로고
    • MD-2-mediated ionic interactions between lipid A and TLR4 are essential for receptor activation
    • Meng, J.; Lien, E.; Golenbock, D.T. MD-2-mediated ionic interactions between lipid A and TLR4 are essential for receptor activation. J. Biol. Chem. 2010, 285, 8695-8702.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8695-8702
    • Meng, J.1    Lien, E.2    Golenbock, D.T.3
  • 7
    • 84940563505 scopus 로고    scopus 로고
    • Activation of human Toll-like receptor 4 (TLR4)· myeloid differentiation factor 2 (MD-2) by hypoacylated lipopolysaccharide from a clinical isolate of burkholderia cenocepacia
    • Di Lorenzo, F.; Kubik,Ł.; Oblak, A.; Lorè, N.I.; Cigana, C.; Lanzetta, R.; Parrilli, M.; Hamad, M.A.; de Soyza, A.; Silipo, A. Activation of human Toll-like receptor 4 (TLR4)· myeloid differentiation factor 2 (MD-2) by hypoacylated lipopolysaccharide from a clinical isolate of burkholderia cenocepacia. J. Biol. Chem. 2015, 290, 21305-21319.
    • (2015) J. Biol. Chem , vol.290 , pp. 21305-21319
    • Di Lorenzo, F.1    Kubik, Ł.2    Oblak, A.3    Lorè, N.I.4    Cigana, C.5    Lanzetta, R.6    Parrilli, M.7    Hamad, M.A.8    De Soyza, A.9    Silipo, A.10
  • 8
    • 84929996030 scopus 로고    scopus 로고
    • Bordetella pertussis lipid A recognition by Toll-like receptor 4 and MD-2 is dependent on distinct charged and uncharged interfaces
    • Maeshima, N.; Evans-Atkinson, T.; Hajjar, A.M.; Fernandez, R.C. Bordetella pertussis lipid A recognition by Toll-like receptor 4 and MD-2 is dependent on distinct charged and uncharged interfaces. J. Biol. Chem. 2015, 290, 13440-13453.
    • (2015) J. Biol. Chem. , vol.290 , pp. 13440-13453
    • Maeshima, N.1    Evans-Atkinson, T.2    Hajjar, A.M.3    Fernandez, R.C.4
  • 9
    • 84860832650 scopus 로고    scopus 로고
    • Structural basis of species-specific endotoxin sensing by innate immune receptor TLR4/MD-2
    • Ohto, U.; Fukase, K.; Miyake, K.; Shimizu, T. Structural basis of species-specific endotoxin sensing by innate immune receptor TLR4/MD-2. Proc. Natl. Acad. Sci. USA 2012, 109, 7421-7426.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 7421-7426
    • Ohto, U.1    Fukase, K.2    Miyake, K.3    Shimizu, T.4
  • 10
    • 67649386535 scopus 로고    scopus 로고
    • Essential roles of hydrophobic residues in both MD-2 and Toll-like receptor 4 in activation by endotoxin
    • Resman, N.; Vašl, J.; Oblak, A.; Pristovšek, P.; Gioannini, T.L.; Weiss, J.P.; Jerala, R. Essential roles of hydrophobic residues in both MD-2 and Toll-like receptor 4 in activation by endotoxin. J. Biol. Chem. 2009, 284, 15052-15060.
    • (2009) J. Biol. Chem. , vol.284 , pp. 15052-15060
    • Resman, N.1    Vašl, J.2    Oblak, A.3    Pristovšek, P.4    Gioannini, T.L.5    Weiss, J.P.6    Jerala, R.7
  • 11
    • 34250813748 scopus 로고    scopus 로고
    • Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa
    • Ohto, U.; Fukase, K.; Miyake, K.; Satow, Y. Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa. Science 2007, 316, 1632-1634.
    • (2007) Science , vol.316 , pp. 1632-1634
    • Ohto, U.1    Fukase, K.2    Miyake, K.3    Satow, Y.4
  • 12
    • 84902198504 scopus 로고    scopus 로고
    • Reviewing and identifying amino acids of human, murine, canine and equine TLR4/MD-2 receptor complexes conferring endotoxic innate immunity activation by LPS/lipid A, or antagonistic effects by eritoran, in contrast to species-dependent modulation by lipid IVa
    • Scior, T.; Alexander, C.; Zaehringer, U. Reviewing and identifying amino acids of human, murine, canine and equine TLR4/MD-2 receptor complexes conferring endotoxic innate immunity activation by LPS/lipid A, or antagonistic effects by eritoran, in contrast to species-dependent modulation by lipid IVa. Comput. Struct. Biotechnol. J. 2013, 5, 1-13.
