메뉴 건너뛰기




Volumn 19, Issue 3, 2013, Pages 127-140

Max Bergmann lecture Protein epitope mimetics in the age of structural vaccinology

Author keywords

Antibiotic; Hairpin conformation; HIV 1; LptD; Outer membrane; Peptide; Vaccine; Virus like particle

Indexed keywords

ANTIBIOTIC AGENT; ARENICIN; CATIONIC ANTIMICROBIAL PEPTIDE; CHEMOKINE RECEPTOR; CYCLIC PEPTIDE L27 11; EPITOPE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 10E8; MONOCLONAL ANTIBODY 2557; MONOCLONAL ANTIBODY 2F5; MONOCLONAL ANTIBODY 447 52D; MONOCLONAL ANTIBODY 4E10; MONOCLONAL ANTIBODY 537 10D; MONOCLONAL ANTIBODY 8066; MONOCLONAL ANTIBODY D5; MONOCLONAL ANTIBODY F425 B4E8; MONOCLONAL ANTIBODY HK20; MONOCLONAL ANTIBODY PG9; MONOCLONAL ANTIBODY Z13E1; OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN LPTD; POL 7001; POL 7080; POLYPEPTIDE ANTIBIOTIC AGENT; POLYPHEMUSIN; PROTEGRIN; PROTEINASE INHIBITOR; TACHYPLESIN; THETA DEFENSIN; UNCLASSIFIED DRUG;

EID: 84874022594     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.2482     Document Type: Review
Times cited : (36)

References (163)
  • 1
    • 22144454687 scopus 로고    scopus 로고
    • Strategies for targeting protein-protein interactions with synthetic agents
    • Yin H, Hamilton AD. Strategies for targeting protein-protein interactions with synthetic agents. Angew. Chem. Int. Ed. 2005; 44: 4130-4163.
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 4130-4163
    • Yin, H.1    Hamilton, A.D.2
  • 3
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T, Wells JA. A hot spot of binding energy in a hormone-receptor interface. Science 1995; 267: 383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 4
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: progress and challenges
    • DeLano WL. Unraveling hot spots in binding interfaces: progress and challenges. Curr. Opin. Struct. Biol. 2002; 12: 14-20.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 14-20
    • DeLano, W.L.1
  • 5
    • 11844249426 scopus 로고    scopus 로고
    • Hot regions in protein-protein interactions: the organization and contribution of structurally conserved hot spot residues
    • Keskin O, Ma B, Nussinov R. Hot regions in protein-protein interactions: the organization and contribution of structurally conserved hot spot residues. J. Mol. Biol. 2005; 345: 1281-1294.
    • (2005) J. Mol. Biol. , vol.345 , pp. 1281-1294
    • Keskin, O.1    Ma, B.2    Nussinov, R.3
  • 7
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells JA, McClendon CL. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 2007; 450: 1001-1009.
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 8
    • 2942553723 scopus 로고    scopus 로고
    • Protein-protein interactions: coupling of structurally conserved residues and of hot spots across interfaces. Implications for docking
    • Halperin I, Wolfson H, Nussinov R. Protein-protein interactions: coupling of structurally conserved residues and of hot spots across interfaces. Implications for docking. Structure 2004; 12: 1027-1038.
    • (2004) Structure , vol.12 , pp. 1027-1038
    • Halperin, I.1    Wolfson, H.2    Nussinov, R.3
  • 9
    • 54249137135 scopus 로고    scopus 로고
    • Computational redesign of a protein-protein interface for high affinity and binding specificity using modular architecture and naturally occurring template fragments
    • Potapov V, Reichmann D, Abramovich R, Filchtinski D, Zohar N, Ben Halevy D, Edelman M, Sobolev V, Schreiber G. Computational redesign of a protein-protein interface for high affinity and binding specificity using modular architecture and naturally occurring template fragments. J. Mol. Biol. 2008; 384: 109-119.
    • (2008) J. Mol. Biol. , vol.384 , pp. 109-119
    • Potapov, V.1    Reichmann, D.2    Abramovich, R.3    Filchtinski, D.4    Zohar, N.5    Ben Halevy, D.6    Edelman, M.7    Sobolev, V.8    Schreiber, G.9
  • 12
    • 77957753971 scopus 로고    scopus 로고
    • Enzyme catalysis from improved packing in their transition-state structures
    • Williams DH. Enzyme catalysis from improved packing in their transition-state structures. Curr. Opin. Chem. Biol. 2010; 14: 666-670.
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 666-670
    • Williams, D.H.1
  • 13
    • 84864651001 scopus 로고    scopus 로고
    • Protein activity regulation by conformational entropy
    • Tzeng S-R, Kalodimos CG. Protein activity regulation by conformational entropy. Nature 2012; 488: 236-240.
    • (2012) Nature , vol.488 , pp. 236-240
    • Tzeng, S.-R.1    Kalodimos, C.G.2
  • 14
    • 0031455857 scopus 로고    scopus 로고
    • β-Hairpins in proteins revisited: lessons for de novo design
    • Gunasekaran K, Ramakrishnan C, Balaram P. β-Hairpins in proteins revisited: lessons for de novo design. Prot. Engineer. 1997; 10: 1131-1141.
    • (1997) Prot. Engineer. , vol.10 , pp. 1131-1141
    • Gunasekaran, K.1    Ramakrishnan, C.2    Balaram, P.3
  • 15
    • 0024391832 scopus 로고
    • Conformation of β-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering
    • Sibanda BL, Blundell TL, Thornton JM. Conformation of β-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering. J. Mol. Biol. 1989; 206: 759-777.
    • (1989) J. Mol. Biol. , vol.206 , pp. 759-777
    • Sibanda, B.L.1    Blundell, T.L.2    Thornton, J.M.3
  • 16
    • 57349151828 scopus 로고    scopus 로고
    • β-Hairpin peptidomimetics: design, structures and biological activities
    • Robinson JA. β-Hairpin peptidomimetics: design, structures and biological activities. Accts. Chem. Res. 2008; 41: 1278-1288.
