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Volumn 423, Issue 1, 2012, Pages 63-78

Structures of hepatitis b virus cores presenting a model epitope and their complexes with antibodies

Author keywords

cryomicroscopy; image processing; improved immunogenicity; vaccine carriers; virus like particles

Indexed keywords

CORE PROTEIN; EPITOPE; HEPATITIS B SURFACE ANTIGEN; HEPATITIS B VACCINE; VIRUS DNA;

EID: 84866319710     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.06.032     Document Type: Article
Times cited : (25)

References (56)
  • 1
    • 0034889864 scopus 로고    scopus 로고
    • HBV core particles as a carrier for B cell/T cell epitopes
    • DOI 10.1159/000050037
    • P. Pumpens, and E. Grens HBV core particles as a carrier for B cell/T cell epitopes Intervirology 44 2001 98 114 (Pubitemid 32757388)
    • (2001) Intervirology , vol.44 , Issue.2-3 , pp. 98-114
    • Pumpens, P.1    Grens, E.2
  • 2
    • 70649089583 scopus 로고    scopus 로고
    • Construction of novel vaccines on the basis of the virus-like particles: Hepatitis B virus proteins as vaccine carriers
    • Y. Khudyakov, CRC Press, Taylor & Francis Group Boca Raton London, New York
    • P. Pumpens, R. Ulrich, K. Sasnauskas, A. Kazaks, V. Ose, and E. Grens Construction of novel vaccines on the basis of the virus-like particles: hepatitis B virus proteins as vaccine carriers Y. Khudyakov, Medicinal Protein Engineering 2008 CRC Press, Taylor & Francis Group Boca Raton London, New York 205 248
    • (2008) Medicinal Protein Engineering , pp. 205-248
    • Pumpens, P.1    Ulrich, R.2    Sasnauskas, K.3    Kazaks, A.4    Ose, V.5    Grens, E.6
  • 3
    • 70449337697 scopus 로고    scopus 로고
    • Use of hepadnavirus core proteins as vaccine platforms
    • D.C. Whitacre, B.O. Lee, and D.R. Milich Use of hepadnavirus core proteins as vaccine platforms Expert Rev. Vaccines 8 2009 1565 1573
    • (2009) Expert Rev. Vaccines , vol.8 , pp. 1565-1573
    • Whitacre, D.C.1    Lee, B.O.2    Milich, D.R.3
  • 4
    • 0023546339 scopus 로고
    • Improved immunogenicity of a peptide epitope after fusion to hepatitis B core protein
    • B.E. Clarke, S.E. Newton, A.R. Carroll, M.J. Francis, G. Appleyard, and A.D. Syred Improved immunogenicity of a peptide epitope after fusion to hepatitis B core protein Nature 330 1987 381 384
    • (1987) Nature , vol.330 , pp. 381-384
    • Clarke, B.E.1    Newton, S.E.2    Carroll, A.R.3    Francis, M.J.4    Appleyard, G.5    Syred, A.D.6
  • 5
    • 0035852348 scopus 로고    scopus 로고
    • Conversion of poorly immunogenic malaria repeat sequences into a highly immunogenic vaccine candidate
    • DOI 10.1016/S0264-410X(01)00400-5, PII S0264410X01004005
    • D.R. Milich, J. Hughes, J. Jones, M. Sällberg, and T.R. Phillips Conversion of poorly immunogenic malaria repeat sequences into a highly immunogenic vaccine candidate Vaccine 20 2002 771 788 (Pubitemid 34015817)
    • (2001) Vaccine , vol.20 , Issue.5-6 , pp. 771-788
    • Milich, D.R.1    Hughes, J.2    Jones, J.3    Sallberg, M.4    Phillips, T.R.5
  • 7
    • 45249093689 scopus 로고    scopus 로고
    • Phase I trial of an Alhydrogel adjuvanted hepatitis B core virus-like particle containing epitopes of Plasmodium falciparum circumsporozoite protein
    • DOI 10.1371/journal.pone.0001556
    • A.L. Gregson, G. Oliveira, C. Othoro, J.M. Calvo-Calle, G.B. Thorton, E. Nardin, and R. Edelman Phase I trial of an alhydrogel adjuvanted hepatitis B core virus-like particle containing epitopes of Plasmodium falciparum circumsporozoite protein PLoS One 3 2008 e1556 10.1371/journal.pone.0001556 (Pubitemid 351836831)
    • (2008) PLoS ONE , vol.3 , Issue.2
