메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

A highly potent human antibody neutralizes dengue virus serotype 3 by binding across three surface proteins

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN; EPITOPE; HUMAN MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; VIRUS ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT; MEMBRANE PROTEIN; MONOCLONAL ANTIBODY; PROTEIN BINDING;

EID: 84923347933     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7341     Document Type: Article
Times cited : (174)

References (58)
  • 1
    • 84876804736 scopus 로고    scopus 로고
    • The global distribution and burden of dengue
    • Bhatt, S. et al. The global distribution and burden of dengue. Nature 496, 504-507 (2013).
    • (2013) Nature , vol.496 , pp. 504-507
    • Bhatt, S.1
  • 2
    • 80052496440 scopus 로고    scopus 로고
    • Critical issues in dengue vaccine development
    • Thomas, S. J. & Endy, T. P. Critical issues in dengue vaccine development. Curr. Opin. Infect. Dis. 24, 442-450 (2011).
    • (2011) Curr. Opin. Infect. Dis. , vol.24 , pp. 442-450
    • Thomas, S.J.1    Endy, T.P.2
  • 3
    • 84863825362 scopus 로고    scopus 로고
    • Dengue vectors and their spatial distribution
    • Higa, Y. Dengue vectors and their spatial distribution. Trop. Med. Health 39, 17-27 (2011).
    • (2011) Trop. Med. Health , vol.39 , pp. 17-27
    • Higa, Y.1
  • 4
    • 0037404062 scopus 로고    scopus 로고
    • The origin, emergence and evolutionary genetics of dengue virus
    • Holmes, E. & Twiddy, S. The origin, emergence and evolutionary genetics of dengue virus. Infect. Genet. Evol. 3, 19-28 (2003).
    • (2003) Infect. Genet. Evol. , vol.3 , pp. 19-28
    • Holmes, E.1    Twiddy, S.2
  • 5
    • 57149111281 scopus 로고    scopus 로고
    • The history and evolution of human dengue emergence
    • Vasilakis, N. & Weaver, S. C. The history and evolution of human dengue emergence. Adv. Virus Res. 72, 1-76 (2008).
    • (2008) Adv. Virus Res. , vol.72 , pp. 1-76
    • Vasilakis, N.1    Weaver, S.C.2
  • 7
    • 37549003979 scopus 로고    scopus 로고
    • Antibody to dengue 1 detected more than 60 years after infection
    • Imrie, A. et al. Antibody to dengue 1 detected more than 60 years after infection. Viral Immunol. 20, 672-675 (2007).
    • (2007) Viral Immunol. , vol.20 , pp. 672-675
    • Imrie, A.1
  • 8
    • 0642287817 scopus 로고    scopus 로고
    • Neutralization and antibody-dependent enhancement of dengue viruses
    • Halstead, S. B. Neutralization and antibody-dependent enhancement of dengue viruses. Adv. Virus Res. 60, 421-467 (2003).
    • (2003) Adv. Virus Res. , vol.60 , pp. 421-467
    • Halstead, S.B.1
  • 9
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion
    • Kuhn, R. J. et al. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108, 717-725 (2002).
    • (2002) Cell , vol.108 , pp. 717-725
    • Kuhn, R.J.1
  • 10
    • 84872048730 scopus 로고    scopus 로고
    • Cryo-EM structure of the mature dengue virus at 3.5-A resolution
    • Zhang, X. et al. Cryo-EM structure of the mature dengue virus at 3.5-A resolution. Nat. Struct. Mol. Biol. 20, 105-110 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 105-110
    • Zhang, X.1
  • 11
    • 84880368336 scopus 로고    scopus 로고
    • Immature and mature dengue serotype 1 virus structures provide insight into the maturation process
    • Kostyuchenko, V. A., Zhang, Q., Tan, J. L., Ng, T. S. & Lok, S. M. Immature and mature dengue serotype 1 virus structures provide insight into the maturation process. J. Virol. 87, 7700-7707 (2013).
    • (2013) J. Virol. , vol.87 , pp. 7700-7707
    • Kostyuchenko, V.A.1    Zhang, Q.2    Tan, J.L.3    Ng, T.S.4    Lok, S.M.5
  • 12
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis, Y., Ogata, S., Clements, D. & Harrison, S. C. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc. Natl Acad. Sci. USA 100, 6986-6991 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 13
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • Modis, Y., Ogata, S., Clements, D. & Harrison, S. C. Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J. Virol. 79, 1223-1231 (2005).