    • (2013) Comput. Struct. Biotechnol. J. , vol.5 , pp. 1-13
    • Scior, T.1    Alexander, C.2    Zaehringer, U.3
  • 14
    • 84902171021 scopus 로고    scopus 로고
    • Three-dimensional mapping of differential amino acids of human, murine, canine and equine TLR4/MD-2 receptor complexes conferring endotoxic activation by lipid A, antagonism by eritoran and species-dependent activities of lipid IVa in the mammalian lps sensor system
    • Scior, T.; Lozano-Aponte, J.; Figueroa-Vazquez, V.; Yunes-Rojas, J.A.; Zähringer, U.; Alexander, C. Three-dimensional mapping of differential amino acids of human, murine, canine and equine TLR4/MD-2 receptor complexes conferring endotoxic activation by lipid A, antagonism by eritoran and species-dependent activities of lipid IVa in the mammalian lps sensor system. Comput. Struct. Biotechnol. J. 2013, 7, 1-11.
    • (2013) Comput. Struct. Biotechnol. J. , vol.7 , pp. 1-11
    • Scior, T.1    Lozano-Aponte, J.2    Figueroa-Vazquez, V.3    Yunes-Rojas, J.A.4    Zähringer, U.5    Alexander, C.6
  • 15
    • 84900320851 scopus 로고    scopus 로고
    • Toll-like receptor 4 (TLR4) modulation by synthetic and natural compounds: An update
    • Peri, F.; Calabrese, V. Toll-like receptor 4 (TLR4) modulation by synthetic and natural compounds: An update. J. Med. Chem. 2014, 57, 3612-3622.
    • (2014) J. Med. Chem. , vol.57 , pp. 3612-3622
    • Peri, F.1    Calabrese, V.2
  • 17
    • 84874809137 scopus 로고    scopus 로고
    • Lipid A from lipopolysaccharide recognition: Structure, dynamics and cooperativity by molecular dynamics simulations
    • Garate, J.A.; Oostenbrink, C. Lipid A from lipopolysaccharide recognition: Structure, dynamics and cooperativity by molecular dynamics simulations. Proteins Struct. Funct. Bioinf. 2013, 81, 658-674.
    • (2013) Proteins Struct. Funct. Bioinf. , vol.81 , pp. 658-674
    • Garate, J.A.1    Oostenbrink, C.2
  • 18
    • 82455198557 scopus 로고    scopus 로고
    • From agonist to antagonist: Structure and dynamics of innate immune glycoprotein MD-2 upon recognition of variably acylated bacterial endotoxins
    • DeMarco, M.L.; Woods, R.J. From agonist to antagonist: Structure and dynamics of innate immune glycoprotein MD-2 upon recognition of variably acylated bacterial endotoxins. Mol. Immunol. 2011, 49, 124-133.
    • (2011) Mol. Immunol , vol.49 , pp. 124-133
    • DeMarco, M.L.1    Woods, R.J.2
  • 19
    • 84890959830 scopus 로고    scopus 로고
    • The structural basis for endotoxin-induced allosteric regulation of the Toll-like receptor 4 (TLR4) innate immune receptor
    • Paramo, T.; Piggot, T.J.; Bryant, C.E.; Bond, P.J. The structural basis for endotoxin-induced allosteric regulation of the Toll-like receptor 4 (TLR4) innate immune receptor. J. Biol. Chem. 2013, 288, 36215-36225.
    • (2013) J. Biol. Chem. , vol.288 , pp. 36215-36225
    • Paramo, T.1    Piggot, T.J.2    Bryant, C.E.3    Bond, P.J.4
  • 20
    • 84860870432 scopus 로고    scopus 로고
    • NMR studies of hexaacylated endotoxin bound to wild-type and F126A mutant MD-2 and MD-2 TLR4 ectodomain complexes
    • Yu, L.; Phillips, R.L.; Zhang, D.; Teghanemt, A.; Weiss, J.P.; Gioannini, T.L. NMR studies of hexaacylated endotoxin bound to wild-type and F126A mutant MD-2 and MD-2 TLR4 ectodomain complexes. J. Biol. Chem. 2012, 287, 16346-16355.