    • Gregson, A.L.1    Oliveira, G.2    Othoro, C.3    Calvo-Calle, J.M.4    Thorton, G.B.5    Nardin, E.6    Edelman, R.7
  • 8
    • 19444368726 scopus 로고    scopus 로고
    • Universal influenza A vaccine: Optimization of M2-based constructs
    • DOI 10.1016/j.virol.2005.04.004, PII S0042682205002114
    • M. De Filette, W.M. Jou, A. Birkett, K. Lyons, B. Schultz, and A. Tonkyro Universal influenza A vaccine: optimization of M2-based constructs Virology 337 2005 149 161 (Pubitemid 40725448)
    • (2005) Virology , vol.337 , Issue.1 , pp. 149-161
    • De Filette, M.1    Jou, W.M.2    Birkett, A.3    Lyons, K.4    Schultz, B.5    Tonkyro, A.6    Resch, S.7    Fiers, W.8
  • 9
    • 14744292190 scopus 로고    scopus 로고
    • A fusion product of the complete Borrelia burgdorferi outer surface protein A (OspA) and the hepatitis B virus capsid protein is highly immunogenic and induces protective immunity similar to that seen with an effective lipidated OspA vaccine formula
    • DOI 10.1002/eji.200425449
    • M. Nassal, C. Skamel, P.A. Kratz, R. Wallich, T. Stehle, and M.M. Simon A fusion product of the complete Borrelia burgdorferi outer surface protein A (OspA) and the hepatitis B virus capsid protein is highly immunogenic and induces protective immunity similar to that seen with an effective lipidated OspA vaccine formula Eur. J. Immunol. 35 2005 655 665 (Pubitemid 40331342)
    • (2005) European Journal of Immunology , vol.35 , Issue.2 , pp. 655-665
    • Nassal, M.1    Skamel, C.2    Kratz, P.A.3    Wallich, R.4    Stehle, T.5    Simon, M.M.6
  • 10
    • 0344875095 scopus 로고    scopus 로고
    • The nucleocapsid of the hepatitis B virus: A remarkable immunogenic structure
    • DOI 10.1016/j.antiviral.2003.08.011
    • P. Vanlandschoot, T. Cao, and G. Leroux-Roels The nucleocapsid of the hepatitis B virus: a remarkable immunogenic structure Antiviral Res. 60 2003 67 74 (Pubitemid 37452448)
    • (2003) Antiviral Research , vol.60 , Issue.2 , pp. 67-74
    • Vanlandschoot, P.1    Cao, T.2    Leroux-Roels, G.3
  • 11
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy
    • DOI 10.1016/0092-8674(94)90142-2
    • R.A. Crowther, N.A. Kiselev, B. Böttcher, J.A. Berriman, G.P. Borisova, V. Ose, and P. Pumpens Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy Cell 77 1994 943 950 (Pubitemid 24187691)
    • (1994) Cell , vol.77 , Issue.6 , pp. 943-950
    • Crowther, R.A.1    Kiselev, N.A.2    Bottcher, B.3    Berriman, J.A.4    Borisova, G.P.5    Ose, V.6    Pumpens, P.7
  • 13
    • 0023705210 scopus 로고
    • Genetically engineered mutants of the core antigen of the human hepatitis B virus preserving the ability for native self-assembly [Article in Russian]
    • G.P. Borisova, J.V. Kalis, P.M. Pushko, V.V. Tsibinogin, V.J. Loseva, and V.P. Ose Genetically engineered mutants of the core antigen of the human hepatitis B virus preserving the ability for native self-assembly [Article in Russian] Dokl. Akad. Nauk SSSR. 298 1988 1474 1478
    • (1988) Dokl. Akad. Nauk SSSR. , vol.298 , pp. 1474-1478
    • Borisova, G.P.1    Kalis, J.V.2    Pushko, P.M.3    Tsibinogin, V.V.4    Loseva, V.J.5    Ose, V.P.6
  • 14
    • 0024474088 scopus 로고
    • A recombination hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids
    • A. Gallina, F. Bonelli, L. Zentilin, G. Rindi, M. Muttini, and G. Milanesi A recombinant hepatitis-B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids J. Virol. 63 1989 4645 4652 (Pubitemid 19257839)
    • (1989) Journal of Virology , vol.63 , Issue.11 , pp. 4645-4652
    • Gallina, A.1    Bonelli, F.2    Zentilin, L.3    Rindi, G.4    Muttini, M.5    Milanesi, G.6
  • 15
    • 0025316017 scopus 로고
    • Hepatitis B virus nucleocapsid assembly: Primary structure requirements in the core protein
