메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Approaching rational epitope vaccine design for hepatitis C virus with meta-server and multivalent scaffolding

Author keywords

[No Author keywords available]

Indexed keywords

E1 PROTEIN, HEPATITIS C VIRUS; EPITOPE; HEPATITIS VACCINE; NEUTRALIZING ANTIBODY; PROTEIN BINDING; RECOMBINANT PROTEIN; VIRUS ANTIGEN; VIRUS ENVELOPE PROTEIN;

EID: 84938769263     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep12501     Document Type: Article
Times cited : (64)

References (91)
  • 1
    • 59149085501 scopus 로고    scopus 로고
    • The global burden of hepatitis c
    • Lavanchy, D. The global burden of hepatitis C. Liver Int. 29, 74-81, doi: 10.1111/j.1478-3231.2008.01934.x (2009
    • (2009) Liver Int , vol.29 , pp. 74-81
    • Lavanchy, D.1
  • 2
    • 84857144025 scopus 로고    scopus 로고
    • The increasing burden of mortality from viral hepatitis in the United States between 1999 and 2007
    • Ly, K. N., et al. The increasing burden of mortality from viral hepatitis in the United States between 1999 and 2007. Ann. Intern. Med. 156, 271-278, doi: 10.7326/0003-4819-156-4-201202210-00004 (2012
    • (2012) Ann. Intern. Med , vol.156 , pp. 271-278
    • Ly, K.N.1
  • 3
    • 23944506014 scopus 로고    scopus 로고
    • Global epidemiology of hepatitis C virus infection
    • Shepard, C. W., Finelli, L. & Alter, M. Global epidemiology of hepatitis C virus infection. Lancet Infect. Dis. 5, 558-567, doi: 10.1016/s1473-3099(05)70216-4 (2005
    • (2005) Lancet Infect. Dis , vol.5 , pp. 558-567
    • Shepard, C.W.1    Finelli, L.2    Alter, M.3
  • 4
    • 84921060015 scopus 로고    scopus 로고
    • Global distribution and prevalence of hepatitis c virus genotypes
    • Messina, J. P., et al. Global distribution and prevalence of hepatitis C virus genotypes. Hepatology 61, 77-87, doi: 10.1002/hep.27259 (2015
    • (2015) Hepatology , vol.61 , pp. 77-87
    • Messina, J.P.1
  • 5
    • 84901586232 scopus 로고    scopus 로고
    • Hepatitis c treatment: An incipient therapeutic revolution
    • deLemos, A. S. & Chung, R. T. Hepatitis C treatment: an incipient therapeutic revolution. Trends Mol. Med. 20, 315-321, doi: 10.1016/j.molmed.2014.02.002 (2014
    • (2014) Trends Mol. Med , vol.20 , pp. 315-321
    • Delemos, A.S.1    Chung, R.T.2
  • 6
    • 84880301028 scopus 로고    scopus 로고
    • Current progress in development of hepatitis c virus vaccines
    • Liang, T. J. Current progress in development of hepatitis C virus vaccines. Nat. Med. 19, 869-878, doi: 10.1038/nm.3183 (2013
    • (2013) Nat. Med , vol.19 , pp. 869-878
    • Liang, T.J.1
  • 7
    • 23944452579 scopus 로고    scopus 로고
    • Prospects for a vaccine against the hepatitis c virus
    • Houghton, M. & Abrignani, S. Prospects for a vaccine against the hepatitis C virus. Nature 436, 961-966, doi: 10.1038/nature04081 (2005
    • (2005) Nature , vol.436 , pp. 961-966
    • Houghton, M.1    Abrignani, S.2
  • 8
    • 84865742652 scopus 로고    scopus 로고
    • Prospects for prophylactic and therapeutic vaccines against hepatitis c virus
    • Feinstone, S. M., Hu, D. J. & Major, M. E. Prospects for prophylactic and therapeutic vaccines against hepatitis C virus. Clin. Infect. Dis. 55, S25-S32, doi: 10.1093/cid/cis362 (2012
    • (2012) Clin. Infect. Dis , vol.55 , pp. S25-S32
    • Feinstone, S.M.1    Hu, D.J.2    Major, M.E.3
  • 9
    • 22344448015 scopus 로고    scopus 로고
    • Mutational escape from cd8(+ ) t cell immunity: Hcv evolution, from chimpanzees to man
    • Bowen, D. G. & Walker, C. M. Mutational escape from CD8(+ ) T cell immunity: HCV evolution, from chimpanzees to man. J. Exp. Med. 201, 1709-1714, doi: 10.1084/jem.20050808 (2005
    • (2005) J. Exp. Med , vol.201 , pp. 1709-1714
    • Bowen, D.G.1    Walker, C.M.2
  • 10
    • 7444256169 scopus 로고    scopus 로고
    • Genetic diversity and evolution of hepatitis c virus-15 years on
    • Simmonds, P. Genetic diversity and evolution of hepatitis C virus-15 years on. J. Gen. Virol. 85, 3173-3188, doi: 10.1099/vir.0.80401-0 (2004
    • (2004) J. Gen. Virol , vol.85 , pp. 3173-3188
    • Simmonds, P.1
  • 11
    • 0032582538 scopus 로고    scopus 로고
    • Binding of hepatitis c virus to cd81
    • Pileri, P., et al. Binding of hepatitis C virus to CD81. Science 282, 938-941, doi: 10.1126/science.282.5390.938 (1998
    • (1998) Science , vol.282 , pp. 938-941
    • Pileri, P.1
  • 12
    • 18644378971 scopus 로고    scopus 로고
