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Volumn 5, Issue , 2015, Pages

Energetics of Endotoxin Recognition in the Toll-Like Receptor 4 Innate Immune Response

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTOXIN; LIPOPOLYSACCHARIDE; PROTEIN BINDING; PROTEIN MD 2; TOLL LIKE RECEPTOR 4;

EID: 84949559950     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep17997     Document Type: Article
Times cited : (24)

References (71)
  • 1
    • 0016138375 scopus 로고
    • Structure and biogenesis of the cell envelope of gram-negative bacteria
    • Osborn, M. J., Rick, P. D., Lehmann, V., Rupprecht, E. & Singh, M. Structure and biogenesis of the cell envelope of gram-negative bacteria. Ann N Y Acad Sci 235, 52-65 (1974).
    • (1974) Ann N y Acad Sci , vol.235 , pp. 52-65
    • Osborn, M.J.1    Rick, P.D.2    Lehmann, V.3    Rupprecht, E.4    Singh, M.5
  • 2
    • 69249230732 scopus 로고    scopus 로고
    • Transport of lipopolysaccharide across the cell envelope: The long road of discovery
    • Ruiz, N., Kahne, D. & Silhavy, T. J. Transport of lipopolysaccharide across the cell envelope: the long road of discovery. Nat Rev Microbiol 7, 677-683 (2009).
    • (2009) Nat Rev Microbiol , vol.7 , pp. 677-683
    • Ruiz, N.1    Kahne, D.2    Silhavy, T.J.3
  • 4
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67, 593-656 (2003).
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 5
    • 64649088018 scopus 로고    scopus 로고
    • Outer membrane permeability and antibiotic resistance
    • Delcour, A. H. Outer membrane permeability and antibiotic resistance. Biochim Biophys Acta 1794, 808-816 (2009).
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 808-816
    • Delcour, A.H.1
  • 6
    • 73949133993 scopus 로고    scopus 로고
    • The molecular basis of the host response to lipopolysaccharide
    • Bryant, C. E., Spring, D. R., Gangloff, M. & Gay, N. J. The molecular basis of the host response to lipopolysaccharide. Nat Rev Microbiol 8, 8-14 (2010).
    • (2010) Nat Rev Microbiol , vol.8 , pp. 8-14
    • Bryant, C.E.1    Spring, D.R.2    Gangloff, M.3    Gay, N.J.4
  • 7
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira, S., Uematsu, S. & Takeuchi, O. Pathogen recognition and innate immunity. Cell 124, 783-801 (2006).
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 8
    • 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
    • Nunez Miguel, R. et al. A dimer of the Toll-like receptor 4 cytoplasmic domain provides a specific scaffold for the recruitment of signalling adaptor proteins. PLoS One 2, e788 (2007).
    • (2007) PLoS One , vol.2 , pp. e788
    • Nunez Miguel, R.1
  • 9
    • 33748090945 scopus 로고    scopus 로고
    • Toll-like receptors as molecular switches
    • Gay, N. J., Gangloff, M. & Weber, A. N. Toll-like receptors as molecular switches. Nat Rev Immunol 6, 693-698 (2006).
    • (2006) Nat Rev Immunol , vol.6 , pp. 693-698
    • Gay, N.J.1    Gangloff, M.2    Weber, A.N.3
  • 10
    • 67649422321 scopus 로고    scopus 로고
    • Therapeutic targeting of Toll-like receptors for infectious and inflammatory diseases and cancer
    • O'Neill, L. A., Bryant, C. E. & Doyle, S. L. Therapeutic targeting of Toll-like receptors for infectious and inflammatory diseases and cancer. Pharmacol Rev 61, 177-197 (2009).
    • (2009) Pharmacol Rev , vol.61 , pp. 177-197
    • O'Neill, L.A.1    Bryant, C.E.2    Doyle, S.L.3
  • 11
    • 84879418353 scopus 로고    scopus 로고
    • Fortifying the barrier: The impact of lipid A remodelling on bacterial pathogenesis
    • Needham, B. D. & Trent, M. S. Fortifying the barrier: the impact of lipid A remodelling on bacterial pathogenesis. Nat Rev Microbiol 11, 467-481 (2013).
    • (2013) Nat Rev Microbiol , vol.11 , pp. 467-481
    • Needham, B.D.1    Trent, M.S.2
  • 12
    • 0037372661 scopus 로고    scopus 로고
    • Inhibition of endotoxin response by e5564, a novel Toll-like receptor 4-directed endotoxin antagonist
    • Mullarkey, M. et al. Inhibition of endotoxin response by e5564, a novel Toll-like receptor 4-directed endotoxin antagonist. J Pharmacol Exp Ther 304, 1093-1102 (2003).