    • F. Birnbaum, and M. Nassal Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein J. Virol. 64 1990 3319 3330 (Pubitemid 20219537)
    • (1990) Journal of Virology , vol.64 , Issue.7 , pp. 3319-3330
    • Birnbaum, F.1    Nassal, M.2
  • 16
    • 0029950758 scopus 로고    scopus 로고
    • Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein
    • A. Zlotnick, N. Cheng, J.F. Conway, F.P. Booy, A.C. Steven, S.J. Stahl, and P.T. Wingfield Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein Biochemistry 35 1996 7412 7421
    • (1996) Biochemistry , vol.35 , pp. 7412-7421
    • Zlotnick, A.1    Cheng, N.2    Conway, J.F.3    Booy, F.P.4    Steven, A.C.5    Stahl, S.J.6    Wingfield, P.T.7
  • 17
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • DOI 10.1038/386088a0
    • B. Böttcher, S.A. Wynne, and R.A. Crowther Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy Nature 386 1997 88 91 (Pubitemid 27130926)
    • (1997) Nature , vol.386 , Issue.6620 , pp. 88-91
    • Bottcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 18
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • DOI 10.1016/S1097-2765(01)80009-5
    • S.A. Wynne, R.A. Crowther, and A.G.W. Leslie The crystal structure of the human hepatitis B virus capsid Mol. Cell 3 1999 771 780 (Pubitemid 29323055)
    • (1999) Molecular Cell , vol.3 , Issue.6 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.W.3
  • 19
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • DOI 10.1038/386091a0
    • J.F. Conway, N. Cheng, A. Zlotnick, P.T. Wingfield, S.J. Stahl, and A.C. Steven Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy Nature 386 1997 91 94 (Pubitemid 27130927)
    • (1997) Nature , vol.386 , Issue.6620 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 23
    • 0025887285 scopus 로고
    • Foreign epitopes in immunodominant regions of hepatitis B core particles are highly immunogenic and conformationally restricted
    • A.L. Brown, M.J. Francis, G.Z. Hastings, N.R. Parry, P.V. Barnett, D.J. Rowlands, and B.E. Clarke Foreign epitopes in immunodominant regions of hepatitis B core particles are highly immunogenic and conformationally restricted Vaccine 9 1991 595 601
    • (1991) Vaccine , vol.9 , pp. 595-601
    • Brown, A.L.1    Francis, M.J.2    Hastings, G.Z.3    Parry, N.R.4    Barnett, P.V.5    Rowlands, D.J.6    Clarke, B.E.7
  • 24
    • 0032568864 scopus 로고    scopus 로고
    • Hepatitis B virus capsid: Localization of the putative immunodominant loop (residues 78 to 83) on the capsid surface, and implications for the distinction between c and e-antigens
    • DOI 10.1006/jmbi.1998.1845
    • J.F. Conway, N. Cheng, A. Zlotnick, S.J. Stahl, P.T. Wingfield, and D.M. Belnap Hepatitis B virus capsid: Localization of the putative immunodominant loop (residues 78 to 83) on the capsid surface, and implications for the distinction between c and e-antigens J. Mol. Biol. 279 1998 1111 1121 (Pubitemid 28302388)
    • (1998) Journal of Molecular Biology , vol.279 , Issue.5 , pp. 1111-1121
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Stahl, S.J.4    Wingfield, P.T.5    Belnap, D.M.6    Kanngiesser, U.7    Noah, M.8    Steven, A.C.9
  • 25
    • 0037688298 scopus 로고    scopus 로고
    • Characterization of a conformational epitope on hepatitis B virus core antigen and quasiequivalent variations in antibody binding
    • DOI 10.1128/JVI.77.11.6466-6473.2003
    • J.F. Conway, N.R. Watts, D.M. Belnap, N. Cheng, S.J. Stahl, P.T. Wingfield, and A.C. Steven Characterization of a conformational epitope on hepatitis B virus core antigen and quasiequivalent variations in antibody binding J. Virol. 77 2003 6466 6473 (Pubitemid 36588416)