    • The human scavenger receptor class b type i is a novel candidate receptor for the hepatitis c virus
    • Scarselli, E., et al. The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus. EMBO J. 21, 5017-5025, doi: 10.1093/emboj/cdf529 (2002
    • (2002) EMBO J. , vol.21 , pp. 5017-5025
    • Scarselli, E.1
  • 13
    • 84900798422 scopus 로고    scopus 로고
    • Structure of the core ectodomain of the hepatitis c virus envelope glycoprotein 2
    • Khan, A. G., et al. Structure of the core ectodomain of the hepatitis C virus envelope glycoprotein 2. Nature 509, 381-384, doi: 10.1038/nature13117 (2014
    • (2014) Nature , vol.509 , pp. 381-384
    • Khan, A.G.1
  • 14
    • 77649269513 scopus 로고    scopus 로고
    • The disulfide bonds in glycoprotein e2 of hepatitis c virus reveal the tertiary organization of the molecule
    • Krey, T., et al. The disulfide bonds in glycoprotein E2 of hepatitis C virus reveal the tertiary organization of the molecule. PLoS Pathog. 6, e1000762, doi: 10.1371/journal.ppat.1000762 (2010
    • (2010) PLoS Pathog , vol.6 , pp. e1000762
    • Krey, T.1
  • 15
    • 34547775736 scopus 로고    scopus 로고
    • Characterization of fusion determinants points to the involvement of three discrete regions of both e1 and e2 glycoproteins in the membrane fusion process of hepatitis c virus
    • Lavillette, D., et al. Characterization of fusion determinants points to the involvement of three discrete regions of both E1 and E2 glycoproteins in the membrane fusion process of hepatitis C virus. J. Virol. 81, 8752-8765, doi: 10.1128/jvi.02642-06 (2007
    • (2007) J. Virol , vol.81 , pp. 8752-8765
    • Lavillette, D.1
  • 17
    • 0034959575 scopus 로고    scopus 로고
    • Intrahepatic genetic inoculation of hepatitis c virus RNA confers cross-protective immunity
    • Weiner, A. J., et al. Intrahepatic genetic inoculation of hepatitis C virus RNA confers cross-protective immunity. J. Virol. 75, 7142-7148, doi: 10.1128/jvi.75.15.7142-7148.2001 (2001
    • (2001) J. Virol , vol.75 , pp. 7142-7148
    • Weiner, A.J.1
  • 18
    • 12644289313 scopus 로고    scopus 로고
    • Prevention of hepatitis c virus infection in chimpanzees by hyperimmune serum against the hypervariable region 1 of the envelope 2 protein
    • Farci, P., et al. Prevention of hepatitis C virus infection in chimpanzees by hyperimmune serum against the hypervariable region 1 of the envelope 2 protein. Proc. Natl. Acad. Sci. USA 93, 15394-15399, doi: 10.1073/pnas.93.26.15394 (1996
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15394-15399
    • Farci, P.1
  • 19
    • 0027081378 scopus 로고
    • Characterization of hypervariable regions in the putative envelope protein of hepatitis c virus
    • Kato, N., et al. Characterization of hypervariable regions in the putative envelope protein of hepatitis C virus. Biochem. Biophys. Res. Commun. 189, 119-127, doi: 10.1016/0006-291x(92)91533-v (1992
    • (1992) Biochem. Biophys. Res. Commun , vol.189 , pp. 119-127
    • Kato, N.1
  • 20
    • 0030587469 scopus 로고    scopus 로고
    • A hyperimmune serum against a synthetic peptide corresponding to the hypervariable region 1 of hepatitis c virus can prevent viral infection in cell cultures
    • Shimizu, Y. K., et al A hyperimmune serum against a synthetic peptide corresponding to the hypervariable region 1 of hepatitis C virus can prevent viral infection in cell cultures. Virology 223, 409-412, doi: 10.1006/viro.1996.0497 (1996
    • (1996) Virology , vol.223 , pp. 409-412
    • Shimizu, Y.K.1
  • 21
    • 0026025737 scopus 로고
    • Variable and hypervariable domains are found in the regions of hcv corresponding to the flavivirus envelope and ns1 proteins and the pestivirus envelope glycoproteins
    • Weiner, A. J., et al. Variable and hypervariable domains are found in the regions of HCV corresponding to the flavivirus envelope and NS1 proteins and the pestivirus envelope glycoproteins. Virology 180, 842-848, doi: 10.1016/0042-6822(91)90104-j (1991
    • (1991) Virology , vol.180 , pp. 842-848
    • Weiner, A.J.1
  • 22
    • 0034646996 scopus 로고    scopus 로고
    • The outcome of acute hepatitis c predicted by the evolution of the viral quasispecies
    • Farci, P., et al. The outcome of acute hepatitis C predicted by the evolution of the viral quasispecies. Science 288, 339-344, doi: 10.1126/science.288.5464.339 (2000
    • (2000) Science , vol.288 , pp. 339-344
    • Farci, P.1
  • 23