    • (2003) J Pharmacol Exp Ther , vol.304 , pp. 1093-1102
    • Mullarkey, M.1
  • 13
    • 45949103247 scopus 로고    scopus 로고
    • Effects of the second-generation synthetic lipid A analogue E5564 on responses to endotoxin in [corrected] equine whole blood and monocytes
    • Figueiredo, M. D., Moore, J. N., Vandenplas, M. L., Sun, W. C. & Murray, T. F. Effects of the second-generation synthetic lipid A analogue E5564 on responses to endotoxin in [corrected] equine whole blood and monocytes. Am J Vet Res 69, 796-803 (2008).
    • (2008) Am J Vet Res , vol.69 , pp. 796-803
    • Figueiredo, M.D.1    Moore, J.N.2    Vandenplas, M.L.3    Sun, W.C.4    Murray, T.F.5
  • 15
    • 34548222514 scopus 로고    scopus 로고
    • Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran
    • Kim, H. M. et al. Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Cell 130, 906-917 (2007).
    • (2007) Cell , vol.130 , pp. 906-917
    • Kim, H.M.1
  • 16
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • Park, B. S. et al. The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 458, 1191-1195 (2009).
    • (2009) Nature , vol.458 , pp. 1191-1195
    • Park, B.S.1
  • 17
    • 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 316, 1632-1634 (2007).
    • (2007) Science , vol.316 , pp. 1632-1634
    • Ohto, U.1    Fukase, K.2    Miyake, K.3    Satow, Y.4
  • 18
    • 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 288, 36215-36225 (2013).
    • (2013) J Biol Chem , vol.288 , pp. 36215-36225
    • Paramo, T.1    Piggot, T.J.2    Bryant, C.E.3    Bond, P.J.4
  • 19
    • 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 27, 219-221 (2002).
    • (2002) Trends Biochem Sci , vol.27 , pp. 219-221
    • Inohara, N.1    Nunez, G.2
  • 20
    • 18244371923 scopus 로고    scopus 로고
    • NMR study on the major mite allergen der f 2: Its refined tertiary structure, epitopes for monoclonal antibodies and characteristics shared by ML protein group members
    • Ichikawa, S. et al. NMR study on the major mite allergen Der f 2: its refined tertiary structure, epitopes for monoclonal antibodies and characteristics shared by ML protein group members. J Biochem 137, 255-263 (2005).
    • (2005) J Biochem , vol.137 , pp. 255-263
    • Ichikawa, S.1
  • 21
    • 0032531058 scopus 로고    scopus 로고
    • Tertiary structure of the major house dust mite allergen der p 2: Sequential and structural homologies
    • Mueller, G. A., Benjamin, D. C. & Rule, G. S. Tertiary structure of the major house dust mite allergen Der p 2: sequential and structural homologies. Biochemistry 37, 12707-12714 (1998).
    • (1998) Biochemistry , vol.37 , pp. 12707-12714
    • Mueller, G.A.1    Benjamin, D.C.2    Rule, G.S.3
  • 22
    • 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. et al. NMR studies of hexaacylated endotoxin bound to wild-type and F126A mutant MD-2 and MD-2.TLR4 ectodomain complexes. J Biol Chem 287, 16346-16355 (2012).
    • (2012) J Biol Chem , vol.287 , pp. 16346-16355
    • Yu, L.1
  • 23
    • 33646494167 scopus 로고    scopus 로고
    • Regulatory roles for MD-2 and TLR4 in ligand-induced receptor clustering
    • Kobayashi, M. et al. Regulatory roles for MD-2 and TLR4 in ligand-induced receptor clustering. J Immunol 176, 6211-6218 (2006).
    • (2006) J Immunol , vol.176 , pp. 6211-6218
    • Kobayashi, M.1
  • 24
    • 38349186906 scopus 로고    scopus 로고
    • Novel roles in human MD-2 of phenylalanines 121 and 126 and tyrosine 131 in activation of Toll-like receptor 4 by endotoxin
    • Teghanemt, A. et al. Novel roles in human MD-2 of phenylalanines 121 and 126 and tyrosine 131 in activation of Toll-like receptor 4 by endotoxin. J Biol Chem 283, 1257-1266 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 1257-1266
    • Teghanemt, A.1
  • 25
    • 34547553097 scopus 로고    scopus 로고
    • The physicochemistry of endotoxins in relation to bioactivity
    • Gutsmann, T., Schromm, A. B. & Brandenburg, K. The physicochemistry of endotoxins in relation to bioactivity. Int J Med Microbiol 297, 341-352 (2007).