    • (2003) Journal of Virology , vol.77 , Issue.11 , pp. 6466-6473
    • Conway, J.F.1    Watts, N.R.2    Belnap, D.M.3    Cheng, N.4    Stahl, S.J.5    Wingfield, P.T.6    Steven, A.C.7
  • 28
    • 0026663304 scopus 로고
    • Determination of the minimal length of preS1 epitope recognized by a monoclonal antibody which inhibits attachment of hepatitis B virus to hepatocytes
    • I. Sominskaya, P. Pushko, D. Dreilina, T. Kozlovskaya, and P. Pumpen Determination of the minimal length of preS1 epitope recognized by a monoclonal antibody which inhibits attachment of hepatitis B virus to hepatocytes Med. Microbiol. Immunol. 181 1992 215 226
    • (1992) Med. Microbiol. Immunol. , vol.181 , pp. 215-226
    • Sominskaya, I.1    Pushko, P.2    Dreilina, D.3    Kozlovskaya, T.4    Pumpen, P.5
  • 30
    • 0021710644 scopus 로고
    • Large surface proteins of hepatitis B virus containing the pre-s sequence
    • K.H. Heermann, U. Goldmann, W. Schwartz, T. Seyffarth, H. Baumgarten, and W.H. Gerlich Large surface proteins of hepatitis B virus containing the pre-S sequence J. Virol. 52 1984 396 402 (Pubitemid 15202474)
    • (1984) Journal of Virology , vol.52 , Issue.2 , pp. 396-402
    • Heermann, K.H.1    Goldmann, U.2    Schwartz, W.3
  • 31
    • 0028908286 scopus 로고
    • Screening a monoclonal antibody with a fusion-phage display library shows a discontinuity in a linear epitope within PreS1 of hepatitis B virus
    • V. Germaschewski, and K. Murray Screening a monoclonal antibody with a fusion-phage display library shows a discontinuity in a linear epitope within PreS1 of hepatitis B virus J. Med. Virol. 45 1995 300 305
    • (1995) J. Med. Virol. , vol.45 , pp. 300-305
    • Germaschewski, V.1    Murray, K.2
  • 32
    • 0024814254 scopus 로고
    • Identification of an attachment site for human liver plasma membranes on hepatitis B virus particles
    • DOI 10.1016/0042-6822(89)90564-3
    • P. Pontisso, M.G. Ruvoletto, W.H. Gerlich, K.H. Heermann, R. Bardini, and A. Alberti Identification of an attachment site for human liver plasma membranes on hepatitis B virus particles Virology 173 1989 522 530 (Pubitemid 20014479)
    • (1989) Virology , vol.173 , Issue.2 , pp. 522-530
    • Pontisso, P.1    Ruvoletto, M.G.2    Gerlich, W.H.3    Heermann, K.-H.4    Bardini, R.5    Alberti, A.6
  • 33
    • 0042389550 scopus 로고    scopus 로고
    • Pre-S1 antigen-dependent infection of Tupaia hepatocyte cultures with human hepatitis B virus
    • DOI 10.1128/JVI.77.17.9511-9521.2003
    • D. Glebe, M. Aliakbari, P. Krass, E.V. Knoop, K.P. Valerius, and W.H. Gerlich Pre-s1 antigen-dependent infection of Tupaia hepatocyte cultures with human hepatitis B virus J. Virol. 77 2003 9511 9521 (Pubitemid 37011046)
    • (2003) Journal of Virology , vol.77 , Issue.17 , pp. 9511-9521
    • Glebe, D.1    Aliakbari, M.2    Krass, P.3    Knoop, E.V.4    Valerius, K.P.5    Gerlich, W.H.6
  • 34
    • 31344442517 scopus 로고    scopus 로고
    • High plasticity of the hepatitis B virus capsid revealed by conformational stress
    • DOI 10.1016/j.jmb.2005.11.053, PII S0022283605014579
    • B. Böttcher, M. Vogel, M. Ploss, and M. Nassal High plasticity of the hepatitis B virus capsid revealed by conformational stress J. Mol. Biol. 356 2006 812 822 (Pubitemid 43139340)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.3 , pp. 812-822
    • Bottcher, B.1    Vogel, M.2    Ploss, M.3    Nassal, M.4
  • 35
    • 34748861981 scopus 로고    scopus 로고
    • Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus
    • DOI 10.1110/ps.072983507
    • S.W. Chi, D.H. Kim, S.H. Lee, I. Chang, and K.H. Han Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus Protein Sci. 16 2007 2108 2117 (Pubitemid 47481646)