    • 70450162452 scopus 로고    scopus 로고
    • Identification and characterization of broadly neutralizing human monoclonal antibodies directed against the e2 evelope glycoprotein of hepatitis c virus
    • Broering, T. J., et al. Identification and characterization of broadly neutralizing human monoclonal antibodies directed against the E2 evelope glycoprotein of hepatitis C virus. J. Virol. 83, 12473-12482, doi: 10.1128/jvi.01138-09 (2009
    • (2009) J. Virol , vol.83 , pp. 12473-12482
    • Broering, T.J.1
  • 24
    • 84861205239 scopus 로고    scopus 로고
    • Human monoclonal antibodies to a novel cluster of conformational epitopes on hcv e2 with resistance to neutralization escape in a genotype 2a isolate
    • Keck, Z.-y., et al. Human monoclonal antibodies to a novel cluster of conformational epitopes on HCV E2 with resistance to neutralization escape in a genotype 2a isolate. PLoS Pathog. 8, e1002653, doi: 10.1371/journal.ppat.1002653 (2012
    • (2012) PLoS Pathog , vol.8 , pp. e1002653
    • Keck, Z.-Y.1
  • 25
    • 38049083122 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies protect against hepatitis c virus quasispecies challenge
    • Law, M., et al. Broadly neutralizing antibodies protect against hepatitis C virus quasispecies challenge. Nat. Med. 14, 25-27, doi: 10.1038/nm1698 (2008
    • (2008) Nat. Med , vol.14 , pp. 25-27
    • Law, M.1
  • 26
    • 23844553059 scopus 로고    scopus 로고
    • Monoclonal antibody ap33 defines a broadly neutralizing epitope on the hepatitis c virus e2 envelope glycoprotein
    • Owsianka, A., et al. Monoclonal antibody AP33 defines a broadly neutralizing epitope on the hepatitis C virus E2 envelope glycoprotein. J. Virol. 79, 11095-11104, doi: 10.1128/jvi.79.17.11095-11104.2005 (2005
    • (2005) J. Virol , vol.79 , pp. 11095-11104
    • Owsianka, A.1
  • 27
    • 36048952785 scopus 로고    scopus 로고
    • Human combinatorial libraries yield rare antibodies that broadly neutralize hepatitis c virus
    • Johansson, D. X., et al. Human combinatorial libraries yield rare antibodies that broadly neutralize hepatitis C virus. Proc. Natl. Acad. Sci. USA 104, 16269-16274, doi: 10.1073/pnas.0705522104 (2007
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 16269-16274
    • Johansson, D.X.1
  • 28
    • 37849010852 scopus 로고    scopus 로고
    • Isolation and characterization of broadly neutralizing human monoclonal antibodies to the e1 glycoprotein of hepatitis c virus
    • Meunier, J.-C., et al. Isolation and characterization of broadly neutralizing human monoclonal antibodies to the E1 glycoprotein of hepatitis C virus. J. Virol. 82, 966-973, doi: 10.1128/jvi.01872-07 (2008
    • (2008) J. Virol , vol.82 , pp. 966-973
    • Meunier, J.-C.1
  • 30
    • 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., et al. Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33. J. Virol. 86, 13085-13088, doi: 10.1128/jvi.01939-12 (2012
    • (2012) J. Virol , vol.86 , pp. 13085-13088
    • Kong, L.1
  • 31
    • 84862177880 scopus 로고    scopus 로고
    • Structural basis of hepatitis c virus neutralization by broadly neutralizing antibody hcv1
    • Kong, L., et al. Structural basis of hepatitis C virus neutralization by broadly neutralizing antibody HCV1. Proc. Natl. Acad. Sci. USA 109, 9499-9504, doi: 10.1073/pnas.1202924109 (2012
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 9499-9504
    • Kong, L.1
  • 32
    • 84878472445 scopus 로고    scopus 로고
    • Structural basis of hcv neutralization by human monoclonal antibodies resistant to viral neutralization escape
    • Krey, T., et al. Structural basis of HCV neutralization by human monoclonal antibodies resistant to viral neutralization escape. PLoS Pathog. 9, e1003364, doi: 10.1371/journal.ppat.1003364 (2013
    • (2013) PLoS Pathog , vol.9 , pp. e1003364
    • Krey, T.1
  • 33
    • 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, J. A., et al. Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody. J. Virol. 86, 12923-12932, doi: 10.1128/jvi.02052-12 (2012
    • (2012) J. Virol , vol.86 , pp. 12923-12932
    • Potter, J.A.1
  • 34
    • 84877720407 scopus 로고    scopus 로고
    • Glycan shifting on hepatitis c virus (hcv) e2 glycoprotein is a mechanism for escape from broadly neutralizing antibodies
    • Pantua, H., et al. Glycan shifting on hepatitis C virus (HCV) E2 glycoprotein is a mechanism for escape from broadly neutralizing antibodies. J. Mol. Biol. 425, 1899-1914, doi: 10.1016/j.jmb.2013.02.025 (2013