    • (2007) Int J Med Microbiol , vol.297 , pp. 341-352
    • Gutsmann, T.1    Schromm, A.B.2    Brandenburg, K.3
  • 26
    • 0025220127 scopus 로고
    • A mutant of Escherichia coli defective in the first step of endotoxin biosynthesis
    • Galloway, S. M. & Raetz, C. R. A mutant of Escherichia coli defective in the first step of endotoxin biosynthesis. J Biol Chem 265, 6394-6402 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 6394-6402
    • Galloway, S.M.1    Raetz, C.R.2
  • 27
    • 29944441136 scopus 로고    scopus 로고
    • Determination of critical micelle concentrations and aggregation numbers by fluorescence correlation spectroscopy: Aggregation of a lipopolysaccharide
    • Yu, L., Tan, M., Ho, B., Ding, J. L. & Wohland, T. Determination of critical micelle concentrations and aggregation numbers by fluorescence correlation spectroscopy: aggregation of a lipopolysaccharide. Anal Chim Acta 556, 216-225 (2006).
    • (2006) Anal Chim Acta , vol.556 , pp. 216-225
    • Yu, L.1    Tan, M.2    Ho, B.3    Ding, J.L.4    Wohland, T.5
  • 28
    • 0037415015 scopus 로고    scopus 로고
    • Evaluation of lipopolysaccharide aggregation by light scattering spectroscopy
    • Santos, N. C., Silva, A. C., Castanho, M. A., Martins-Silva, J. & Saldanha, C. Evaluation of lipopolysaccharide aggregation by light scattering spectroscopy. ChemBioChem 4, 96-100 (2003).
    • (2003) ChemBioChem , vol.4 , pp. 96-100
    • Santos, N.C.1    Silva, A.C.2    Castanho, M.A.3    Martins-Silva, J.4    Saldanha, C.5
  • 29
    • 37549001771 scopus 로고    scopus 로고
    • Transfer of monomeric endotoxin from MD-2 to CD14: Characterization and functional consequences
    • Teghanemt, A., Prohinar, P., Gioannini, T. L. & Weiss, J. P. Transfer of monomeric endotoxin from MD-2 to CD14: characterization and functional consequences. J Biol Chem 282, 36250-36256 (2007).
    • (2007) J Biol Chem , vol.282 , pp. 36250-36256
    • Teghanemt, A.1    Prohinar, P.2    Gioannini, T.L.3    Weiss, J.P.4
  • 30
    • 48749127416 scopus 로고    scopus 로고
    • Elucidation of the MD-2/TLR4 interface required for signaling by lipid IVa
    • Walsh, C. et al. Elucidation of the MD-2/TLR4 interface required for signaling by lipid IVa. J Immunol 181, 1245-1254 (2008).
    • (2008) J Immunol , vol.181 , pp. 1245-1254
    • Walsh, C.1
  • 32
    • 77954100856 scopus 로고    scopus 로고
    • Novel roles of lysines 122, 125, and 58 in functional differences between human and murine MD-2
    • Vasl, J., Oblak, A., Gioannini, T. L., Weiss, J. P. & Jerala, R. Novel roles of lysines 122, 125, and 58 in functional differences between human and murine MD-2. J Immunol 183, 5138-5145 (2009).
    • (2009) J Immunol , vol.183 , pp. 5138-5145
    • Vasl, J.1    Oblak, A.2    Gioannini, T.L.3    Weiss, J.P.4    Jerala, R.5
  • 33
    • 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. et al. Essential roles of hydrophobic residues in both MD-2 and toll-like receptor 4 in activation by endotoxin. J Biol Chem 284, 15052-15060 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 15052-15060
    • Resman, N.1
  • 34
    • 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. L. 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 101, 4186-4191 (2004).
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4186-4191
    • Gioannini, T.L.1
  • 35
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu, R. et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J Exp Med 189, 1777-1782 (1999).
    • (1999) J Exp Med , vol.189 , pp. 1777-1782
    • Shimazu, R.1
  • 36
    • 48549109541 scopus 로고
    • Physical aspects of structure and function of membranes made from lipopolysaccharides and free lipid A
    • Brandenburg, K. & Seydel, U. Physical aspects of structure and function of membranes made from lipopolysaccharides and free lipid A. Biochim Biophys Acta 775, 225-238 (1984).