    • (2012) J. Biol. Chem. , vol.287 , pp. 16346-16355
    • Yu, L.1    Phillips, R.L.2    Zhang, D.3    Teghanemt, A.4    Weiss, J.P.5    Gioannini, T.L.6
  • 21
    • 84937577161 scopus 로고    scopus 로고
    • Dynamics on human Toll-like receptor 4 complexation to MD-2: The coreceptor stabilizing function
    • De Aguiar, C.; Costa, M.G.; Verli, H. Dynamics on human Toll-like receptor 4 complexation to MD-2: The coreceptor stabilizing function. Proteins Struct. Funct. Bioinf. 2015, 83, 373-382.
    • (2015) Proteins Struct. Funct. Bioinf , vol.83 , pp. 373-382
    • De Aguiar, C.1    Costa, M.G.2    Verli, H.3
  • 22
    • 84942750883 scopus 로고    scopus 로고
    • Insights into the species-specific TLR4 signaling mechanism in response to Rhodobacter sphaeroides lipid A detection
    • Anwar, M.A.; Panneerselvam, S.; Shah, M.; Choi, S. Insights into the species-specific TLR4 signaling mechanism in response to Rhodobacter sphaeroides lipid A detection. Sci. Rep. 2015, 5, 7657.
    • (2015) Sci. Rep , vol.5 , pp. 7657
    • Anwar, M.A.1    Panneerselvam, S.2    Shah, M.3    Choi, S.4
  • 26
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O.; Olson, A.J. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 2010, 31, 455-461.
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 28
    • 84962016594 scopus 로고    scopus 로고
    • Molecular basis of the functional differences between soluble human versus murine MD-2: Role of Val135 in transfer of lipopolysaccharide from CD14 to MD-2
    • Vašl, J.; Oblak, A.; Peternelj, T.T.; Klett, J.; Martín-Santamaría, S.; Gioannini, T.L.; Weiss, J.P.; Jerala, R. Molecular basis of the functional differences between soluble human versus murine MD-2: Role of Val135 in transfer of lipopolysaccharide from CD14 to MD-2. J. Immunol. 2016, 196, 2309-2318.
    • (2016) J. Immunol , vol.196 , pp. 2309-2318
    • Vašl, J.1    Oblak, A.2    Peternelj, T.T.3    Klett, J.4    Martín-Santamaría, S.5    Gioannini, T.L.6    Weiss, J.P.7    Jerala, R.8
  • 30
    • 70450106216 scopus 로고    scopus 로고
    • Improved prediction of protein side-chain conformations with SCWRL4
    • Krivov, G.G.; Shapovalov, M.V.; Dunbrack, R.L., Jr. Improved prediction of protein side-chain conformations with SCWRL4. Proteins 2009, 77, 778-795.
    • (2009) Proteins , vol.77 , pp. 778-795
    • Krivov, G.G.1    Shapovalov, M.V.2    Dunbrack, R.L.3
  • 32
    • 84982767748 scopus 로고    scopus 로고
    • accessed on 26 July 2016
    • Glide & Impact software. Available online: http://www.schrodinger.com (accessed on 26 July 2016).
    • Glide & Impact Software
  • 34
    • 78049435260 scopus 로고    scopus 로고
    • The cationic amphiphile 3,4-bis(tetradecyloxy)benzylamine inhibits LPS signaling by competing with endotoxin for CD14 binding
    • Piazza, M.; Calabrese, V.; Baruffa, C.; Gioannini, T.; Weiss, J.; Peri, F. The cationic amphiphile 3,4-bis(tetradecyloxy)benzylamine inhibits LPS signaling by competing with endotoxin for CD14 binding. Biochem. Pharmacol. 2010, 80, 2050-2056.
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 2050-2056
    • Piazza, M.1    Calabrese, V.2    Baruffa, C.3    Gioannini, T.4    Weiss, J.5    Peri, F.6
  • 36
    • 33747818007 scopus 로고    scopus 로고
    • Castp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas, J.; Ouyang, Z.; Tseng, J.; Binkowski, A.; Turpaz, Y.; Liang, J. Castp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 2006, 34, W116-W118.
    • (2006) Nucleic Acids Res , vol.34 , pp. W116-W118
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 37
    • 84949215654 scopus 로고    scopus 로고
    • Comparative protein structure modeling using modeller
    • Webb, B.; Sali, A. Comparative protein structure modeling using modeller. Curr. Protoc. Bioinform. 2014, 47.