    • (2013) J. Mol. Biol , vol.425 , pp. 1899-1914
    • Pantua, H.1
  • 35
    • 84888778890 scopus 로고    scopus 로고
    • Hepatitis c virus e2 envelope glycoprotein core structure
    • Kong, L., et al. Hepatitis C virus E2 envelope glycoprotein core structure. Science 342, 1090-1094, doi: 10.1126/science.1243876 (2013
    • (2013) Science , vol.342 , pp. 1090-1094
    • Kong, L.1
  • 36
    • 84898023899 scopus 로고    scopus 로고
    • Unraveling hepatitis c virus structure
    • Fauvelle, C., Felmlee, D. J. & Baumert, T. F. Unraveling hepatitis C virus structure. Cell Res. 24, 385-386, doi: 10.1038/cr.2014.31 (2014
    • (2014) Cell Res , vol.24 , pp. 385-386
    • Fauvelle, C.1    Felmlee, D.J.2    Baumert, T.F.3
  • 37
    • 82155191729 scopus 로고    scopus 로고
    • Hepatitis c virus evasion mechanisms from neutralizing antibodies
    • Di Lorenzo, C., Angus, A. G. N. & Patel, A. H. Hepatitis C virus evasion mechanisms from neutralizing antibodies. Viruses-Basel 3, 2280-2300, doi: 10.3390/v3112280 (2011
    • (2011) Viruses-Basel , vol.3 , pp. 2280-2300
    • Di Lorenzo, C.1    Angus, A.G.N.2    Patel, A.H.3
  • 38
    • 80054987354 scopus 로고    scopus 로고
    • The hepatitis c virus glycan shield and evasion of the humoral immune response
    • Helle, F., Duverlie, G. & Dubuisson, J. The hepatitis C virus glycan shield and evasion of the humoral immune response. Viruses-Basel 3, 1909-1932, doi: 10.3390/v3101909 (2011
    • (2011) Viruses-Basel , vol.3 , pp. 1909-1932
    • Helle, F.1    Duverlie, G.2    Dubuisson, J.3
  • 39
    • 78149277602 scopus 로고    scopus 로고
    • Scaffolding to build a rational vaccine design strategy
    • Burton, D. R. Scaffolding to build a rational vaccine design strategy. Proc. Natl. Acad. Sci. USA 107, 17859-17860, doi: 10.1073/pnas.1012923107 (2010
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17859-17860
    • Burton, D.R.1
  • 40
    • 78650414310 scopus 로고    scopus 로고
    • Computational protein design using flexible backbone remodeling and resurfacing: Case studies in structurebased antigen design
    • Correia, B. E., et al. Computational protein design using flexible backbone remodeling and resurfacing: case studies in structurebased antigen design. J. Mol. Biol. 405, 284-297, doi: 10.1016/j.jmb.2010.09.061 (2011
    • (2011) J. Mol. Biol , vol.405 , pp. 284-297
    • Correia, B.E.1
  • 41
    • 78149242586 scopus 로고    scopus 로고
    • Elicitation of structure-specific antibodies by epitope scaffolds
    • Ofek, G., et al. Elicitation of structure-specific antibodies by epitope scaffolds. Proc. Natl. Acad. Sci. USA 107, 17880-17887, doi: 10.1073/pnas.1004728107 (2010
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17880-17887
    • Ofek, G.1
  • 42
    • 84903757787 scopus 로고    scopus 로고
    • Transplanting supersites of HIV-1 vulnerability
    • Zhou, T., et al. Transplanting supersites of HIV-1 vulnerability. PLoS ONE 9, e99881, doi: 10.1371/journal.pone.0099881 (2014
    • (2014) PLoS ONE , vol.9 , pp. e99881
    • Zhou, T.1
  • 43
    • 79958059341 scopus 로고    scopus 로고
    • Design and characterization of epitope-scaffold immunogens that present the motavizumab epitope from respiratory syncytial virus
    • McLellan, J. S., et al. Design and characterization of epitope-scaffold immunogens that present the motavizumab epitope from respiratory syncytial virus. J. Mol. Biol. 409, 853-866, doi: 10.1016/j.jmb.2011.04.044 (2011
    • (2011) J. Mol. Biol , vol.409 , pp. 853-866
    • McLellan, J.S.1
  • 44
    • 84896315237 scopus 로고    scopus 로고
    • Proof of principle for epitope-focused vaccine design
    • Correia, B. E., et al. Proof of principle for epitope-focused vaccine design. Nature 507, 201-206, doi: 10.1038/nature12966 (2014
    • (2014) Nature , vol.507 , pp. 201-206
    • Correia, B.E.1
  • 45
    • 84961289547 scopus 로고    scopus 로고
    • Computational tools for epitope vaccine design and evaluation
    • He, L. & Zhu, J. Computational tools for epitope vaccine design and evaluation. Curr. Opin. Virol. 11, 103-112, doi: 10.1016/j. coviro.2015.03.013 (2015
    • (2015) Curr. Opin. Virol , vol.11 , pp. 103-112
    • He, L.1    Zhu, J.2
  • 46
    • 77956317558 scopus 로고    scopus 로고
    • Computational design of epitope-scaffolds allows induction of antibodies specific for a poorly immunogenic HIV vaccine epitope