    • (1984) Biochim Biophys Acta , vol.775 , pp. 225-238
    • Brandenburg, K.1    Seydel, U.2
  • 37
    • 0033578344 scopus 로고    scopus 로고
    • Lipopolysaccharide bilayer structure: Effect of chemotype, core mutations, divalent cations, and temperature
    • Snyder, S., Kim, D. & McIntosh, T. J. Lipopolysaccharide bilayer structure: effect of chemotype, core mutations, divalent cations, and temperature. Biochemistry 38, 10758-10767 (1999).
    • (1999) Biochemistry , vol.38 , pp. 10758-10767
    • Snyder, S.1    Kim, D.2    McIntosh, T.J.3
  • 39
    • 0025543112 scopus 로고
    • Phase diagram of lipid A from Salmonella Minnesota and Escherichia coli rough mutant lipopolysaccharide
    • Brandenburg, K., Koch, M. H. & Seydel, U. Phase diagram of lipid A from Salmonella minnesota and Escherichia coli rough mutant lipopolysaccharide. J Struct Biol 105, 11-21 (1990).
    • (1990) J Struct Biol , vol.105 , pp. 11-21
    • Brandenburg, K.1    Koch, M.H.2    Seydel, U.3
  • 40
    • 0030061787 scopus 로고    scopus 로고
    • Crystallization of synthetic Escherichia coli-type lipid A
    • Kato, N. et al. Crystallization of synthetic Escherichia coli-type lipid A. Microbiol Immunol 40, 33-38 (1996).
    • (1996) Microbiol Immunol , vol.40 , pp. 33-38
    • Kato, N.1
  • 41
    • 0034907678 scopus 로고    scopus 로고
    • Computer simulation of the rough lipopolysaccharide membrane of Pseudomonas aeruginosa
    • Lins, R. D. & Straatsma, T. P. Computer simulation of the rough lipopolysaccharide membrane of Pseudomonas aeruginosa. Biophys J 81, 1037-1046 (2001).
    • (2001) Biophys J , vol.81 , pp. 1037-1046
    • Lins, R.D.1    Straatsma, T.P.2
  • 42
    • 84889070118 scopus 로고    scopus 로고
    • Hydration, ionic valence and cross-linking propensities of cations determine the stability of lipopolysaccharide (LPS) membranes
    • Nascimento, A., Jr., Pontes, F. J., Lins, R. D. & Soares, T. A. Hydration, ionic valence and cross-linking propensities of cations determine the stability of lipopolysaccharide (LPS) membranes. Chem Commun (Camb) 50, 231-233 (2014).
    • (2014) Chem Commun (Camb) , vol.50 , pp. 231-233
    • Nascimento, A.1    Pontes, F.J.2    Lins, R.D.3    Soares, T.A.4
  • 43
    • 84884303247 scopus 로고    scopus 로고
    • Molecular dynamics and NMR spectroscopy studies of e coli lipopolysaccharide structure and dynamics
    • Wu, E. L. et al. Molecular dynamics and NMR spectroscopy studies of E. coli lipopolysaccharide structure and dynamics. Biophys J 105, 1444-1455 (2013).
    • (2013) Biophys J , vol.105 , pp. 1444-1455
    • Wu, E.L.1
  • 44
    • 0018888056 scopus 로고
    • Lateral mobility in reconstituted membranes-comparisons with diffusion in polymers
    • Schindler, M., Osborn, M. J. & Koppel, D. E. Lateral mobility in reconstituted membranes-comparisons with diffusion in polymers. Nature 283, 346-350 (1980).
    • (1980) Nature , vol.283 , pp. 346-350
    • Schindler, M.1    Osborn, M.J.2    Koppel, D.E.3
  • 45
    • 84927522993 scopus 로고    scopus 로고
    • Exploring the local elastic properties of bilayer membranes using molecular dynamics simulations
    • Pieffet, G., Botero, A., Peters, G. H., Forero-Shelton, M. & Leidy, C. Exploring the local elastic properties of bilayer membranes using molecular dynamics simulations. J Phys Chem B 118, 12883-12891 (2014).