    • (2005) J. Virol. , vol.79 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 14
    • 4444338894 scopus 로고    scopus 로고
    • Conformational changes of the flavivirus e glycoprotein
    • Zhang, Y. et al. Conformational changes of the flavivirus E glycoprotein. Structure 12, 1607-1618 (2004).
    • (2004) Structure , vol.12 , pp. 1607-1618
    • Zhang, Y.1
  • 15
    • 33846496754 scopus 로고    scopus 로고
    • The envelope glycoprotein domain III of dengue virus serotypes 1 and 2 inhibit virus entry
    • Chin, J. F., Chu, J. J. & Ng, M. L. The envelope glycoprotein domain III of dengue virus serotypes 1 and 2 inhibit virus entry. Microbes Infect. 9, 1-6 (2007).
    • (2007) Microbes Infect. , vol.9 , pp. 1-6
    • Chin, J.F.1    Chu, J.J.2    Ng, M.L.3
  • 16
    • 84873849253 scopus 로고    scopus 로고
    • Structure of a dengue virus envelope protein late-stage fusion intermediate
    • Klein, D. E., Choi, J. L. & Harrison, S. C. Structure of a dengue virus envelope protein late-stage fusion intermediate. J. Virol. 87, 2287-2293 (2013).
    • (2013) J. Virol. , vol.87 , pp. 2287-2293
    • Klein, D.E.1    Choi, J.L.2    Harrison, S.C.3
  • 17
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis, Y., Ogata, S., Clements, D. & Harrison, S. C. Structure of the dengue virus envelope protein after membrane fusion. Nature 427, 313-319 (2004).
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 18
    • 1542466883 scopus 로고    scopus 로고
    • Antigenic structure of flavivirus proteins
    • Roehrig, J. T. Antigenic structure of flavivirus proteins. Adv. Virus Res. 59, 141-175 (2003).
    • (2003) Adv. Virus Res. , vol.59 , pp. 141-175
    • Roehrig, J.T.1
  • 19
    • 34548627957 scopus 로고    scopus 로고
    • Characterization of an antigenic site that contains a dominant, type-specific neutralization determinant on the envelope protein domain III (ED3) of dengue 2 virus
    • Gromowski, G. D. & Barrett, A. D. Characterization of an antigenic site that contains a dominant, type-specific neutralization determinant on the envelope protein domain III (ED3) of dengue 2 virus. Virology 366, 349-360 (2007).
    • (2007) Virology , vol.366 , pp. 349-360
    • Gromowski, G.D.1    Barrett, A.D.2
  • 20
    • 77954039828 scopus 로고    scopus 로고
    • The development of therapeutic antibodies that neutralize homologous and heterologous genotypes of dengue virus type 1
    • Shrestha, B. et al. The development of therapeutic antibodies that neutralize homologous and heterologous genotypes of dengue virus type 1. PLoS Pathog. 6, e1000823 (2010).
    • (2010) PLoS Pathog. , vol.6 , pp. e1000823
    • Shrestha, B.1
  • 21
    • 36348963709 scopus 로고    scopus 로고
    • Type- and subcomplex-specific neutralizing antibodies against domain III of dengue virus type 2 envelope protein recognize adjacent epitopes
    • Sukupolvi-Petty, S. et al. Type- and subcomplex-specific neutralizing antibodies against domain III of dengue virus type 2 envelope protein recognize adjacent epitopes. J. Virol. 81, 12816-12826 (2007).
    • (2007) J. Virol. , vol.81 , pp. 12816-12826
    • Sukupolvi-Petty, S.1
  • 22
    • 84860814270 scopus 로고    scopus 로고
    • Recombinant dengue type 2 viruses with altered e protein domain III epitopes are efficiently neutralized by human immune sera
    • Wahala, W. M., Huang, C., Butrapet, S., White, L. J. & de Silva, A. M. Recombinant dengue type 2 viruses with altered e protein domain III epitopes are efficiently neutralized by human immune sera. J. Virol. 86, 4019-4023 (2012).