    • Correia, B. E., et al. Computational design of epitope-scaffolds allows induction of antibodies specific for a poorly immunogenic HIV vaccine epitope. Structure 18, 1116-1126, doi: 10.1016/j.str.2010.06.010 (2010
    • (2010) Structure , vol.18 , pp. 1116-1126
    • Correia, B.E.1
  • 47
    • 84855258847 scopus 로고    scopus 로고
    • Computational design of high-Affinity epitope scaffolds by backbone grafting of a linear epitope
    • Azoitei, M. L., et al. Computational design of high-Affinity epitope scaffolds by backbone grafting of a linear epitope. J. Mol. Biol. 415, 175-192, doi: 10.1016/j.jmb.2011.10.003 (2012
    • (2012) J. Mol. Biol , vol.415 , pp. 175-192
    • Azoitei, M.L.1
  • 48
    • 44949145113 scopus 로고    scopus 로고
    • Progress and challenges in protein structure prediction
    • Zhang, Y. Progress and challenges in protein structure prediction. Curr. Opin. Struct. Biol. 18, 342-348, doi: 10.1016/i. sbi.2008.02.004 (2008
    • (2008) Curr. Opin. Struct. Biol , vol.18 , pp. 342-348
    • Zhang, Y.1
  • 49
    • 0036839162 scopus 로고    scopus 로고
    • Mammoth (matching molecular models obtained from theory an automated method for model comparison
    • Ortiz, A. R., Strauss, C. E. M. & Olmea, O. MAMMOTH (Matching molecular models obtained from theory): An automated method for model comparison. Protein Sci. 11, 2606-2621, doi: 10.1110/ps.0215902 (2002
    • (2002) Protein Sci , vol.11 , pp. 2606-2621
    • Ortiz, A.R.1    Strauss, C.E.M.2    Olmea, O.3
  • 50
    • 17644392830 scopus 로고    scopus 로고
    • Tm-Align a protein structure alignment algorithm based on the tm-score
    • Zhang, Y. & Skolnick, J. TM-Align: a protein structure alignment algorithm based on the TM-score. Nucleic Acids Res. 33, 2302-2309, doi: 10.1093/nar/gki524 (2005
    • (2005) Nucleic Acids Res , vol.33 , pp. 2302-2309
    • Zhang, Y.1    Skolnick, J.2
  • 51
    • 84863784145 scopus 로고    scopus 로고
    • A new size-independent score for pairwise protein structure alignment and its application to structure classification and nucleic-Acid binding prediction
    • Yang, Y., Zhan, J., Zhao, H. & Zhou, Y A new size-independent score for pairwise protein structure alignment and its application to structure classification and nucleic-Acid binding prediction. Proteins 80, 2080-2088, doi: 10.1002/prot.24100 (2012
    • (2012) Proteins , vol.80 , pp. 2080-2088
    • Yang, Y.1    Zhan, J.2    Zhao, H.3    Zhou, Y.4
  • 52
    • 79959919131 scopus 로고    scopus 로고
    • Click-Topology-independent comparison of biomolecular 3d structures
    • Nguyen, M. N., Tan, K. P. & Madhusudhan, M. S. CLICK-Topology-independent comparison of biomolecular 3D structures. Nucleic Acids Res. 39, W24-W28, doi: 10.1093/nar/gkr393 (2011
    • (2011) Nucleic Acids Res , vol.39 , pp. W24-W28
    • Nguyen, M.N.1    Tan, K.P.2    Madhusudhan, M.S.3
  • 53
    • 12944271968 scopus 로고    scopus 로고
    • Fast: A novel protein structure alignment algorithm
    • Zhu, J. H. & Weng, Z. P. FAST: A novel protein structure alignment algorithm. Proteins 58, 618-627, doi: 10.1002/prot.20331 (2005
    • (2005) Proteins , vol.58 , pp. 618-627
    • Zhu, J.H.1    Weng, Z.P.2
  • 54
    • 0043180474 scopus 로고    scopus 로고
    • Pisces: A protein sequence culling server
    • Wang, G. L. & Dunbrack, R. L. PISCES: a protein sequence culling server. Bioinformatics 19, 1589-1591, doi: 10.1093/bioinformatics/btg224 (2003
    • (2003) Bioinformatics , vol.19 , pp. 1589-1591
    • Wang, G.L.1    Dunbrack, R.L.2
  • 55
    • 0036838311 scopus 로고    scopus 로고
    • Distance-scaled finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction
    • Zhou, H. Y. & Zhou, Y. Q. Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci. 11, 2714-2726, doi: 10.1110/ps.0217002 (2002
    • (2002) Protein Sci , vol.11 , pp. 2714-2726
    • Zhou, H.Y.1    Zhou, Y.Q.2
  • 56
    • 51349134973 scopus 로고    scopus 로고
    • Refining homology models by combining replica-exchange molecular dynamics and statistical potentials
    • Zhu, J., Fan, H., Periole, X., Honig, B. & Mark, A. E. Refining homology models by combining replica-exchange molecular dynamics and statistical potentials. Proteins 72, 1171-1188, doi: 10.1002/prot.22005 (2008
    • (2008) Proteins , vol.72 , pp. 1171-1188
    • Zhu, J.1    Fan, H.2    Periole, X.3    Honig, B.4    Mark, A.E.5
  • 57
    • 84906330457 scopus 로고    scopus 로고
    • Fine mapping of murine antibody responses to immunization with a novel soluble form of hepatitis c virus envelope glycoprotein complex