    • (2008) Accts. Chem. Res. , vol.41 , pp. 1278-1288
    • Robinson, J.A.1
  • 17
    • 0007912674 scopus 로고
    • X-ray crystal structure of pivaloyl- d-Pro- l-Pro- l-Ala-N-methylamide: observation of a consecutive β-turn conformation
    • Nair CM, Vijayan M, Venkatachalapathi YV, Balaram P. X-ray crystal structure of pivaloyl- d-Pro- l-Pro- l-Ala-N-methylamide: observation of a consecutive β-turn conformation. J. Chem. Soc., Chem. Comm 1979: 1183-1184.
    • (1979) J. Chem. Soc., Chem. Comm , pp. 1183-1184
    • Nair, C.M.1    Vijayan, M.2    Venkatachalapathi, Y.V.3    Balaram, P.4
  • 18
    • 0000032313 scopus 로고
    • Conformational analysis of cyclic hexapeptides containing the d-Pro- l-Pro sequence to fix β-turn positions
    • Bean JW, Kopple KD, Peishoff CE. Conformational analysis of cyclic hexapeptides containing the d-Pro- l-Pro sequence to fix β-turn positions. J. Am. Chem. Soc. 1992; 114: 5328-5334.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 5328-5334
    • Bean, J.W.1    Kopple, K.D.2    Peishoff, C.E.3
  • 19
    • 0000325130 scopus 로고
    • Pro- d-NMe-amino acid and d-Pro-NMe-amino acid: simple, efficient reverse turn constraints
    • Chalmers DK, Marshall GR. Pro- d-NMe-amino acid and d-Pro-NMe-amino acid: simple, efficient reverse turn constraints. J. Am. Chem. Soc. 1995; 117: 5927-5937.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5927-5937
    • Chalmers, D.K.1    Marshall, G.R.2
  • 20
    • 0033620414 scopus 로고    scopus 로고
    • Structural mimicry of canonical conformations in antibody hypervariable loops using cyclic peptides containing a heterochiral diproline template
    • Favre M, Moehle K, Jiang L, Bfeiffer B, Robinson JA. Structural mimicry of canonical conformations in antibody hypervariable loops using cyclic peptides containing a heterochiral diproline template. J. Am. Chem. Soc. 1999; 121: 2679-2685.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2679-2685
    • Favre, M.1    Moehle, K.2    Jiang, L.3    Bfeiffer, B.4    Robinson, J.A.5
  • 21
    • 0021844602 scopus 로고
    • β-Hairpin families in globular proteins
    • Sibanda BL, Thornton JM. β-Hairpin families in globular proteins. Nature 1985; 316: 170-174.
    • (1985) Nature , vol.316 , pp. 170-174
    • Sibanda, B.L.1    Thornton, J.M.2
  • 22
    • 83355160728 scopus 로고    scopus 로고
    • Synthetic virus-like particles and conformationally constrained peptidomimetics in vaccine design
    • Riedel T, Ghasparian A, Moehle K, Rusert P, Trkola A, Robinson JA. Synthetic virus-like particles and conformationally constrained peptidomimetics in vaccine design. ChemBioChem 2011; 12: 2829-2836.
    • (2011) ChemBioChem , vol.12 , pp. 2829-2836
    • Riedel, T.1    Ghasparian, A.2    Moehle, K.3    Rusert, P.4    Trkola, A.5    Robinson, J.A.6
  • 23
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano WL, Ultsch MH, de Vos AM, Wells JA. Convergent solutions to binding at a protein-protein interface. Science 2000; 287: 1279-1283.
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    de Vos, A.M.3    Wells, J.A.4
  • 24
    • 33644647749 scopus 로고    scopus 로고
    • Protein ligand design: from phage display to synthetic protein epitope mimetics in human antibody Fc-binding peptidomimetics
    • Dias RLA, Fasan R, Moehle K, Renard A, Obrecht D, Robinson JA. Protein ligand design: from phage display to synthetic protein epitope mimetics in human antibody Fc-binding peptidomimetics. J. Am. Chem. Soc. 2006; 128: 2726-2732.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2726-2732
    • Dias, R.L.A.1    Fasan, R.2    Moehle, K.3    Renard, A.4    Obrecht, D.5    Robinson, J.A.6
  • 25
    • 33846391016 scopus 로고    scopus 로고
    • Structure-guided peptidomimetic design leads to nanomolar β-hairpin inhibitors of the tat-tar interaction of bovine immunodeficiency virus
    • Athanassiou Z, Patora K, Dias RLA, Moehle K, Robinson JA, Varani G. Structure-guided peptidomimetic design leads to nanomolar β-hairpin inhibitors of the tat-tar interaction of bovine immunodeficiency virus. Biochemistry 2007; 46: 741-751.
    • (2007) Biochemistry , vol.46 , pp. 741-751
    • Athanassiou, Z.1    Patora, K.2    Dias, R.L.A.3    Moehle, K.4    Robinson, J.A.5    Varani, G.6
  • 27
    • 85047698934 scopus 로고    scopus 로고
    • A new family of β-hairpin mimetics based on a trypsin inhibitor form sunflower seeds
    • Descours A, Moehle K, Renard A, Robinson JA. A new family of β-hairpin mimetics based on a trypsin inhibitor form sunflower seeds. ChemBioChem 2002; 3: 318-323.
    • (2002) ChemBioChem , vol.3 , pp. 318-323
    • Descours, A.1    Moehle, K.2    Renard, A.3    Robinson, J.A.4
  • 28
    • 0034470558 scopus 로고    scopus 로고
    • Combinatorial biomimetic chemistry. Parallel synthesis of a small library of β-hairpin mimetics based on loop III from human platelet-derived growth factor B
    • Jiang L, Moehle K, Dhanapal B, Obrecht D, Robinson JA. Combinatorial biomimetic chemistry. Parallel synthesis of a small library of β-hairpin mimetics based on loop III from human platelet-derived growth factor B. Helv. Chim. Acta 2000; 83: 3097-3112.
    • (2000) Helv. Chim. Acta , vol.83 , pp. 3097-3112
    • Jiang, L.1    Moehle, K.2    Dhanapal, B.3    Obrecht, D.4    Robinson, J.A.5
  • 29
    • 67651174506 scopus 로고    scopus 로고
    • Thermodynamic and computational studies on the binding of p53-derived peptides and peptidomimetic inhibitors to HDM2
    • Grässlin A, Amoreira C, Baldridge KK, Robinson JA. Thermodynamic and computational studies on the binding of p53-derived peptides and peptidomimetic inhibitors to HDM2. ChemBioChem 2009; 10: 1360-1368.