    • (2014) Curr. Protoc. Bioinform , vol.47
    • Webb, B.1    Sali, A.2
  • 39
    • 84902349981 scopus 로고    scopus 로고
    • Identification of key residues that confer rhodobacter sphaeroides LPS activity at horse TLR4/MD-2
    • Irvine, K.L.; Gangloff, M.; Walsh, C.M.; Spring, D.R.; Gay, N.J.; Bryant, C.E. Identification of key residues that confer rhodobacter sphaeroides LPS activity at horse TLR4/MD-2. PLoS ONE 2014, 9, e98776.
    • (2014) PLoS ONE , vol.9 , pp. e98776
    • Irvine, K.L.1    Gangloff, M.2    Walsh, C.M.3    Spring, D.R.4    Gay, N.J.5    Bryant, C.E.6
  • 40
    • 0034723186 scopus 로고    scopus 로고
    • Mouse Toll-like receptor 4. MD-2 complex mediates lipopolysaccharide-mimetic signal transduction by taxol
    • Kawasaki, K.; Akashi, S.; Shimazu, R.; Yoshida, T.; Miyake, K.; Nishijima, M. Mouse Toll-like receptor 4.MD-2 complex mediates lipopolysaccharide-mimetic 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
  • 41
    • 0027227678 scopus 로고
    • Lipopolysaccharide antagonists block taxol-induced signaling in murine macrophages
    • Manthey, C.L.; Qureshi, N.; Stutz, P.L.; Vogel, S.N. Lipopolysaccharide antagonists block taxol-induced signaling in murine macrophages. J. Exp. Med. 1993, 178, 695-702.
    • (1993) J. Exp. Med. , vol.178 , pp. 695-702
    • Manthey, C.L.1    Qureshi, N.2    Stutz, P.L.3    Vogel, S.N.4
  • 44
    • 84872177473 scopus 로고    scopus 로고
    • accessed on 26 July 2016
    • Sybyl-x Suite. Available online: https://www.certara.com/software/molecular-modeling-and-simulation/ sybyl-x-suite/ (accessed on 26 July 2016).
    • Sybyl-X Suite
  • 45
    • 84957603841 scopus 로고    scopus 로고
    • Determination of the binding mode for anti-inflammatory natural product xanthohumol with myeloid differentiation protein 2
    • Fu, W.; Chen, L.; Wang, Z.; Zhao, C.; Chen, G.; Liu, X.; Dai, Y.; Cai, Y.; Li, C.; Zhou, J. Determination of the binding mode for anti-inflammatory natural product xanthohumol with myeloid differentiation protein 2. Drug Des. Dev. Ther. 2016, 10, 455-463.
    • (2016) Drug Des. Dev. Ther , vol.10 , pp. 455-463
    • Fu, W.1    Chen, L.2    Wang, Z.3    Zhao, C.4    Chen, G.5    Liu, X.6    Dai, Y.7    Cai, Y.8    Li, C.9    Zhou, J.10
  • 46
    • 84934966024 scopus 로고    scopus 로고
    • Insights into the binding mode of curcumin to MD-2: Studies from molecular docking, molecular dynamics simulations and experimental assessments
    • Wang, Z.; Chen, G.; Chen, L.; Liu, X.; Fu, W.; Zhang, Y.; Li, C.; Liang, G.; Cai, Y. Insights into the binding mode of curcumin to MD-2: Studies from molecular docking, molecular dynamics simulations and experimental assessments. Mol. Biosyst. 2015, 11, 1933-1938.
    • (2015) Mol. Biosyst , vol.11 , pp. 1933-1938
    • Wang, Z.1    Chen, G.2    Chen, L.3    Liu, X.4    Fu, W.5    Zhang, Y.6    Li, C.7    Liang, G.8    Cai, Y.9
  • 49
    • 84880470388 scopus 로고    scopus 로고
    • Sulforaphane inhibits the engagement of LPS with TLR4/MD2 complex by preferential binding to Cys133 in MD2
    • Koo, J.E.; Park, Z.-Y.; Kim, N.D.; Lee, J.Y. Sulforaphane inhibits the engagement of LPS with TLR4/MD2 complex by preferential binding to Cys133 in MD2. Biochem. Biophys. Res. Commun. 2013, 434, 600-605.