    • Ruwona, T. B., Giang, E., Nieusma, T. & Law, M. Fine mapping of murine antibody responses to immunization with a novel soluble form of hepatitis C virus envelope glycoprotein complex. J. Virol. 88, 10459-10471, doi: 10.1128/jvi.01584-14 (2014
    • (2014) J. Virol , vol.88 , pp. 10459-10471
    • Ruwona, T.B.1    Giang, E.2    Nieusma, T.3    Law, M.4
  • 58
    • 33644842641 scopus 로고    scopus 로고
    • Structural insight into interactions between dihydrolipoamide dehydrogenase (e3) and e3 binding protein of human pyruvate dehydrogenase complex
    • Brautigam, C. A., et al. Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex. Structure 14, 611-621, doi: 10.1016/j.str.2006.01.001 (2006
    • (2006) Structure , vol.14 , pp. 611-621
    • Brautigam, C.A.1
  • 59
    • 27644557445 scopus 로고    scopus 로고
    • Structural insights into the roles of water and the 2? Hydroxyl of the p site trna in the peptidyl transferase reaction
    • Schmeing, T. M., Huang, K. S., Kitchen, D. E., Strobel, S. A. & Steitz, T. A. Structural insights into the roles of water and the 2? hydroxyl of the P site tRNA in the peptidyl transferase reaction. Mol. Cell 20, 437-448, doi: 10.1016/j.molcel.2005.09.006 (2005
    • (2005) Mol. Cell , vol.20 , pp. 437-448
    • Schmeing, T.M.1    Huang, K.S.2    Kitchen, D.E.3    Strobel, S.A.4    Steitz, T.A.5
  • 60
    • 0142242265 scopus 로고    scopus 로고
    • Cell entry of hepatitis c virus requires a set of co-receptors that include the cd81 tetraspanin and the sr-b1 scavenger receptor
    • Bartosch, B., et al. Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor. J. Biol. Chem. 278, 41624-41630, doi: 10.1074/jbc.M305289200 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 41624-41630
    • Bartosch, B.1
  • 61
    • 84869085954 scopus 로고    scopus 로고
    • Interdomain allostery promotes assembly of the poly(a) mrna complex with pabp and eif4g
    • Safaee, N., et al. Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. Mol. Cell 48, 375-386, doi: 10.1016/j.molcel.2012.09.001 (2012
    • (2012) Mol. Cell , vol.48 , pp. 375-386
    • Safaee, N.1
  • 62
    • 33748794562 scopus 로고    scopus 로고
    • Virus-like particles: Passport to immune recognition
    • Grgacic, E. V. L. & Anderson, D. A. Virus-like particles: Passport to immune recognition. Methods 40, 60-65, doi: 10.1016/j. ymeth.2006.07.018 (2006
    • (2006) Methods , vol.40 , pp. 60-65
    • Grgacic, E.V.L.1    Anderson, D.A.2
  • 63
    • 37549006787 scopus 로고    scopus 로고
    • Virus-like particles-universal molecular toolboxes
    • Ludwig, C. & Wagner, R. Virus-like particles-universal molecular toolboxes. Curr. Opin. Biotechnol. 18, 537-545, doi: 10.1016/j. copbio.2007.10.013 (2007
    • (2007) Curr. Opin. Biotechnol , vol.18 , pp. 537-545
    • Ludwig, C.1    Wagner, R.2
  • 64
    • 45749103230 scopus 로고    scopus 로고
    • Coming of age of virus-like particle vaccines
    • Jennings, G. T. & Bachmann, M. F. Coming of age of virus-like particle vaccines. Biol. Chem. 389, 521-536, doi: 10.1515/bc.2008.064 (2008
    • (2008) Biol. Chem , vol.389 , pp. 521-536
    • Jennings, G.T.1    Bachmann, M.F.2
  • 65
    • 84887620206 scopus 로고    scopus 로고
    • Virus-like particles: The future of microbial factories and cell-free systems as platforms for vaccine development
    • Rodriguez-Limas, W. A., Sekar, K. & Tyo, K. E. J. Virus-like particles: the future of microbial factories and cell-free systems as platforms for vaccine development. Curr. Opin. Biotechnol. 24, 1089-1093, doi: 10.1016/j.copbio.2013.02.008 (2013
    • (2013) Curr. Opin. Biotechnol , vol.24 , pp. 1089-1093
    • Rodriguez-Limas, W.A.1    Sekar, K.2    Tyo, K.E.J.3
  • 66
    • 0020071393 scopus 로고
    • Specific cellular stimulation in the primary immune response: Experimental test of a quantized model
    • Dintzis, R. Z., Vogelstein, B. & Dintzis, H. M. Specific cellular stimulation in the primary immune response: experimental test of a quantized model. Proc. Natl. Acad. Sci. USA 79, 884-888, doi: 10.1073/pnas.79.3.884 (1982
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 884-888
    • Dintzis, R.Z.1    Vogelstein, B.2    Dintzis, H.M.3
  • 67
    • 84877609579 scopus 로고    scopus 로고
    • Rational HIV immunogen design to target specific germline b cell receptors
    • Jardine, J., et al. Rational HIV immunogen design to target specific germline B cell receptors. Science 340, 711-716, doi: 10.1126/science.1234150 (2013