    • (2009) ChemBioChem , vol.10 , pp. 1360-1368
    • Grässlin, A.1    Amoreira, C.2    Baldridge, K.K.3    Robinson, J.A.4
  • 30
    • 33644896783 scopus 로고    scopus 로고
    • Structure-activity studies in a family of β-hairpin protein epitope mimetic inhibitors of the p53-HDM2 protein-protein interaction
    • Fasan R, Dias RLA, Moehle K, Zerbe O, Obrecht D, Mittl PRE, Grutter MG, Robinson JA. Structure-activity studies in a family of β-hairpin protein epitope mimetic inhibitors of the p53-HDM2 protein-protein interaction. ChemBioChem 2006; 7: 515-526.
    • (2006) ChemBioChem , vol.7 , pp. 515-526
    • Fasan, R.1    Dias, R.L.A.2    Moehle, K.3    Zerbe, O.4    Obrecht, D.5    Mittl, P.R.E.6    Grutter, M.G.7    Robinson, J.A.8
  • 31
    • 4544342753 scopus 로고    scopus 로고
    • Using a beta-hairpin to mimic an alpha-helix: cyclic peptidomimetic inhibitors of the p53-HDM2 protein-protein interaction
    • Fasan R, Dias RLA, Moehle K, Zerbe O, Vrijbloed JW, Obrecht D, Robinson JA. Using a beta-hairpin to mimic an alpha-helix: cyclic peptidomimetic inhibitors of the p53-HDM2 protein-protein interaction. Angew. Chem. Int. Ed. 2004; 43: 2109-2112.
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 2109-2112
    • Fasan, R.1    Dias, R.L.A.2    Moehle, K.3    Zerbe, O.4    Vrijbloed, J.W.5    Obrecht, D.6    Robinson, J.A.7
  • 36
    • 84862862332 scopus 로고    scopus 로고
    • Epithelial antimicrobial defence of the skin and intestine
    • Gallo RL, Hooper LV. Epithelial antimicrobial defence of the skin and intestine. Nat. Rev. Immunol. 2012; 12: 503-516.
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 503-516
    • Gallo, R.L.1    Hooper, L.V.2
  • 37
    • 84860601877 scopus 로고    scopus 로고
    • Antimicrobial peptides: key components of the innate immune system
    • Pasupuleti M, Schmidtchen A, Malmsten M. Antimicrobial peptides: key components of the innate immune system. Crit. Rev. Biotechnol. 2012; 32: 143-171.
    • (2012) Crit. Rev. Biotechnol. , vol.32 , pp. 143-171
    • Pasupuleti, M.1    Schmidtchen, A.2    Malmsten, M.3
  • 38
    • 84855865471 scopus 로고    scopus 로고
    • Emerging themes and therapeutic prospects for anti-infective peptides
    • Yount NY, Yeaman MR. Emerging themes and therapeutic prospects for anti-infective peptides. Annu. Rev. Pharmacol. Toxicol. 2012; 52: 337-360.
    • (2012) Annu. Rev. Pharmacol. Toxicol. , vol.52 , pp. 337-360
    • Yount, N.Y.1    Yeaman, M.R.2
  • 39
    • 79960782055 scopus 로고    scopus 로고
    • Antibiotic activities of host defense peptides: more to it than lipid bilayer perturbation
    • Wilmes M, Cammue BPA, Sahl H-G, Thevissen K. Antibiotic activities of host defense peptides: more to it than lipid bilayer perturbation. Nat. Prod. Rep. 2011; 28: 1350-1358.
    • (2011) Nat. Prod. Rep. , vol.28 , pp. 1350-1358
    • Wilmes, M.1    Cammue, B.P.A.2    Sahl, H.-G.3    Thevissen, K.4
  • 40
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • Nguyen LT, Haney EF, Vogel HJ. The expanding scope of antimicrobial peptide structures and their modes of action. Trends Biotechnol. 2011; 29: 464-472.
    • (2011) Trends Biotechnol. , vol.29 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 41
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 2005; 3: 238-250.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 42
    • 79955637689 scopus 로고    scopus 로고
    • Real-time attack on single Escherichia coli cells by the human antimicrobial peptide LL-37
    • Sochacki KA, Barns KJ, Bucki R, Weisshaar JC. Real-time attack on single Escherichia coli cells by the human antimicrobial peptide LL-37. Proc. Nat. Acad. Sci. 2011; 108: E77-E81.
    • (2011) Proc. Nat. Acad. Sci. , vol.108
    • Sochacki, K.A.1    Barns, K.J.2    Bucki, R.3    Weisshaar, J.C.4
  • 44
    • 77952298917 scopus 로고    scopus 로고
    • Current concepts: hospital-acquired infections due to Gram-negative bacteria
    • Peleg AY, Hooper DC. Current concepts: hospital-acquired infections due to Gram-negative bacteria. New Engl. J. Med. 2010; 362: 1804-1813.
    • (2010) New Engl. J. Med. , vol.362 , pp. 1804-1813
    • Peleg, A.Y.1    Hooper, D.C.2
  • 45
    • 80052080449 scopus 로고    scopus 로고
    • The structural biology of β-barrel membrane proteins: a summary of recent reports
    • Fairman JW, Noinaj N, Buchanan SK. The structural biology of β-barrel membrane proteins: a summary of recent reports. Curr. Opin. Struct. Biol. 2011; 21: 523-531.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 523-531
    • Fairman, J.W.1    Noinaj, N.2    Buchanan, S.K.3
  • 46
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the Gram-negative bacterial outer membrane
    • Bos MP, Robert V, Tommassen J. Biogenesis of the Gram-negative bacterial outer membrane. Annu. Rev. Microbiol. 2007; 61: 191-214.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 47
    • 69249230732 scopus 로고    scopus 로고
    • Transport of lipopolysaccharide across the cell envelope: the long road of discovery
    • Ruiz N, Kahne D, Silhavy TJ. Transport of lipopolysaccharide across the cell envelope: the long road of discovery. Nat. Rev. Microbiol. 2009; 7: 677-683.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 677-683
    • Ruiz, N.1    Kahne, D.2    Silhavy, T.J.3
  • 49
    • 79952289193 scopus 로고    scopus 로고
    • The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel
    • Freinkman E, Chng SS, Kahne D. The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel. Proc. Natl. Acad. Sci. U.S.A. 2011; 108: 2486-2491.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 2486-2491
    • Freinkman, E.1    Chng, S.S.2    Kahne, D.3
  • 50
    • 84856237412 scopus 로고    scopus 로고
    • Structural analysis of lipopolysaccharides from Gram-negative bacteria
    • Kabanov DS, Prokhorenko IR. Structural analysis of lipopolysaccharides from Gram-negative bacteria. Biochemistry (Moscow) 2010; 75: 469-491.