    • (2007) Protein Science , vol.16 , Issue.10 , pp. 2108-2117
    • Chi, S.-W.1    Kim, D.-H.2    Lee, S.I.-H.3    Chang, I.4    Han, K.-H.5
  • 36
    • 0027408022 scopus 로고
    • Epitopes recognized by antibodies to denatured core protein of hepatitis B virus
    • V. Bichko, F. Schödel, M. Nassal, E. Gren, I. Berzinsh, and G. Borisova Epitopes recognized by antibodies to denatured core protein of hepatitis B virus Mol. Immunol. 30 1993 221 231
    • (1993) Mol. Immunol. , vol.30 , pp. 221-231
    • Bichko, V.1    Schödel, F.2    Nassal, M.3    Gren, E.4    Berzinsh, I.5    Borisova, G.6
  • 37
    • 0027264854 scopus 로고
    • The structure of the variable regions of mouse monoclonal antibodies to hepatitis B virus core antigen
    • V. Skrivelis, Y. Steinberg, V. Bichko, E. Gren, and A. Tsimanis The structure of the variable regions of mouse monoclonal antibodies to hepatitis B virus core antigen Scand. J. Immunol. 37 1993 637 643 (Pubitemid 23181485)
    • (1993) Scandinavian Journal of Immunology , vol.37 , Issue.6 , pp. 637-643
    • Skrivelis, V.1    Steinberg, Y.2    Bichko, V.3    Gren, E.4    Tsimanis, A.5
  • 38
    • 0028142830 scopus 로고
    • Identification of hepatitis B virus core protein regions exposed or internalized at the surface of HBcAg particles by scanning with monoclonal antibodies
    • DOI 10.1006/viro.1994.1413
    • P. Pushko, M. Sallberg, G. Borisova, U. Ruden, V. Bichko, and B. Wahren Identification of hepatitis B virus core protein regions exposed or internalized at the surface of HBcAg particles by scanning with monoclonal antibodies Virology 202 1994 912 920 (Pubitemid 24254905)
    • (1994) Virology , vol.202 , Issue.2 , pp. 912-920
    • Pushko, P.1    Sallberg, M.2    Borisova, G.3    Ruden, U.4    Bichko, V.5    Wahren, B.6    Pumpens, P.7    Magnius, L.8
  • 39
    • 0036889348 scopus 로고    scopus 로고
    • An antibody to the putative aphid recognition site on cucumber mosaic virus recognizes pentons but not hexons
    • DOI 10.1128/JVI.76.23.12250-12258.2002
    • V.D. Bowman, E.S. Chase, A.W.E. Franz, P.R. Chipman, X. Zhang, and K.L. Perry An antibody to the putative aphid recognition site on cucumber mosaic virus recognizes pentons but not hexons J. Virol. 76 2002 12250 12258 (Pubitemid 35304322)
    • (2002) Journal of Virology , vol.76 , Issue.23 , pp. 12250-12258
    • Bowman, V.D.1    Chase, E.S.2    Franz, A.W.E.3    Chipman, P.R.4    Zhang, X.5    Perry, K.L.6    Baker, T.S.7    Smith, T.J.8
  • 40
    • 0023710629 scopus 로고
    • Elbow motion in the immunoglobulins involves a molecular ball-and-socket joint
    • A.M. Lesk, and C. Chothia Elbow motion in the immunoglobulins involves a molecular ball-and-socket joint Nature 335 1988 188 190
    • (1988) Nature , vol.335 , pp. 188-190
    • Lesk, A.M.1    Chothia, C.2
  • 41
    • 0022996325 scopus 로고
    • The nucleocapsid of hepatitis B virus is both a T-cell-independent and a T-cell-dependent antigen
    • D.R. Milich, and A. McLachlan The nucleocapsid of hepatitis B virus is both a T-cell-independent and a T-cell-dependent antigen Science 234 1986 1398 1401 (Pubitemid 17210220)
    • (1986) Science , vol.234 , Issue.4782 , pp. 1398-1401
    • Milich, D.R.1    McLachlan, A.2
  • 43
    • 84860119495 scopus 로고    scopus 로고
    • SplitCore: An exceptionally versatile viral nanoparticle for native whole protein display regardless of 3D structure
    • 10.1038/srep00005
    • A. Walker, C. Skamel, and M. Nassal SplitCore: an exceptionally versatile viral nanoparticle for native whole protein display regardless of 3D structure Sci. Rep. 1 2011 5 10.1038/srep00005
    • (2011) Sci. Rep. , vol.1 , pp. 5
    • Walker, A.1    Skamel, C.2    Nassal, M.3