    • (2013) Biochem. Biophys. Res. Commun , vol.434 , pp. 600-605
    • Koo, J.E.1    Park, Z.Y.2    Kim, N.D.3    Lee, J.Y.4
  • 50
    • 84875472803 scopus 로고    scopus 로고
    • Suppression of Toll-like receptor 4 activation by caffeic acid phenethyl ester is mediated by interference of LPS binding to MD2. Br
    • Kim, S.Y.; Koo, J.E.; Seo, Y.J.; Tyagi, N.; Jeong, E.; Choi, J.; Lim, K.M.; Park, Z.Y.; Lee, J.Y. Suppression of Toll-like receptor 4 activation by caffeic acid phenethyl ester is mediated by interference of LPS binding to MD2. Br. J. Pharmacol. 2013, 168, 1933-1945.
    • (2013) J. Pharmacol. , vol.168 , pp. 1933-1945
    • Kim, S.Y.1    Koo, J.E.2    Seo, Y.J.3    Tyagi, N.4    Jeong, E.5    Choi, J.6    Lim, K.M.7    Park, Z.Y.8    Lee, J.Y.9
  • 54
    • 70350026412 scopus 로고    scopus 로고
    • Influence of apple polyphenols on inflammatory gene expression
    • Jung, M.; Triebel, S.; Anke, T.; Richling, E.; Erkel, G. Influence of apple polyphenols on inflammatory gene expression. Mol. Nutr. Food Res. 2009, 53, 1263-1280.
    • (2009) Mol. Nutr. Food Res , vol.53 , pp. 1263-1280
    • Jung, M.1    Triebel, S.2    Anke, T.3    Richling, E.4    Erkel, G.5
  • 55
    • 84939256315 scopus 로고    scopus 로고
    • Anti-inflammatory effect of procyanidin B1 on LPS-treated THP1 cells via interaction with the TLR4-MD-2 heterodimer and p38 MAPK and NF-κB signaling
    • Xing, J.; Li, R.; Li, N.; Zhang, J.; Li, Y.; Gong, P.; Gao, D.; Liu, H.; Zhang, Y. Anti-inflammatory effect of procyanidin B1 on LPS-treated THP1 cells via interaction with the TLR4-MD-2 heterodimer and p38 MAPK and NF-κB signaling. Mol. Cell. Biochem. 2015, 407, 89-95.
    • (2015) Mol. Cell. Biochem , vol.407 , pp. 89-95
    • Xing, J.1    Li, R.2    Li, N.3    Zhang, J.4    Li, Y.5    Gong, P.6    Gao, D.7    Liu, H.8    Zhang, Y.9
  • 57
    • 84945310707 scopus 로고    scopus 로고
    • Eritoran inhibits S100A8-mediated TLR4/MD-2 activation and tumor growth by changing the immune microenvironment
    • Deguchi, A.; Tomita, T.; Ohto, U.; Takemura, K.; Kitao, A.; Akashi-Takamura, S.; Miyake, K.; Maru, Y. Eritoran inhibits S100A8-mediated TLR4/MD-2 activation and tumor growth by changing the immune microenvironment. Oncogene 2016, 35, 1445-1456.
    • (2016) Oncogene , vol.35 , pp. 1445-1456
    • Deguchi, A.1    Tomita, T.2    Ohto, U.3    Takemura, K.4    Kitao, A.5    Akashi-Takamura, S.6    Miyake, K.7    Maru, Y.8
  • 58
    • 0038526303 scopus 로고    scopus 로고
    • Zdock: An initial-stage protein-docking algorithm
    • Chen, R.; Li, L.; Weng, Z. Zdock: An initial-stage protein-docking algorithm. Proteins 2003, 52, 80-87.
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 59
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: Linking Ca2+ signalling to membrane dynamics
    • Gerke, V.; Creutz, C.E.; Moss, S.E. Annexins: Linking Ca2+ signalling to membrane dynamics. Nat. Rev. Mol. Cell Biol. 2005, 6, 449-461.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 60
    • 84946607022 scopus 로고    scopus 로고
    • Annexin A2 binds to endosomes and negatively regulates TLR4-triggered inflammatory responses via the TRAM-TRIF pathway
    • Zhang, S.; Yu, M.; Guo, Q.; Li, R.; Li, G.; Tan, S.; Li, X.; Wei, Y.; Wu, M. Annexin A2 binds to endosomes and negatively regulates TLR4-triggered inflammatory responses via the TRAM-TRIF pathway. Sci. Rep. 2015, 5, 15859.