    • (2010) Biochemistry (Moscow) , vol.75 , pp. 469-491
    • Kabanov, D.S.1    Prokhorenko, I.R.2
  • 52
    • 77953084208 scopus 로고    scopus 로고
    • Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex
    • Chng SS, Gronenberg LS, Kahne D. Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex. Biochemistry 2010; 49: 4565-4567.
    • (2010) Biochemistry , vol.49 , pp. 4565-4567
    • Chng, S.S.1    Gronenberg, L.S.2    Kahne, D.3
  • 53
    • 84870243063 scopus 로고    scopus 로고
    • Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coli
    • Okuda S, Freinkman E, Kahne D. Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coli. Science 2012; 338: 1214-1217.
    • (2012) Science , vol.338 , pp. 1214-1217
    • Okuda, S.1    Freinkman, E.2    Kahne, D.3
  • 54
    • 46049106143 scopus 로고    scopus 로고
    • Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli
    • Sperandeo P, Lau FK, Carpentieri A, De Castro C, Molinaro A, Dehò G, Silhavy TJ, Polissi A. Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli. J. Bacteriol. 2008; 190: 4460-4469.
    • (2008) J. Bacteriol. , vol.190 , pp. 4460-4469
    • Sperandeo, P.1    Lau, F.K.2    Carpentieri, A.3    De Castro, C.4    Molinaro, A.5    Dehò, G.6    Silhavy, T.J.7    Polissi, A.8
  • 55
    • 33746852673 scopus 로고    scopus 로고
    • Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli
    • Wu T, McCandlish AC, Gronenberg LS, Chng S-S, Silhavy TJ, Kahne D. Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. 2006; 103: 11754-11759.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 11754-11759
    • Wu, T.1    McCandlish, A.C.2    Gronenberg, L.S.3    Chng, S.-S.4    Silhavy, T.J.5    Kahne, D.6
  • 57
    • 79952300098 scopus 로고    scopus 로고
    • Lipoprotein LptE is required for the assembly of LptD by the β-barrel assembly machine in the outer membrane of Escherichia coli
    • Chimalakonda G, Ruiz N, Chng SS, Garner RA, Kahne D, Silhavy TJ. Lipoprotein LptE is required for the assembly of LptD by the β-barrel assembly machine in the outer membrane of Escherichia coli. Proc. Nat. Acad. Sci. 2011; 108: 2492-2497.
    • (2011) Proc. Nat. Acad. Sci. , vol.108 , pp. 2492-2497
    • Chimalakonda, G.1    Ruiz, N.2    Chng, S.S.3    Garner, R.A.4    Kahne, D.5    Silhavy, T.J.6
  • 58
    • 79959468179 scopus 로고    scopus 로고
    • β-Barrel membrane protein assembly by the Bam complex
    • Hagan CL, Silhavy TJ, Kahne D. β-Barrel membrane protein assembly by the Bam complex. Annu. Rev. Biochem. 2011; 80: 189-210.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 189-210
    • Hagan, C.L.1    Silhavy, T.J.2    Kahne, D.3
  • 59
    • 84866759557 scopus 로고    scopus 로고
    • Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export
    • Chng SS, Xue MY, Garner RA, Kadokura H, Boyd D, Beckwith J, Kahne D. Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export. Science 2012; 337: 1665-1668.
    • (2012) Science , vol.337 , pp. 1665-1668
    • Chng, S.S.1    Xue, M.Y.2    Garner, R.A.3    Kadokura, H.4    Boyd, D.5    Beckwith, J.6    Kahne, D.7
  • 60
    • 77955463665 scopus 로고    scopus 로고
    • Nonconsecutive disulfide bond formation in an essential integral outer membrane protein
    • Ruiz N, Chng SS, Hiniker A, Kahne D, Silhavy TJ. Nonconsecutive disulfide bond formation in an essential integral outer membrane protein. Proc. Nat. Acad. Sci. 2010; 107: 12245-12250.
    • (2010) Proc. Nat. Acad. Sci. , vol.107 , pp. 12245-12250
    • Ruiz, N.1    Chng, S.S.2    Hiniker, A.3    Kahne, D.4    Silhavy, T.J.5
  • 63
    • 34249042613 scopus 로고    scopus 로고
    • The pan-genome: towards a knowledge-based discovery of novel targets for vaccines and antibacterials
    • Muzzi A, Masignani V, Rappuoli R. The pan-genome: towards a knowledge-based discovery of novel targets for vaccines and antibacterials. Drug Discov. Today 2007; 12: 429-439.
    • (2007) Drug Discov. Today , vol.12 , pp. 429-439
    • Muzzi, A.1    Masignani, V.2    Rappuoli, R.3
  • 65
    • 84867397072 scopus 로고    scopus 로고
    • Developing vaccines in the era of genomics: a decade of reverse vaccinology
    • Seib KL, Zhao X, Rappuoli R. Developing vaccines in the era of genomics: a decade of reverse vaccinology. Clin. Microbiol. Infect. 2012; 18: 109-116.
    • (2012) Clin. Microbiol. Infect. , vol.18 , pp. 109-116
    • Seib, K.L.1    Zhao, X.2    Rappuoli, R.3
  • 69
    • 78650476327 scopus 로고    scopus 로고
    • Adjuvants: no longer a 'dirty little secret', but essential key players in vaccines of the future
    • Arakawa T. Adjuvants: no longer a 'dirty little secret', but essential key players in vaccines of the future. Exp. Rev. Vaccines 2011; 10: 1-5.