    • (2012) J. Virol. , vol.86 , pp. 4019-4023
    • Wahala, W.M.1    Huang, C.2    Butrapet, S.3    White, L.J.4    De Silva, A.M.5
  • 23
    • 69249213373 scopus 로고    scopus 로고
    • Dengue virus neutralization by human immune sera: Role of envelope protein domain III-reactive antibody
    • Wahala, W. M., Kraus, A. A., Haymore, L. B., Accavitti-Loper, M. A. & de Silva, A. M. Dengue virus neutralization by human immune sera: role of envelope protein domain III-reactive antibody. Virology 392, 103-113 (2009).
    • (2009) Virology , vol.392 , pp. 103-113
    • Wahala, W.M.1    Kraus, A.A.2    Haymore, L.B.3    Accavitti-Loper, M.A.4    De Silva, A.M.5
  • 24
    • 84891619354 scopus 로고    scopus 로고
    • The potent and broadly neutralizing human dengue virusspecific monoclonal antibody 1C19 reveals a unique cross-reactive epitope on the bc loop of domain II of the envelope protein
    • Smith, S. A. et al. The potent and broadly neutralizing human dengue virusspecific monoclonal antibody 1C19 reveals a unique cross-reactive epitope on the bc loop of domain II of the envelope protein. MBio 4, e00873-13 (2013).
    • (2013) MBio , vol.4 , pp. e00873-e00913
    • Smith, S.A.1
  • 25
    • 84871962876 scopus 로고    scopus 로고
    • Mechanistic study of broadly neutralizing human monoclonal antibodies against dengue virus that target the fusion loop
    • Costin, J. M. et al. Mechanistic study of broadly neutralizing human monoclonal antibodies against dengue virus that target the fusion loop. J. Virol. 87, 52-66 (2013).
    • (2013) J. Virol. , vol.87 , pp. 52-66
    • Costin, J.M.1
  • 26
    • 84860826712 scopus 로고    scopus 로고
    • Identification of human neutralizing antibodies that bind to complex epitopes on dengue virions
    • de Alwis, R. et al. Identification of human neutralizing antibodies that bind to complex epitopes on dengue virions. Proc. Natl Acad. Sci. USA 109, 7439-7444 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 7439-7444
    • De Alwis, R.1
  • 27
    • 77956605864 scopus 로고    scopus 로고
    • The human immune response to Dengue virus is dominated by highly cross-reactive antibodies endowed with neutralizing and enhancing activity
    • Beltramello, M. et al. The human immune response to Dengue virus is dominated by highly cross-reactive antibodies endowed with neutralizing and enhancing activity. Cell Host Microbe 8, 271-283 (2010).
    • (2010) Cell Host Microbe , vol.8 , pp. 271-283
    • Beltramello, M.1
  • 28
    • 84907979176 scopus 로고    scopus 로고
    • Isolation of dengue virus-specific memory B cells with live virus antigen from human subjects following natural infection reveals the presence of diverse novel functional groups of antibody clones
    • Smith, S. A. et al. Isolation of dengue virus-specific memory B cells with live virus antigen from human subjects following natural infection reveals the presence of diverse novel functional groups of antibody clones. J. Virol. 88, 12233-12241 (2014).
    • (2014) J. Virol. , vol.88 , pp. 12233-12241
    • Smith, S.A.1
  • 29
    • 84862850400 scopus 로고    scopus 로고
    • The structural basis for serotype-specific neutralization of dengue virus by a human antibody
    • Teoh, E. P. et al. The structural basis for serotype-specific neutralization of dengue virus by a human antibody. Sci. Transl. Med. 4, 139ra83 (2012).
    • (2012) Sci. Transl. Med. , vol.4 , pp. 139ra83
    • Teoh, E.P.1
  • 30
    • 84863230437 scopus 로고    scopus 로고
    • Persistence of circulating memory B cell clones with potential for dengue virus disease enhancement for decades following infection
    • Smith, S. A. et al. Persistence of circulating memory B cell clones with potential for dengue virus disease enhancement for decades following infection. J. Virol. 86, 2665-2675 (2012).
    • (2012) J. Virol. , vol.86 , pp. 2665-2675
    • Smith, S.A.1
  • 31
    • 34249030028 scopus 로고    scopus 로고
    • Neutralization of animal virus infectivity by antibody
    • Reading, S. A. & Dimmock, N. J. Neutralization of animal virus infectivity by antibody. Arch. Virol. 152, 1047-1059 (2007).