    • (2013) Science , vol.340 , pp. 711-716
    • Jardine, J.1
  • 68
    • 84879882264 scopus 로고    scopus 로고
    • Self-Assembling influenza nanoparticle vaccines elicit broadly neutralizing h1n1 antibodies
    • Kanekiyo, M., et al. Self-Assembling influenza nanoparticle vaccines elicit broadly neutralizing H1N1 antibodies. Nature 499, 102-106, doi: 10.1038/nature12202 (2013
    • (2013) Nature , vol.499 , pp. 102-106
    • Kanekiyo, M.1
  • 69
    • 77953543379 scopus 로고    scopus 로고
    • Rational antibody-based HIV-1 vaccine design: Current approaches and future directions
    • Walker, L. M. & Burton, D. R. Rational antibody-based HIV-1 vaccine design: current approaches and future directions. Curr. Opin. Immunol. 22, 358-366 (2010
    • (2010) Curr. Opin. Immunol , vol.22 , pp. 358-366
    • Walker, L.M.1    Burton, D.R.2
  • 70
    • 33645028340 scopus 로고    scopus 로고
    • The cyclotides and related macrocyclic peptides as scaffolds in drug design
    • Craik, D. J., Cemazar, M. & Daly, N. L. The cyclotides and related macrocyclic peptides as scaffolds in drug design. Curr. Opin. Drug Discovery Dev. 9, 251-260 (2006
    • (2006) Curr. Opin. Drug Discovery Dev , vol.9 , pp. 251-260
    • Craik, D.J.1    Cemazar, M.2    Daly, N.L.3
  • 71
    • 0036489968 scopus 로고    scopus 로고
    • The cyclotides: Novel macrocyclic peptides as scaffolds in drug design
    • Craik, D. J., Simonsen, S. & Daly, N. L. The cyclotides: Novel macrocyclic peptides as scaffolds in drug design. Curr. Opin. Drug Discovery Dev. 5, 251-260 (2002
    • (2002) Curr. Opin. Drug Discovery Dev , vol.5 , pp. 251-260
    • Craik, D.J.1    Simonsen, S.2    Daly, N.L.3
  • 73
    • 48149098354 scopus 로고    scopus 로고
    • A new generation of protein therapeutics
    • Stumpp, M. T., Binz, H. K. & Amstutz, P. DARPins: A new generation of protein therapeutics. Drug Discovery Today 13, 695-701, doi: 10.1016/j.drudis.2008.04.013 (2008
    • (2008) Drug Discovery Today , vol.13 , pp. 695-701
    • Stumpp, M.T.1    Binz, H.K.2    Darpins, A.P.3
  • 74
    • 79956017135 scopus 로고    scopus 로고
    • Computational design of proteins targeting the conserved stem region of influenza hemagglutinin
    • Fleishman, S. J., et al. Computational design of proteins targeting the conserved stem region of influenza hemagglutinin. Science 332, 816-821, doi: 10.1126/science.1202617 (2011
    • (2011) Science , vol.332 , pp. 816-821
    • Fleishman, S.J.1
  • 75
    • 0038386050 scopus 로고    scopus 로고
    • 3d-jury: A simple approach to improve protein structure predictions
    • Ginalski, K., Elofsson, A., Fischer, D. & Rychlewski, L. 3D-Jury: a simple approach to improve protein structure predictions. Bioinformatics 19, 1015-1018, doi: 10.1093/bioinformatics/btg124 (2003
    • (2003) Bioinformatics , vol.19 , pp. 1015-1018
    • Ginalski, K.1    Elofsson, A.2    Fischer, D.3    Rychlewski, L.4
  • 76
    • 0037624841 scopus 로고    scopus 로고
    • 3d-shotgun: A novel, cooperative, fold-recognition meta-predictor
    • Fischer, D. 3D-SHOTGUN: A novel, cooperative, fold-recognition meta-predictor. Proteins 51, 434-441, doi: 10.1002/prot.10357 (2003
    • (2003) Proteins , vol.51 , pp. 434-441
    • Fischer, D.1
  • 77
    • 84892785219 scopus 로고    scopus 로고
    • Bioengineering virus-like particles as vaccines
    • Lua, L. H. L., et al. Bioengineering virus-like particles as vaccines. Biotechnol. Bioeng. 111, 425-440, doi: 10.1002/bit.25159 (2014
    • (2014) Biotechnol. Bioeng , vol.111 , pp. 425-440
    • Lua, L.H.L.1
  • 78
    • 79960011784 scopus 로고    scopus 로고
    • Structural model of the trpp2/pkd1 c-Terminal coiled-coil complex produced by a combined computational and experimental approach
    • Zhu, J., et al. Structural model of the TRPP2/PKD1 C-Terminal coiled-coil complex produced by a combined computational and experimental approach. Proc. Natl. Acad. Sci. USA 108, 10133-10138, doi: 10.1073/pnas.1017669108 (2011
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 10133-10138
    • Zhu, J.1
  • 79
    • 38549154569 scopus 로고    scopus 로고
    • Loop modeling: Sampling, filtering, and scoring
    • Soto, C. S., Fasnacht, M., Zhu, J., Forrest, L. & Honig, B. Loop modeling: Sampling, filtering, and scoring. Proteins 70, 834-843, doi: 10.1002/prot.21612 (2008
    • (2008) Proteins , vol.70 , pp. 834-843
    • Soto, C.S.1    Fasnacht, M.2    Zhu, J.3    Forrest, L.4    Honig, B.5