    • (2011) Exp. Rev. Vaccines , vol.10 , pp. 1-5
    • Arakawa, T.1
  • 70
    • 55549114992 scopus 로고    scopus 로고
    • Structure-based antigen design: a strategy for next generation vaccines
    • Dormitzer PR, Ulmer JB, Rappuoli R. Structure-based antigen design: a strategy for next generation vaccines. Trends Biotechnol. 2008; 26: 659-667.
    • (2008) Trends Biotechnol. , vol.26 , pp. 659-667
    • Dormitzer, P.R.1    Ulmer, J.B.2    Rappuoli, R.3
  • 71
    • 84863774072 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses
    • Burton DR, Poignard P, Stanfield RL, Wilson IA. Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses. Science 2012; 337: 183-186.
    • (2012) Science , vol.337 , pp. 183-186
    • Burton, D.R.1    Poignard, P.2    Stanfield, R.L.3    Wilson, I.A.4
  • 75
    • 0042693012 scopus 로고    scopus 로고
    • Protein grafting of an HIV-1-inhibiting epitope
    • Sia SK, Kim PS. Protein grafting of an HIV-1-inhibiting epitope. Proc. Nat. Acad. Sci. 2003; 100: 9756-9761.
    • (2003) Proc. Nat. Acad. Sci. , vol.100 , pp. 9756-9761
    • Sia, S.K.1    Kim, P.S.2
  • 80
    • 82555168289 scopus 로고    scopus 로고
    • Structure-based design of a protein immunogen that displays an HIV-1 gp41 neutralizing epitope
    • Stanfield RL, Julien J-P, Pejchal R, Gach JS, Zwick MB, Wilson IA. Structure-based design of a protein immunogen that displays an HIV-1 gp41 neutralizing epitope. J. Mol. Biol. 2011; 414: 460-476.
    • (2011) J. Mol. Biol. , vol.414 , pp. 460-476
    • Stanfield, R.L.1    Julien, J.-P.2    Pejchal, R.3    Gach, J.S.4    Zwick, M.B.5    Wilson, I.A.6
  • 82
    • 79955953910 scopus 로고    scopus 로고
    • Epitope grafting, re-creating a conformational bet v 1 antibody epitope on the surface of the homologous apple allergen Mal d 1
    • Holm J, Ferreras M, Ipsen H, Wurtzen PA, Gajhede M, Larsen JN, Lund K, Spangfort MD. Epitope grafting, re-creating a conformational bet v 1 antibody epitope on the surface of the homologous apple allergen Mal d 1. J. Biol. Chem. 2011; 286: 17569-17578.
    • (2011) J. Biol. Chem. , vol.286 , pp. 17569-17578
    • Holm, J.1    Ferreras, M.2    Ipsen, H.3    Wurtzen, P.A.4    Gajhede, M.5    Larsen, J.N.6    Lund, K.7    Spangfort, M.D.8
  • 84
    • 80052047442 scopus 로고    scopus 로고
    • Stabilized helical peptides: overview of the technologies and therapeutic promises
    • Estieu-Gionnet K, Guichard G. Stabilized helical peptides: overview of the technologies and therapeutic promises. Exp. Opin. Drug Discov. 2011; 6: 937-963.
    • (2011) Exp. Opin. Drug Discov. , vol.6 , pp. 937-963
    • Estieu-Gionnet, K.1    Guichard, G.2
  • 85
    • 0031566953 scopus 로고    scopus 로고
    • Structure-based design of a constrained peptide mimic of the HIV-1 V3 loop neutralization site
    • Ghiara JB, Ferguson DC, Satterthwait AC, Dyson HJ, Wilson IA. Structure-based design of a constrained peptide mimic of the HIV-1 V3 loop neutralization site. J. Mol. Biol. 1997; 266: 31-39.
    • (1997) J. Mol. Biol. , vol.266 , pp. 31-39
    • Ghiara, J.B.1    Ferguson, D.C.2    Satterthwait, A.C.3    Dyson, H.J.4    Wilson, I.A.5
  • 86
    • 32444436232 scopus 로고    scopus 로고
    • Structure-function analysis of the epitope for 4E10, a broadly neutralizing human immunodeficiency virus type 1 antibody
    • Brunel FM, Zwick MB, Cardoso RMF, Nelson JD, Wilson IA, Burton DR, Dawson PE. Structure-function analysis of the epitope for 4E10, a broadly neutralizing human immunodeficiency virus type 1 antibody. J. Virol. 2006; 80: 1680-1687.
    • (2006) J. Virol. , vol.80 , pp. 1680-1687
    • Brunel, F.M.1    Zwick, M.B.2    Cardoso, R.M.F.3    Nelson, J.D.4    Wilson, I.A.5    Burton, D.R.6    Dawson, P.E.7
  • 87
    • 33845995027 scopus 로고    scopus 로고
    • Structural basis of enhanced binding of extended and helically constrained peptide epitopes of the broadly neutralizing HIV-1 antibody 4E10
    • Cardoso RMF, Brunel FM, Ferguson S, Zwick M, Burton DR, Dawson PE, Wilson IA. Structural basis of enhanced binding of extended and helically constrained peptide epitopes of the broadly neutralizing HIV-1 antibody 4E10. J. Mol. Biol. 2007; 365: 1533-1544.
    • (2007) J. Mol. Biol. , vol.365 , pp. 1533-1544
    • Cardoso, R.M.F.1    Brunel, F.M.2    Ferguson, S.3    Zwick, M.4    Burton, D.R.5    Dawson, P.E.6    Wilson, I.A.7
  • 88
    • 0036001491 scopus 로고    scopus 로고
    • Structure-affinity relationships in the gp41 ELDKWA epitope for the HIV-1 neutralizing monoclonal antibody 2F5: effects of side-chain and backbone modifications and conformational constraints
    • Tian Y, Ramesh CV, Ma X, Naqvi S, Patel T, Cenizal T, Tiscione M, Diaz K, Crea T, Arnold E, Arnold GF, Taylor JW. Structure-affinity relationships in the gp41 ELDKWA epitope for the HIV-1 neutralizing monoclonal antibody 2F5: effects of side-chain and backbone modifications and conformational constraints. J. Pept. Res. 2002; 59: 264-276.