  • 44
    • 0033081676 scopus 로고    scopus 로고
    • Crystallization of hepatitis B virus core protein shells: Determination of cryoprotectant conditions and preliminary X-ray characterization
    • DOI 10.1107/S0907444998012621
    • S.A. Wynne, A.G.W. Leslie, P.J.G. Butler, and R.A. Crowther Crystallization of hepatitis B virus core protein shells: determination of cryoprotectant conditions and preliminary X-ray characterization Acta Crystallogr., Sect. D 55 1999 557 560 (Pubitemid 29083740)
    • (1999) Acta Crystallographica Section D: Biological Crystallography , vol.55 , Issue.2 , pp. 557-560
    • Wynne, S.A.1    Leslie, A.G.W.2    Butler, P.J.G.3    Crowther, R.A.4
  • 45
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Cold Spring Harbor, NY pp. 628-629
    • E. Harlow, and D. Lane Antibodies: A Laboratory Manual 1988 Cold Spring Harbor Laboratory Cold Spring Harbor, NY pp. 628-629
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 47
    • 83755192300 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • R.A. Crowther Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs Philos. Trans. R. Soc., B 363 1971 221 230
    • (1971) Philos. Trans. R. Soc., B , vol.363 , pp. 221-230
    • Crowther, R.A.1
  • 48
    • 0032815040 scopus 로고    scopus 로고
    • Ximdisp - A visualization tool to aid structure determination from electron microscope images
    • DOI 10.1006/jsbi.1998.4073
    • J.M. Smith Ximdisp - a visualization tool to aid structure determination from electron microscope images J. Struct. Biol. 125 1999 223 228 (Pubitemid 29402607)
    • (1999) Journal of Structural Biology , vol.125 , Issue.2-3 , pp. 223-228
    • Smith, J.M.1
  • 49
    • 0346816491 scopus 로고    scopus 로고
    • FindEM - A fast, efficient program for automatic selection of particles from electron micrographs
    • DOI 10.1016/j.jsb.2003.11.007
    • A.M. Roseman FindEM - a fast, efficient program for automatic selection of particles from electron micrographs J. Struct. Biol. 145 2004 91 99 (Pubitemid 38058471)
    • (2004) Journal of Structural Biology , vol.145 , Issue.1-2 , pp. 91-99
    • Roseman, A.M.1
  • 50
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • DOI 10.1006/jsbi.1996.0030
    • J. Frank, M. Radermacher, P. Penczek, J. Zhu, Y. Li, M. Ladjadj, and A. Leith SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields J. Struct. Biol. 116 1996 190 199 (Pubitemid 26093143)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 52
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • DOI 10.1016/j.jmb.2003.07.013
    • P.B. Rosenthal, and R. Henderson Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy J. Mol. Biol. 333 2003 721 745 (Pubitemid 37268015)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.4 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 53
    • 0033776245 scopus 로고    scopus 로고
    • Docking structures of domains into maps from cryo-electron microscopy using local correlation
    • A.M. Roseman Docking structures of domains into maps from cryo-electron microscopy using local correlation Acta Crystallogr., Sect. D 56 2000 1332 1340
    • (2000) Acta Crystallogr., Sect. D , vol.56 , pp. 1332-1340
    • Roseman, A.M.1
  • 54
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D , vol.50 , pp. 760-763
  • 55
    • 0034458999 scopus 로고    scopus 로고
    • WAM: An improved algorithm for modelling antibodies on the WEB
    • N.R.J. Whitelegg, and A.R. Rees WAM: an improved algorithm for modelling antibodies on the WEB Protein Eng. 12 2000 819 824 (Pubitemid 32233940)
    • (2000) Protein Engineering , vol.13 , Issue.12 , pp. 819-824
    • Whitelegg, N.R.J.1    Rees, A.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.