    • (2007) Arch. Virol. , vol.152 , pp. 1047-1059
    • Reading, S.A.1    Dimmock, N.J.2
  • 32
    • 84880395430 scopus 로고    scopus 로고
    • Structural changes in dengue virus when exposed to a temperature of 37 degrees C
    • Fibriansah, G. et al. Structural changes in dengue virus when exposed to a temperature of 37 degrees C. J. Virol. 87, 7585-7592 (2013).
    • (2013) J. Virol. , vol.87 , pp. 7585-7592
    • Fibriansah, G.1
  • 33
    • 84876842073 scopus 로고    scopus 로고
    • Dengue structure differs at the temperatures of its human and mosquito hosts
    • Zhang, X. et al. Dengue structure differs at the temperatures of its human and mosquito hosts. Proc. Natl Acad. Sci. USA 110, 6795-6799 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 6795-6799
    • Zhang, X.1
  • 34
    • 83755178493 scopus 로고    scopus 로고
    • Residues in domain III of the dengue virus envelope glycoprotein involved in cell-surface glycosaminoglycan binding
    • Watterson, D., Kobe, B. & Young, P. R. Residues in domain III of the dengue virus envelope glycoprotein involved in cell-surface glycosaminoglycan binding. J. Gen. Virol. 93, 72-82 (2012).
    • (2012) J. Gen. Virol. , vol.93 , pp. 72-82
    • Watterson, D.1    Kobe, B.2    Young, P.R.3
  • 35
    • 78650608263 scopus 로고    scopus 로고
    • Molecular mechanisms involved in the early steps of flavivirus cell entry
    • Kaufmann, B. & Rossmann, M. G. Molecular mechanisms involved in the early steps of flavivirus cell entry. Microbes Infect. 13, 1-9 (2011).
    • (2011) Microbes Infect. , vol.13 , pp. 1-9
    • Kaufmann, B.1    Rossmann, M.G.2
  • 36
    • 32044436044 scopus 로고    scopus 로고
    • Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN
    • Pokidysheva, E. et al. Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN. Cell 124, 485-493 (2006).
    • (2006) Cell , vol.124 , pp. 485-493
    • Pokidysheva, E.1
  • 37
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its lowpH-induced membrane fusion conformation
    • Bressanelli, S. et al. Structure of a flavivirus envelope glycoprotein in its lowpH-induced membrane fusion conformation. EMBO J. 23, 728-738 (2004).
    • (2004) EMBO J. , vol.23 , pp. 728-738
    • Bressanelli, S.1
  • 38
    • 84895752114 scopus 로고    scopus 로고
    • A potent anti-dengue human antibody preferentially recognizes the conformation of e protein monomers assembled on the virus surface
    • Fibriansah, G. et al. A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface. EMBO Mol. Med. 6, 358-371 (2014).
    • (2014) EMBO Mol. Med. , vol.6 , pp. 358-371
    • Fibriansah, G.1
  • 39
    • 78650495030 scopus 로고    scopus 로고
    • Neutralization of West Nile virus by cross-linking of its surface proteins with Fab fragments of the human monoclonal antibody CR4354
    • Kaufmann, B. et al. Neutralization of West Nile virus by cross-linking of its surface proteins with Fab fragments of the human monoclonal antibody CR4354. Proc. Natl Acad. Sci. USA 107, 18950-18955 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 18950-18955
    • Kaufmann, B.1
  • 40
    • 33846024047 scopus 로고    scopus 로고
    • Early dengue infection and outcome study (EDEN)-study design and preliminary findings
    • Low, J. G. et al. Early dengue infection and outcome study (EDEN)-study design and preliminary findings. Ann. Acad. Med. Singapore 35, 783-789 (2006).
    • (2006) Ann. Acad. Med. Singapore , vol.35 , pp. 783-789
    • Low, J.G.1
  • 41
    • 36349025968 scopus 로고    scopus 로고
    • Comparison of plaque- and flow cytometry-based methods for measuring dengue virus neutralization
    • Kraus, A. A., Messer, W., Haymore, L. B. & de Silva, A. M. Comparison of plaque- and flow cytometry-based methods for measuring dengue virus neutralization. J. Clin. Microbiol. 45, 3777-3780 (2007).