    • (2002) J. Pept. Res. , vol.59 , pp. 264-276
    • Tian, Y.1    Ramesh, C.V.2    Ma, X.3    Naqvi, S.4    Patel, T.5    Cenizal, T.6    Tiscione, M.7    Diaz, K.8    Crea, T.9    Arnold, E.10    Arnold, G.F.11    Taylor, J.W.12
  • 90
    • 0033611958 scopus 로고    scopus 로고
    • The hydrogen bond mimic approach. Solid-phase synthesis of a peptide stabilized as an α-helix with a hydrazone link
    • Cabezas E, Satterthwait AC. The hydrogen bond mimic approach. Solid-phase synthesis of a peptide stabilized as an α-helix with a hydrazone link. J. Am. Chem. Soc. 1999; 121: 3862-3875.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 3862-3875
    • Cabezas, E.1    Satterthwait, A.C.2
  • 92
    • 0001515201 scopus 로고    scopus 로고
    • Conformationally constrained peptide mimetics: the use of a small lactam ring as an HIV-1 antigen constraint
    • Long RD, Moeller KD. Conformationally constrained peptide mimetics: the use of a small lactam ring as an HIV-1 antigen constraint. J. Am. Chem. Soc. 1997; 119: 12394-12395.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 12394-12395
    • Long, R.D.1    Moeller, K.D.2
  • 98
    • 69049103280 scopus 로고    scopus 로고
    • HIV-1 peptide vaccine candidates: selecting constrained V3 peptides with highest affinity to antibody 447-52D
    • Mester B, Manor R, Mor A, Arshava B, Rosen O, Ding FX, Naider F, Anglister J. HIV-1 peptide vaccine candidates: selecting constrained V3 peptides with highest affinity to antibody 447-52D. Biochemistry 2009; 48: 7867-7877.
    • (2009) Biochemistry , vol.48 , pp. 7867-7877
    • Mester, B.1    Manor, R.2    Mor, A.3    Arshava, B.4    Rosen, O.5    Ding, F.X.6    Naider, F.7    Anglister, J.8
  • 100
    • 77952299639 scopus 로고    scopus 로고
    • An optimally constrained V3 peptide is a better immunogen than its linear homolog or HIV-1 gp120
    • Moseri A, Tantry S, Sagi Y, Arshava B, Naider F, Anglister J. An optimally constrained V3 peptide is a better immunogen than its linear homolog or HIV-1 gp120. Virology 2010; 401: 293-304.
    • (2010) Virology , vol.401 , pp. 293-304
    • Moseri, A.1    Tantry, S.2    Sagi, Y.3    Arshava, B.4    Naider, F.5    Anglister, J.6
  • 101
    • 34250027638 scopus 로고    scopus 로고
    • Analysis of the neutralization breadth of the anti-V3 antibody F425-B4e8 and re-assessment of its epitope fine specificity by scanning mutagenesis
    • Pantophlet R, Aguilar-Sino RO, Wrin T, Cavacini LA, Burton DR. Analysis of the neutralization breadth of the anti-V3 antibody F425-B4e8 and re-assessment of its epitope fine specificity by scanning mutagenesis. Virology 2007; 364: 441-453.
    • (2007) Virology , vol.364 , pp. 441-453
    • Pantophlet, R.1    Aguilar-Sino, R.O.2    Wrin, T.3    Cavacini, L.A.4    Burton, D.R.5
  • 102
    • 33744933182 scopus 로고    scopus 로고
    • Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity
    • Stanfield RL, Gorny MK, Zolla-Pazner S, Wilson IA. Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity. J. Virol. 2006; 80: 6093-6105.
    • (2006) J. Virol. , vol.80 , pp. 6093-6105
    • Stanfield, R.L.1    Gorny, M.K.2    Zolla-Pazner, S.3    Wilson, I.A.4
  • 103
    • 70350714115 scopus 로고    scopus 로고
    • Structural basis of the cross-reactivity of genetically related human anti-HIV-1 mAbs: implications for design of V3-based immunogens
    • Burke V, Williams C, Sukumaran M, Kim S-S, Li H, Wang X-H, Gorny MK, Zolla-Pazner S, Kong X-P. Structural basis of the cross-reactivity of genetically related human anti-HIV-1 mAbs: implications for design of V3-based immunogens. Structure 2009; 17: 1538-1546.
    • (2009) Structure , vol.17 , pp. 1538-1546
    • Burke, V.1    Williams, C.2    Sukumaran, M.3    Kim, S.-S.4    Li, H.5    Wang, X.-H.6    Gorny, M.K.7    Zolla-Pazner, S.8    Kong, X.-P.9
  • 104
    • 33748996485 scopus 로고    scopus 로고
    • Molecular switch for alternative conformations of the HIV-1 V3 region: implications for phenotype conversion
    • Rosen O, Sharon M, Quadt-Akabayov SR, Anglister J. Molecular switch for alternative conformations of the HIV-1 V3 region: implications for phenotype conversion. Proc. Nat. Acad. Sci. 2006; 103: 13950-13955.
    • (2006) Proc. Nat. Acad. Sci. , vol.103 , pp. 13950-13955
    • Rosen, O.1    Sharon, M.2    Quadt-Akabayov, S.R.3    Anglister, J.4
  • 105
    • 1242351232 scopus 로고    scopus 로고
    • Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D
    • Stanfield RL, Gorny MK, Williams C, Zolla-Pazner S, Wilson IA. Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D. Structure 2004; 12: 193-204.
    • (2004) Structure , vol.12 , pp. 193-204
    • Stanfield, R.L.1    Gorny, M.K.2    Williams, C.3    Zolla-Pazner, S.4    Wilson, I.A.5
  • 110
    • 45749103230 scopus 로고    scopus 로고
    • The coming of age of virus-like particles
    • Jennings GT, Bachmann MF. The coming of age of virus-like particles. Biol. Chem. 2008; 389: 521-536.
    • (2008) Biol. Chem. , vol.389 , pp. 521-536
    • Jennings, G.T.1    Bachmann, M.F.2
  • 111
    • 84856941699 scopus 로고    scopus 로고
    • Pattern recognition receptors: sentinels in innate immunity and targets of new vaccine adjuvants
    • Olive C. Pattern recognition receptors: sentinels in innate immunity and targets of new vaccine adjuvants. Exp. Rev. Vaccines 2012; 11: 237-256.