    • (2014) J Phys Chem B , vol.118 , pp. 12883-12891
    • Pieffet, G.1    Botero, A.2    Peters, G.H.3    Forero-Shelton, M.4    Leidy, C.5
  • 46
    • 84876826729 scopus 로고    scopus 로고
    • Inefficient TLR4/MD-2 heterotetramerization by monophosphoryl lipid A
    • Casella, C. R. & Mitchell, T. C. Inefficient TLR4/MD-2 heterotetramerization by monophosphoryl lipid A. PLoS One 8, e62622 (2013).
    • (2013) PLoS One , vol.8 , pp. e62622
    • Casella, C.R.1    Mitchell, T.C.2
  • 47
    • 34250854079 scopus 로고    scopus 로고
    • The vaccine adjuvant monophosphoryl lipid A as a TRIF-biased agonist of TLR4
    • Mata-Haro, V. et al. The vaccine adjuvant monophosphoryl lipid A as a TRIF-biased agonist of TLR4. Science 316, 1628-1632 (2007).
    • (2007) Science , vol.316 , pp. 1628-1632
    • Mata-Haro, V.1
  • 48
    • 77952540747 scopus 로고    scopus 로고
    • Conformation and supramolecular structure of lipid A
    • Brandenburg, K. & Seydel, U. Conformation and supramolecular structure of lipid A. Adv Exp Med Biol 667, 25-38 (2009).
    • (2009) Adv Exp Med Biol , vol.667 , pp. 25-38
    • Brandenburg, K.1    Seydel, U.2
  • 49
    • 84903716794 scopus 로고    scopus 로고
    • Structural biology: Lipopolysaccharide rolls out the barrel
    • in press
    • Bishop, R. E. Structural biology: Lipopolysaccharide rolls out the barrel. Nature in press (2014).
    • (2014) Nature
    • Bishop, R.E.1
  • 50
    • 84903728454 scopus 로고    scopus 로고
    • Structural basis for outer membrane lipopolysaccharide insertion
    • in press
    • Dong, J. et al. Structural basis for outer membrane lipopolysaccharide insertion. Nature in press (2014).
    • (2014) Nature
    • Dong, J.1
  • 51
    • 84903716134 scopus 로고    scopus 로고
    • Structural basis for lipopolysaccharide insertion in the bacterial outer membrane
    • in press
    • Quai, S., Luo, Q., Zhao, Y., C., Z. X. & Huang, Y. Structural basis for lipopolysaccharide insertion in the bacterial outer membrane. Nature in press (2014).
    • (2014) Nature
    • Quai, S.1    Luo, Q.2    Zhao, Y.C.Z.X.3    Huang, Y.4
  • 52
    • 33847708375 scopus 로고    scopus 로고
    • Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain
    • Prohinar, P. et al. Specific high affinity interactions of monomeric endotoxin.protein complexes with Toll-like receptor 4 ectodomain. J Biol Chem 282, 1010-1017 (2007).
    • (2007) J Biol Chem , vol.282 , pp. 1010-1017
    • Prohinar, P.1
  • 53
    • 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. 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 198, 1035-1042 (2003).
    • (2003) J Exp Med , vol.198 , pp. 1035-1042
    • Akashi, S.1
  • 54
    • 0027301026 scopus 로고
    • Effect of pH on solubility and ionic state of lipopolysaccharide obtained from the deep rough mutant of Escherichia coli
    • Din, Z. Z., Mukerjee, P., Kastowsky, M. & Takayama, K. Effect of pH on solubility and ionic state of lipopolysaccharide obtained from the deep rough mutant of Escherichia coli. Biochemistry 32, 4579-4586 (1993).
    • (1993) Biochemistry , vol.32 , pp. 4579-4586
    • Din, Z.Z.1    Mukerjee, P.2    Kastowsky, M.3    Takayama, K.4
  • 55
    • 47749153335 scopus 로고    scopus 로고
    • Aggregation behavior of an ultra-pure lipopolysaccharide that stimulates TLR-4 receptors
    • Sasaki, H. & White, S. H. Aggregation behavior of an ultra-pure lipopolysaccharide that stimulates TLR-4 receptors. Biophys J 95, 986-993 (2008).
    • (2008) Biophys J , vol.95 , pp. 986-993
    • Sasaki, H.1    White, S.H.2
  • 56
    • 0032754292 scopus 로고    scopus 로고
    • Chemical structure, molecular conformation, and bioactivity of endotoxins
    • Seydel, U., Schromm, A. B., Blunck, R. & Brandenburg, K. Chemical structure, molecular conformation, and bioactivity of endotoxins. Chem Immunol 74, 5-24 (2000).