    • (2015) Sci. Rep. , vol.5 , pp. 15859
    • Zhang, S.1    Yu, M.2    Guo, Q.3    Li, R.4    Li, G.5    Tan, S.6    Li, X.7    Wei, Y.8    Wu, M.9
  • 62
    • 84925426076 scopus 로고    scopus 로고
    • Structure of a TLR4-interacting SPA4 peptide
    • Awasthi, S.; Anbanandam, A.; Rodgers, K.K. Structure of a TLR4-interacting SPA4 peptide. RSC Adv. 2015, 5, 27431-27438.
    • (2015) RSC Adv , vol.5 , pp. 27431-27438
    • Awasthi, S.1    Anbanandam, A.2    Rodgers, K.K.3
  • 63
    • 33747840389 scopus 로고    scopus 로고
    • GRAMM-X public web server for protein-protein docking
    • Tovchigrechko, A.; Vakser, I.A. GRAMM-X public web server for protein-protein docking. Nucleic Acids Res. 2006, 34, W310-W314.
    • (2006) Nucleic Acids Res , vol.34 , pp. W310-W314
    • Tovchigrechko, A.1    Vakser, I.A.2
  • 64
    • 84888873074 scopus 로고    scopus 로고
    • When carbon nanotubes encounter the immune system: Desirable and undesirable effects
    • Dumortier, H. When carbon nanotubes encounter the immune system: Desirable and undesirable effects. Adv. Drug Deliv. Rev. 2013, 65, 2120-2126.
    • (2013) Adv. Drug Deliv. Rev , vol.65 , pp. 2120-2126
    • Dumortier, H.1
  • 65
    • 84937864661 scopus 로고    scopus 로고
    • Advances in mechanisms and signaling pathways of carbon nanotube toxicity
    • Dong, J.; Ma, Q. Advances in mechanisms and signaling pathways of carbon nanotube toxicity. Nanotoxicology 2015, 9, 658-676.
    • (2015) Nanotoxicology , vol.9 , pp. 658-676
    • Dong, J.1    Ma, Q.2
  • 66
    • 84896348692 scopus 로고    scopus 로고
    • Immunotoxicity of nanoparticles: A computational study suggests that CNTs and C60 fullerenes might be recognized as pathogens by Toll-like receptors
    • Turabekova, M.; Rasulev, B.; Theodore, M.; Jackman, J.; Leszczynska, D.; Leszczynski, J. Immunotoxicity of nanoparticles: A computational study suggests that CNTs and C60 fullerenes might be recognized as pathogens by Toll-like receptors. Nanoscale 2014, 6, 3488-3495.
    • (2014) Nanoscale , vol.6 , pp. 3488-3495
    • Turabekova, M.1    Rasulev, B.2    Theodore, M.3    Jackman, J.4    Leszczynska, D.5    Leszczynski, J.6
  • 67
    • 80052967040 scopus 로고    scopus 로고
    • Computational design principles for bioactive dendrimer based constructs as antagonists of the TLR4-MD-2-LPS complex
    • Barata, T.; Teo, I.; Lalwani, S.; Simanek, E.; Zloh, M.; Shaunak, S. Computational design principles for bioactive dendrimer based constructs as antagonists of the TLR4-MD-2-LPS complex. Biomaterials 2011, 32, 8702-8711.
    • (2011) Biomaterials , vol.32 , pp. 8702-8711
    • Barata, T.1    Teo, I.2    Lalwani, S.3    Simanek, E.4    Zloh, M.5    Shaunak, S.6
  • 68
    • 77956174572 scopus 로고    scopus 로고
    • Application of a novel in silico high-throughput screen to identify selective inhibitors for protein-protein interactions
    • Joce, C.; Stahl, J.A.; Shridhar, M.; Hutchinson, M.R.; Watkins, L.R.; Fedichev, P.O.; Yin, H. Application of a novel in silico high-throughput screen to identify selective inhibitors for protein-protein interactions. Bioorg. Med. Chem. Lett. 2010, 20, 5411-5413.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 5411-5413
    • Joce, C.1    Stahl, J.A.2    Shridhar, M.3    Hutchinson, M.R.4    Watkins, L.R.5    Fedichev, P.O.6    Yin, H.7
  • 69
    • 84982691852 scopus 로고    scopus 로고
    • accessed on 26 July 2016
    • Enamine database. Available online: http://www.enamine.net (accessed on 26 July 2016).