    • (2012) Exp. Rev. Vaccines , vol.11 , pp. 237-256
    • Olive, C.1
  • 112
    • 34247622766 scopus 로고    scopus 로고
    • Toll-like receptors and innate immunity in B-cell activation and antibody responses
    • Lanzavecchia A, Sallusto F. Toll-like receptors and innate immunity in B-cell activation and antibody responses. Curr. Opin. Immunol. 2007; 19: 268-274.
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 268-274
    • Lanzavecchia, A.1    Sallusto, F.2
  • 113
    • 79959447465 scopus 로고    scopus 로고
    • Structural biology of the toll-like receptor family
    • Kang JY, Lee J-O. Structural biology of the toll-like receptor family. Annu. Rev. Biochem. 2011; 80: 917-941.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 917-941
    • Kang, J.Y.1    Lee, J.-O.2
  • 114
    • 78049288264 scopus 로고    scopus 로고
    • Vaccine delivery: a matter of size, geometry, kinetics and molecular patterns
    • Bachmann MF, Jennings GT. Vaccine delivery: a matter of size, geometry, kinetics and molecular patterns. Nat. Revs. Immunol. 2010; 10: 787-796.
    • (2010) Nat. Revs. Immunol. , vol.10 , pp. 787-796
    • Bachmann, M.F.1    Jennings, G.T.2
  • 115
    • 80455126057 scopus 로고    scopus 로고
    • Developments in virus-like particle-based vaccines for infectious diseases and cancer
    • Buonaguro L, Tagliamonte M, Tornesello ML, Buonaguro FM. Developments in virus-like particle-based vaccines for infectious diseases and cancer. Exp. Rev. Vaccines 2011; 10: 1569-1583.
    • (2011) Exp. Rev. Vaccines , vol.10 , pp. 1569-1583
    • Buonaguro, L.1    Tagliamonte, M.2    Tornesello, M.L.3    Buonaguro, F.M.4
  • 117
    • 0019985965 scopus 로고
    • Synthesis and assembly of hepatitis B virus surface antigen particles in yeast
    • Valenzuela P, Medina A, Rutter WJ, Ammerer G, Hall BD. Synthesis and assembly of hepatitis B virus surface antigen particles in yeast. Nature 1982; 298: 347-350.
    • (1982) Nature , vol.298 , pp. 347-350
    • Valenzuela, P.1    Medina, A.2    Rutter, W.J.3    Ammerer, G.4    Hall, B.D.5
  • 118
    • 0027050013 scopus 로고
    • Papillomavirus L1 major capsid protein self-assembles into virus-like particles that are highly immunogenic
    • Kirnbauer R, Booy F, Cheng N, Lowy DR, Schiller JT. Papillomavirus L1 major capsid protein self-assembles into virus-like particles that are highly immunogenic. Proc. Nat. Acad. Sci. 1992; 89: 12180-12184.
    • (1992) Proc. Nat. Acad. Sci. , vol.89 , pp. 12180-12184
    • Kirnbauer, R.1    Booy, F.2    Cheng, N.3    Lowy, D.R.4    Schiller, J.T.5
  • 119
    • 36849068111 scopus 로고    scopus 로고
    • Synthetic virus-like particles from self-assembling coiled-coil lipopeptides and their use in antigen display to the immune system
    • Boato F, Thomas RM, Ghasparian A, Freund Renard A, Moehle K, Robinson JA. Synthetic virus-like particles from self-assembling coiled-coil lipopeptides and their use in antigen display to the immune system. Angew. Chem. Int. Ed. 2007; 46: 9015-9018.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 9015-9018
    • Boato, F.1    Thomas, R.M.2    Ghasparian, A.3    Freund Renard, A.4    Moehle, K.5    Robinson, J.A.6
  • 122
    • 84865058597 scopus 로고    scopus 로고
    • Synthetic virus-like particles target dendritic cell lipid rafts for rapid endocytosis primarily but not exclusively by macropinocytosis
    • Sharma R, Ghasparian A, Robinson JA, McCullough KC. Synthetic virus-like particles target dendritic cell lipid rafts for rapid endocytosis primarily but not exclusively by macropinocytosis. PLoS One 2012; 7: e43248.
    • (2012) PLoS One , vol.7
    • Sharma, R.1    Ghasparian, A.2    Robinson, J.A.3    McCullough, K.C.4
  • 123
  • 126
    • 4544379899 scopus 로고    scopus 로고
    • Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope
    • Ofek G, Tang M, Sambor A, Katinger H, Mascola JR, Wyatt R, Kwong PD. Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J. Virol. 2004; 78: 10724-10737.
    • (2004) J. Virol. , vol.78 , pp. 10724-10737
    • Ofek, G.1    Tang, M.2    Sambor, A.3    Katinger, H.4    Mascola, J.R.5    Wyatt, R.6    Kwong, P.D.7
  • 127
    • 70350309664 scopus 로고    scopus 로고
    • Crystallographic definition of the epitope promiscuity of the broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2F5: vaccine design implications
    • Bryson S, Julien J-P, Hynes RC, Pai EF. Crystallographic definition of the epitope promiscuity of the broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2F5: vaccine design implications. J. Virol. 2009; 83: 11862-11875.
    • (2009) J. Virol. , vol.83 , pp. 11862-11875
    • Bryson, S.1    Julien, J.-P.2    Hynes, R.C.3    Pai, E.F.4
  • 128
    • 54849416088 scopus 로고    scopus 로고
    • Structural details of HIV-1 recognition by the broadly neutralizing monoclonal antibody 2F5: epitope conformation, antigen-recognition loop mobility, and anion-binding site
    • Julien J-P, Bryson S, Nieva JL, Pai EF. Structural details of HIV-1 recognition by the broadly neutralizing monoclonal antibody 2F5: epitope conformation, antigen-recognition loop mobility, and anion-binding site. J. Mol. Biol. 2008; 384: 377-392.
    • (2008) J. Mol. Biol. , vol.384 , pp. 377-392
    • Julien, J.-P.1    Bryson, S.2    Nieva, J.L.3    Pai, E.F.4
  • 129
    • 13844255333 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41
    • Cardoso RMF, Zwick MB, Stanfield RL, Kunert R, Binley JM, Katinger H, Burton DR, Wilson IA. Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity 2005; 22: 163-173.