  • 80
    • 33749037718 scopus 로고    scopus 로고
    • Structural refinement of protein segments containing secondary structure elements: Local sampling, knowledge-based potentials, and clustering
    • Zhu, J., Xie, L. & Honig, B. Structural refinement of protein segments containing secondary structure elements: Local sampling, knowledge-based potentials, and clustering. Proteins 65, 463-479, doi: 10.1002/prot.21085 (2006
    • (2006) Proteins , vol.65 , pp. 463-479
    • Zhu, J.1    Xie, L.2    Honig, B.3
  • 81
    • 77649336168 scopus 로고    scopus 로고
    • Building and refining protein models within cryo-electron microscopy density maps based on homology modeling and multiscale structure refinement
    • Zhu, J., Cheng, L., Fang, Q., Zhou, Z. H. & Honig, B. Building and refining protein models within cryo-electron microscopy density maps based on homology modeling and multiscale structure refinement. J. Mol. Biol. 397, 835-851, doi: 10.1016/j. jmb.2010.01.041 (2010
    • (2010) J. Mol. Biol , vol.397 , pp. 835-851
    • Zhu, J.1    Cheng, L.2    Fang, Q.3    Zhou, Z.H.4    Honig, B.5
  • 82
    • 0035838974 scopus 로고    scopus 로고
    • Extending the accuracy limits of prediction for side-chain conformations
    • Xiang, Z. X. & Honig, B. Extending the accuracy limits of prediction for side-chain conformations. J. Mol. Biol. 311, 421-430, doi: 10.1006/jmbi.2001.4865 (2001
    • (2001) J. Mol. Biol , vol.311 , pp. 421-430
    • Xiang, Z.X.1    Honig, B.2
  • 83
    • 0036643430 scopus 로고    scopus 로고
    • Fast and accurate side-chain topology and energy refinement (faster) as a new method for protein structure optimization
    • Desmet, J., Spriet, J. & Lasters, I. Fast and Accurate Side-Chain Topology and Energy Refinement (FASTER) as a new method for protein structure optimization. Proteins 48, 31-43, doi: 10.1002/prot.10131 (2002
    • (2002) Proteins , vol.48 , pp. 31-43
    • Desmet, J.1    Spriet, J.2    Lasters, I.3
  • 84
    • 84988112508 scopus 로고
    • An efficient Newton-like method for molecular mechanics energy minimization of large molecules
    • Ponder, J. W. & Richards, F. M. An efficient Newton-like method for molecular mechanics energy minimization of large molecules. J. Comput. Chem. 8, 1016-1024, doi: 10.1002/jcc.540080710 (1987
    • (1987) J. Comput. Chem , vol.8 , pp. 1016-1024
    • Ponder, J.W.1    Richards, F.M.2
  • 85
    • 33645941402 scopus 로고
    • The opls [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen, W. L. & Tiradorives, J. The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin. J. Am. Chem. Soc. 110, 1657-1666, doi: 10.1021/ja00214a001 (1988
    • (1988) J. Am. Chem. Soc , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tiradorives, J.2
  • 86
    • 0029633168 scopus 로고
    • Gromacs a message-passing parallel molecular dynamics implementation
    • Berendsen, H. J. C., Vanderspoel, D. & Vandrunen, R. GROMACS: A message-passing parallel molecular dynamics implementation. Comput. Phys. Commun. 91, 43-56, doi: 10.1016/0010-4655(95)00042-e (1995
    • (1995) Comput. Phys. Commun , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    Vanderspoel, D.2    Vandrunen, R.3
  • 87
    • 0035789518 scopus 로고    scopus 로고
    • Gromacs 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., Hess, B. & van der Spoel, D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7, 306-317, doi: 10.1007/s008940100045 (2001
    • (2001) J. Mol. Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 88
    • 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, doi: 10.1063/1.470117 (1995
    • (1995) J. Chem. Phys , vol.103 , pp. 8577-8593
    • Essmann, U.1
  • 89
    • 0000388705 scopus 로고    scopus 로고
    • Lincs a linear constraint solver for molecular simulations
    • Hess, B., Bekker, H., Berendsen, H. J. C. & Fraaije, J. LINCS: A linear constraint solver for molecular simulations. J. Comput. Chem. 18, 1463-1472, doi: 10.1002/(sici)1096-987x(199709)18: 12 3.0.co; 2-h (1997
    • (1997) J. Comput. Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.4
  • 90
    • 84986440341 scopus 로고
    • Settle: An analytical version of the shake and rattle algorithm for rigid water models
    • Miyamoto, S. & Kollman, P. A. Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models. J. Comput. Chem. 13, 952-962, doi: 10.1002/jcc.540130805 (1992
    • (1992) J. Comput. Chem , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.