    • Enamine database
  • 70
    • 84886549484 scopus 로고    scopus 로고
    • Novel Toll-like receptor 4 (TLR4) antagonists identified by structure- and ligand-based virtual screening. Eur
    • Svajger, U.; Brus, B.; Turk, S.; Sova, M.; Hodnik, V.; Anderluh, G.; Gobec, S. Novel Toll-like receptor 4 (TLR4) antagonists identified by structure- and ligand-based virtual screening. Eur. J. Med. Chem. 2013, 70, 393-399.
    • (2013) J. Med. Chem. , vol.70 , pp. 393-399
    • Svajger, U.1    Brus, B.2    Turk, S.3    Sova, M.4    Hodnik, V.5    Anderluh, G.6    Gobec, S.7
  • 72
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling
    • O'Neill, L.A.; Bowie, A.G. The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. Nat. Rev. Immunol. 2007, 7, 353-364.
    • (2007) Nat. Rev. Immunol , vol.7 , pp. 353-364
    • O'Neill, L.A.1    Bowie, A.G.2
  • 73
    • 84925486323 scopus 로고    scopus 로고
    • Toll/interleukin-1 receptor (TIR) domain-mediated cellular signaling pathways. Apoptosis Int
    • Narayanan, K.B.; Park, H.H. Toll/interleukin-1 receptor (TIR) domain-mediated cellular signaling pathways. Apoptosis Int. J. Program. Cell Death 2015, 20, 196-209.
    • (2015) J. Program. Cell Death , vol.20 , pp. 196-209
    • Narayanan, K.B.1    Park, H.H.2
  • 74
    • 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.; Tong, L. Structural basis for signal transduction by the Toll/interleukin-1 receptor domains. Nature 2000, 408, 111-115.
    • (2000) Nature , vol.408 , 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
  • 75
    • 20044368019 scopus 로고    scopus 로고
    • Human TLR10 is a functional receptor, expressed by B cells and plasmacytoid dendritic cells, which activates gene transcription through MyD88
    • Hasan, U.; Chaffois, C.; Gaillard, C.; Saulnier, V.; Merck, E.; Tancredi, S.; Guiet, C.; Brière, F.; Vlach, J.; Lebecque, S. Human TLR10 is a functional receptor, expressed by B cells and plasmacytoid dendritic cells, which activates gene transcription through MyD88. J. Immunol. 2005, 174, 2942-2950.
    • (2005) J. Immunol , vol.174 , pp. 2942-2950
    • Hasan, U.1    Chaffois, C.2    Gaillard, C.3    Saulnier, V.4    Merck, E.5    Tancredi, S.6    Guiet, C.7    Brière, F.8    Vlach, J.9    Lebecque, S.10
  • 77
    • 18144362027 scopus 로고    scopus 로고
    • Peptide-mediated interference of TIR domain dimerization in MyD88 inhibits interleukin-1-dependent activation of nf-κb
    • Loiarro, M.; Sette, C.; Gallo, G.; Ciacci, A.; Fantò, N.; Mastroianni, D.; Carminati, P.; Ruggiero, V. Peptide-mediated interference of TIR domain dimerization in MyD88 inhibits interleukin-1-dependent activation of nf-κb. J. Biol. Chem. 2005, 280, 15809-15814.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15809-15814
    • Loiarro, M.1    Sette, C.2    Gallo, G.3    Ciacci, A.4    Fantò, N.5    Mastroianni, D.6    Carminati, P.7    Ruggiero, V.8
  • 79
    • 84859227566 scopus 로고    scopus 로고
    • Structural insights into TIR domain specificity of the bridging adaptor mal in TLR4 signaling
    • Lin, Z.; Lu, J.; Zhou, W.; Shen, Y. Structural insights into TIR domain specificity of the bridging adaptor mal in TLR4 signaling. PLoS ONE 2012, 7, e34202.