    • (2007) J. Clin. Microbiol. , vol.45 , pp. 3777-3780
    • Kraus, A.A.1    Messer, W.2    Haymore, L.B.3    De Silva, A.M.4
  • 42
    • 84877933905 scopus 로고    scopus 로고
    • Human monoclonal antibodies derived from memory B cells following live attenuated dengue virus vaccination or natural infection exhibit similar characteristics
    • Smith, S. A. et al. Human monoclonal antibodies derived from memory B cells following live attenuated dengue virus vaccination or natural infection exhibit similar characteristics. J. Infect. Dis. 207, 1898-1908 (2013).
    • (2013) J. Infect. Dis. , vol.207 , pp. 1898-1908
    • Smith, S.A.1
  • 43
    • 33748948792 scopus 로고    scopus 로고
    • Cryptic properties of a cluster of dominant flavivirus cross-reactive antigenic sites
    • Stiasny, K., Kiermayr, S., Holzmann, H. & Heinz, F. X. Cryptic properties of a cluster of dominant flavivirus cross-reactive antigenic sites. J. Virol. 80, 9557-9568 (2006).
    • (2006) J. Virol. , vol.80 , pp. 9557-9568
    • Stiasny, K.1    Kiermayr, S.2    Holzmann, H.3    Heinz, F.X.4
  • 44
    • 77956031215 scopus 로고    scopus 로고
    • Structure and function analysis of therapeutic monoclonal antibodies against dengue virus type 2
    • Sukupolvi-Petty, S. et al. Structure and function analysis of therapeutic monoclonal antibodies against dengue virus type 2. J. Virol. 84, 9227-9239 (2010).
    • (2010) J. Virol. , vol.84 , pp. 9227-9239
    • Sukupolvi-Petty, S.1
  • 45
    • 0038519591 scopus 로고    scopus 로고
    • Development of group- and serotype-specific one-step SYBR green I-based real-time reverse transcription-PCR assay for dengue virus
    • Shu, P. Y. et al. Development of group- and serotype-specific one-step SYBR green I-based real-time reverse transcription-PCR assay for dengue virus. J. Clin. Microbiol. 41, 2408-2416 (2003).
    • (2003) J. Clin. Microbiol. , vol.41 , pp. 2408-2416
    • Shu, P.Y.1
  • 46
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak, K. J. & Schmittgen, T. D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25, 402-408 (2001).
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 47
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1
  • 48
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R. & Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 49
    • 34548643898 scopus 로고    scopus 로고
    • Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a multi-path simulated annealing optimization algorithm
    • Liu, X., Jiang, W., Jakana, J. & Chiu, W. Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. J. Struct. Biol. 160, 11-27 (2007).
    • (2007) J. Struct. Biol. , vol.160 , pp. 11-27
    • Liu, X.1    Jiang, W.2    Jakana, J.3    Chiu, W.4
  • 50
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 52
    • 42949089487 scopus 로고    scopus 로고
    • Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics
    • Trabuco, L. G., Villa, E., Mitra, K., Frank, J. & Schulten, K. Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure 16, 673-683 (2008).
    • (2008) Structure , vol.16 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 53
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips, J. C. et al. Scalable molecular dynamics with NAMD. J. Comput. Chem. 26, 1781-1802 (2005).
    • (2005) J. Comput. Chem. , vol.26 , pp. 1781-1802
    • Phillips, J.C.1
  • 54
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey, W., Dalke, A. & Schulten, K. VMD: visual molecular dynamics. J. Mol. Graph. 14, 33-38 27-8 (1996).
    • (1996) J. Mol. Graph. , vol.14 , Issue.33-38 , pp. 27-28
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 55
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y. & Cowan, S. W. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3
  • 56
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold, K., Bordoli, L., Kopp, J. & Schwede, T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201 (2006).
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 57
    • 0347250991 scopus 로고    scopus 로고
    • (eds Arnold, E., Himmel, D.M. & Rossmann, M.G.) (International Union of Crystallography)
    • Gerstein, M. & Richards, F. M. in International Tables for Crystallography Vol. F (eds Arnold, E., Himmel, D. M. & Rossmann, M. G.) 703-712 (International Union of Crystallography, 2012).
    • (2012) International Tables for Crystallography , vol.F , pp. 703-712
    • Gerstein, M.1    Richards, F.M.2
  • 58
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16, 10881-10890 (1988).
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.