    • (2005) Immunity , vol.22 , pp. 163-173
    • Cardoso, R.M.F.1    Zwick, M.B.2    Stanfield, R.L.3    Kunert, R.4    Binley, J.M.5    Katinger, H.6    Burton, D.R.7    Wilson, I.A.8
  • 130
  • 131
    • 69249220320 scopus 로고    scopus 로고
    • A conformational switch in human immunodeficiency virus gp41 revealed by the structures of overlapping epitopes recognized by neutralizing antibodies
    • Pejchal R, Gach JS, Brunel FM, Cardoso RM, Stanfield RL, Dawson PE, Burton DR, Zwick MB, Wilson IA. A conformational switch in human immunodeficiency virus gp41 revealed by the structures of overlapping epitopes recognized by neutralizing antibodies. J. Virol. 2009; 83: 8451-8462.
    • (2009) J. Virol. , vol.83 , pp. 8451-8462
    • Pejchal, R.1    Gach, J.S.2    Brunel, F.M.3    Cardoso, R.M.4    Stanfield, R.L.5    Dawson, P.E.6    Burton, D.R.7    Zwick, M.B.8    Wilson, I.A.9
  • 137
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998; 393: 648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 143
    • 84869229723 scopus 로고    scopus 로고
    • Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33
    • Kong L, Giang E, Nieusma T, Robbins JB, Deller MC, Stanfield RL, Wilson IA, Law M. Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33. J. Virol. 2012; 86: 13085-13088.
    • (2012) J. Virol. , vol.86 , pp. 13085-13088
    • Kong, L.1    Giang, E.2    Nieusma, T.3    Robbins, J.B.4    Deller, M.C.5    Stanfield, R.L.6    Wilson, I.A.7    Law, M.8
  • 144
    • 84869233037 scopus 로고    scopus 로고
    • Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody
    • Potter JA, Owsianka AM, Jeffery N, Matthews DJ, Keck ZY, Lau P, Foung SKH, Taylor GL, Patel AH. Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody. J. Virol. 2012; 86: 12923-12932.
    • (2012) J. Virol. , vol.86 , pp. 12923-12932
    • Potter, J.A.1    Owsianka, A.M.2    Jeffery, N.3    Matthews, D.J.4    Keck, Z.Y.5    Lau, P.6    Foung, S.K.H.7    Taylor, G.L.8    Patel, A.H.9
  • 149
    • 77951165843 scopus 로고    scopus 로고
    • Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus
    • Xu R, Ekiert DC, Krause JC, Hai R, Crowe JE, Wilson IA. Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus. Science 2010; 328: 357-360.
    • (2010) Science , vol.328 , pp. 357-360
    • Xu, R.1    Ekiert, D.C.2    Krause, J.C.3    Hai, R.4    Crowe, J.E.5    Wilson, I.A.6
  • 150
    • 84867641531 scopus 로고    scopus 로고
    • Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity
    • Lee PS, Yoshida R, Ekiert DC, Sakai N, Suzuki Y, Takada A, Wilson IA. Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity. Proc. Nat. Acad. Sci. 2012; 109: 17040-17045.
    • (2012) Proc. Nat. Acad. Sci. , vol.109 , pp. 17040-17045
    • Lee, P.S.1    Yoshida, R.2    Ekiert, D.C.3    Sakai, N.4    Suzuki, Y.5    Takada, A.6    Wilson, I.A.7
  • 152
    • 79960387921 scopus 로고    scopus 로고
    • Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes
    • McLellan JS, Yang Y, Graham BS, Kwong PD. Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes. J. Virol. 2011; 85: 7788-7796.
    • (2011) J. Virol. , vol.85 , pp. 7788-7796
    • McLellan, J.S.1    Yang, Y.2    Graham, B.S.3    Kwong, P.D.4
  • 153
    • 78049495019 scopus 로고    scopus 로고
    • Structure of a major antigenic site on the respiratory syncytial virus fusion glycoprotein in complex with neutralizing antibody 101F
    • McLellan JS, Chen M, Chang J-S, Yang Y, Kim A, Graham BS, Kwong PD. Structure of a major antigenic site on the respiratory syncytial virus fusion glycoprotein in complex with neutralizing antibody 101F. J. Virol. 2010; 84: 12236-12244.
    • (2010) J. Virol. , vol.84 , pp. 12236-12244
    • McLellan, J.S.1    Chen, M.2    Chang, J.-S.3    Yang, Y.4    Kim, A.5    Graham, B.S.6    Kwong, P.D.7
  • 155
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor
    • Lee JE, Fusco ML, Hessell AJ, Oswald WB, Burton DR, Saphire EO. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 2008; 454: 177-182.
    • (2008) Nature , vol.454 , pp. 177-182
    • Lee, J.E.1    Fusco, M.L.2    Hessell, A.J.3    Oswald, W.B.4    Burton, D.R.5    Saphire, E.O.6
  • 156
    • 36348950301 scopus 로고    scopus 로고
    • Complex of a protective antibody with its Ebola virus gp peptide epitope: unusual features of a Vλx light chain
    • Lee JE, Kuehne A, Abelson DM, Fusco ML, Hart MK, Saphire EO. Complex of a protective antibody with its Ebola virus gp peptide epitope: unusual features of a Vλx light chain. J. Mol. Biol. 2008; 375: 202-216.
    • (2008) J. Mol. Biol. , vol.375 , pp. 202-216
    • Lee, J.E.1    Kuehne, A.2    Abelson, D.M.3    Fusco, M.L.4    Hart, M.K.5    Saphire, E.O.6
  • 161
    • 34547207674 scopus 로고    scopus 로고
    • Broadly neutralizing anti-hepatitis B virus antibody reveals a complementarity determining region H3 lid-opening mechanism
    • Chi SW, Maeng CY, Kim SJ, Oh MS, Ryu CJ, Kim SJ, Han KH, Hong HJ, Ryu SE. Broadly neutralizing anti-hepatitis B virus antibody reveals a complementarity determining region H3 lid-opening mechanism. Proc. Nat. Acad. Sci. 2007; 104: 9230-9235.
    • (2007) Proc. Nat. Acad. Sci. , vol.104 , pp. 9230-9235
    • Chi, S.W.1    Maeng, C.Y.2    Kim, S.J.3    Oh, M.S.4    Ryu, C.J.5    Kim, S.J.6    Han, K.H.7    Hong, H.J.8    Ryu, S.E.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.