    • (2012) PLoS ONE , vol.7 , pp. e34202
    • Lin, Z.1    Lu, J.2    Zhou, W.3    Shen, Y.4
  • 80
    • 16744364738 scopus 로고    scopus 로고
    • Structural complementarity of Toll/interleukin-1 receptor domains in toll-like receptors and the adaptors Mal and MyD88
    • Dunne, A.; Ejdebäck, M.; Ludidi, P.L.; O'Neill, L.A.; Gay, N.J. Structural complementarity of Toll/interleukin-1 receptor domains in toll-like receptors and the adaptors Mal and MyD88. J. Biol. Chem. 2003, 278, 41443-41451.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41443-41451
    • Dunne, A.1    Ejdebäck, M.2    Ludidi, P.L.3    O'Neill, L.A.4    Gay, N.J.5
  • 81
    • 37749004229 scopus 로고    scopus 로고
    • Structure-function relationships of Toll-like receptor domains through homology modelling and molecular dynamics
    • Kubarenko, A.; Frank, M.; Weber, A. Structure-function relationships of Toll-like receptor domains through homology modelling and molecular dynamics. Biochem. Soc. Trans. 2007, 35, 1515-1518.
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 1515-1518
    • Kubarenko, A.1    Frank, M.2    Weber, A.3
  • 83
    • 40749097627 scopus 로고    scopus 로고
    • A dimer of the Toll-like receptor 4 cytoplasmic domain provides a specific scaffold for the recruitment of signalling adaptor proteins
    • Miguel, R.N.; Wong, J.; Westoll, J.F.; Brooks, H.J.; O1 Neill, L.A.; Gay, N.J.; Bryant, C.E.; Monie, T.P. A dimer of the Toll-like receptor 4 cytoplasmic domain provides a specific scaffold for the recruitment of signalling adaptor proteins. PLoS ONE 2007, 2, e788.
    • (2007) PLoS ONE , vol.2 , pp. e788
    • Miguel, R.N.1    Wong, J.2    Westoll, J.F.3    Brooks, H.J.4    O'Neill, L.A.5    Gay, N.J.6    Bryant, C.E.7    Monie, T.P.8
  • 84
    • 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, R.G.; Choi, S. In silico approach to inhibition of signaling pathways of Toll-like receptors 2 and 4 by ST2L. PLoS ONE 2011, 6, e23989.
    • (2011) PLoS ONE , vol.6 , pp. e23989
    • Basith, S.1    Manavalan, B.2    Govindaraj, R.G.3    Choi, S.4
  • 85
    • 84939824619 scopus 로고    scopus 로고
    • The architecture of the TIR domain signalosome in the Toll-like receptor-4 signaling pathway
    • Guven-Maiorov, E.; Keskin, O.; Gursoy, A.; VanWaes, C.; Chen, Z.; Tsai, C.-J.; Nussinov, R. The architecture of the TIR domain signalosome in the Toll-like receptor-4 signaling pathway. Sci. Rep. 2015, 5, 13128.
    • (2015) Sci. Rep , vol.5 , pp. 13128
    • Guven-Maiorov, E.1    Keskin, O.2    Gursoy, A.3    VanWaes, C.4    Chen, Z.5    Tsai, C.J.6    Nussinov, R.7
  • 86
    • 84856710421 scopus 로고    scopus 로고
    • Identification of interaction sites for dimerization and adapter recruitment in Toll/interleukin-1 receptor (TIR) domain of Toll-like receptor 4
    • Bovijn, C.; Ulrichts, P.; de Smet, A.-S.; Catteeuw, D.; Beyaert, R.; Tavernier, J.; Peelman, F. Identification of interaction sites for dimerization and adapter recruitment in Toll/interleukin-1 receptor (TIR) domain of Toll-like receptor 4. J. Biol. Chem. 2012, 287, 4088-4098.
    • (2012) J. Biol. Chem , vol.287 , pp. 4088-4098
    • Bovijn, C.1    Ulrichts, P.2    De Smet, A.S.3    Catteeuw, D.4    Beyaert, R.5    Tavernier, J.6    Peelman, F.7
  • 87
    • 84896722900 scopus 로고    scopus 로고
    • Ashish. A communication network within the cytoplasmic domain of Toll-like receptors has remained conserved during evolution
    • Singh, S.; Pandey, K.; Rathore, Y.S.; Sagar, A.; Pattnaik, U.B.K.; Ashish. A communication network within the cytoplasmic domain of Toll-like receptors has remained conserved during evolution. J. Biomol. Struct. Dyn. 2014, 32, 694-700.
    • (2014) J. Biomol. Struct. Dyn. , vol.32 , pp. 694-700
    • Singh, S.1    Pandey, K.2    Rathore, Y.S.3    Sagar, A.4    Pattnaik, U.B.K.5


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