    • (2000) Chem Immunol , vol.74 , pp. 5-24
    • Seydel, U.1    Schromm, A.B.2    Blunck, R.3    Brandenburg, K.4
  • 57
    • 33749182054 scopus 로고    scopus 로고
    • Lipids out of equilibrium: Energetics of desorption and pore mediated flip-flop
    • Tieleman, D. P. & Marrink, S. J. Lipids out of equilibrium: energetics of desorption and pore mediated flip-flop. J Am Chem Soc 128, 12462-12467 (2006).
    • (2006) J Am Chem Soc , vol.128 , pp. 12462-12467
    • Tieleman, D.P.1    Marrink, S.J.2
  • 60
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., Van der Spoel, D. & Lindahl, E. GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4, 435-447 (2008).
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 61
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, A. D. et al. All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins. J Phys Chem B 102, 3586-3616 (1998).
    • (1998) J Phys Chem B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1
  • 62
    • 77950106854 scopus 로고    scopus 로고
    • Implementation of the charmm force field in gromacs: Analysis of protein stability effects from correction maps, virtual interaction sites, and water models
    • Bjelkmar, P., Larsson, P., Cuendet, M. A., Hess, B. & Lindahl, E. Implementation of the CHARMM Force Field in GROMACS: Analysis of Protein Stability Effects from Correction Maps, Virtual Interaction Sites, and Water Models. J Chem Theory Comput 6, 459-466 (2010).
    • (2010) J Chem Theory Comput , vol.6 , pp. 459-466
    • Bjelkmar, P.1    Larsson, P.2    Cuendet, M.A.3    Hess, B.4    Lindahl, E.5
  • 63
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi, G., Donadio, D. & Parrinello, M. Canonical sampling through velocity rescaling. J Chem Phys 126, 014101 (2007).
    • (2007) J Chem Phys , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 64
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • Parrinello, M. & Rahman, A. Polymorphic transitions in single crystals: A new molecular dynamics method. J Appl Phys 52, 7182-7190 (1981).
    • (1981) J Appl Phys , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 65
    • 84926811618 scopus 로고
    • Constant pressure molecular-dynamics for molecular-systems
    • Nose, S. & Klein, M. L. Constant Pressure Molecular-Dynamics for Molecular-Systems. Mol Phys 50, 1055-1076 (1983).
    • (1983) Mol Phys , vol.50 , pp. 1055-1076
    • Nose, S.1    Klein, M.L.2
  • 66
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess, B., Bekker, H., Berendsen, H. J. C. & Fraaije, J. G. E. M. LINCS: A linear constraint solver for molecular simulations. J Comput Chem 18, 1463-1472 (1997).
    • (1997) J Comput Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.G.E.M.4
  • 67
    • 33645961739 scopus 로고
    • A smooth particle mesh ewald method
    • Essmann, U. et al. A Smooth Particle Mesh Ewald Method. J Chem Phys 103, 8577-8593 (1995).
    • (1995) J Chem Phys , vol.103 , pp. 8577-8593
    • Essmann, U.1
  • 68
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • 27-38
    • Humphrey, W., Dalke, A. & Schulten, K. VMD: visual molecular dynamics. J Mol Graph 14, 33-38, 27-38 (1996).
    • (1996) J Mol Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 69
    • 84900549764 scopus 로고    scopus 로고
    • Efficient characterization of protein cavities within molecular simulation trajectories: Trjcavity
    • Paramo, T., East, A., Garzon, D., Ulmschneider, M. B. & Bond, P. J. Efficient characterization of protein cavities within molecular simulation trajectories: trjcavity. J Chem Theory Comput 10, 2151-2164 (2014).
    • (2014) J Chem Theory Comput , vol.10 , pp. 2151-2164
    • Paramo, T.1    East, A.2    Garzon, D.3    Ulmschneider, M.B.4    Bond, P.J.5
  • 70
    • 78651282170 scopus 로고    scopus 로고
    • Gwham-A free weighted histogram analysis implementation including robust error and autocorrelation estimates
    • Hub, J. S., De Groot, B. L. & van der Spoel, D. gwham-A Free Weighted Histogram Analysis Implementation Including Robust Error and Autocorrelation Estimates. J Chem Theory Comput 6, 3713-3720 (2010).
    • (2010) J Chem Theory Comput , vol.6 , pp. 3713-3720
    • Hub, J.S.1    De Groot, B.L.2    Van Der Spoel, D.3
  • 71
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels
    • Russell, R. B. & Barton, G. J. Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels. Proteins 14, 309-323 (1992).
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2


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