메뉴 건너뛰기




Volumn 92, Issue 9, 2011, Pages 2020-2033

A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; GLYCOPROTEIN B; MONOCLONAL ANTIBODY;

EID: 80051721138     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/vir.0.032177-0     Document Type: Article
Times cited : (12)

References (52)
  • 1
    • 0033912858 scopus 로고    scopus 로고
    • Cloning and mutagenesis of the murine gammaherpesvirus 68 genome as an infectious bacterial artificial chromosome
    • Adler, H., Messerle, M., Wagner, M. & Koszinowski, U. H. (2000). Cloning and mutagenesis of the murine gammaherpesvirus 68 genome as an infectious bacterial artificial chromosome. J Virol 74, 6964-6974.
    • (2000) J Virol , vol.74 , pp. 6964-6974
    • Adler, H.1    Messerle, M.2    Wagner, M.3    Koszinowski, U.H.4
  • 2
    • 0036008473 scopus 로고    scopus 로고
    • Integrin a3b1 (CD 49c/29) is a cellular receptor for Kaposi's sarcomaassociated herpesvirus (KSHV/HHV-8) entry into the target cells
    • Akula, S. M., Pramod, N. P., Wang, F. Z. & Chandran, B. (2002). Integrin a3b1 (CD 49c/29) is a cellular receptor for Kaposi's sarcomaassociated herpesvirus (KSHV/HHV-8) entry into the target cells. Cell 108, 407-419.
    • (2002) Cell , vol.108 , pp. 407-419
    • Akula, S.M.1    Pramod, N.P.2    Wang, F.Z.3    Chandran, B.4
  • 3
    • 34548158909 scopus 로고    scopus 로고
    • Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity
    • Backovic, M., Jardetzky, T. S. & Longnecker, R. (2007). Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity. J Virol 81, 9596-9600.
    • (2007) J Virol , vol.81 , pp. 9596-9600
    • Backovic, M.1    Jardetzky, T.S.2    Longnecker, R.3
  • 4
    • 62449188223 scopus 로고    scopus 로고
    • Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B
    • Backovic, M., Longnecker, R. & Jardetzky, T. S. (2009). Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B. Proc Natl Acad Sci U S A 106, 2880-2885.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2880-2885
    • Backovic, M.1    Longnecker, R.2    Jardetzky, T.S.3
  • 5
    • 33744529389 scopus 로고    scopus 로고
    • Vaccinal control of Marek's disease: Current challenges, and future strategies to maximize protection
    • Baigent, S. J., Smith, L. P., Nair, V. K. & Currie, R. J. (2006). Vaccinal control of Marek's disease: current challenges, and future strategies to maximize protection. Vet Immunol Immunopathol 112, 78-86.
    • (2006) Vet Immunol Immunopathol , vol.112 , pp. 78-86
    • Baigent, S.J.1    Smith, L.P.2    Nair, V.K.3    Currie, R.J.4
  • 6
    • 0037938686 scopus 로고    scopus 로고
    • Aminophospholipid asymmetry: A matter of life and death
    • Balasubramanian, K. & Schroit, A. J. (2003). Aminophospholipid asymmetry: a matter of life and death. Annu Rev Physiol 65, 701-734.
    • (2003) Annu Rev Physiol , vol.65 , pp. 701-734
    • Balasubramanian, K.1    Schroit, A.J.2
  • 7
    • 0346767635 scopus 로고
    • Identification of the human cytomegalovirus glycoprotein B gene and induction of neutralizing antibodies via its expression in recombinant vaccinia virus
    • Cranage, M. P., Kouzarides, T., Bankier, A. T., Satchwell, S., Weston, K., Tomlinson, P., Barrell, B., Hart, H., Bell, S. E. & other authors (1986). Identification of the human cytomegalovirus glycoprotein B gene and induction of neutralizing antibodies via its expression in recombinant vaccinia virus. EMBO J 5, 3057-3063.
    • (1986) EMBO J , vol.5 , pp. 3057-3063
    • Cranage, M.P.1    Kouzarides, T.2    Bankier, A.T.3    Satchwell, S.4    Weston, K.5    Tomlinson, P.6    Barrell, B.7    Hart, H.8    Bell, S.E.9
  • 8
    • 2342459131 scopus 로고    scopus 로고
    • Murine gammaherpesvirus 68 lacking gp150 shows defective virion release but establishes normal latency in vivo
    • de Lima, B. D., May, J. S. & Stevenson, P. G. (2004). Murine gammaherpesvirus 68 lacking gp150 shows defective virion release but establishes normal latency in vivo. J Virol 78, 5103-5112.
    • (2004) J Virol , vol.78 , pp. 5103-5112
    • de Lima, B.D.1    May, J.S.2    Stevenson, P.G.3
  • 9
    • 77549086793 scopus 로고    scopus 로고
    • Low pH-induced conformational change in herpes simplex virus glycoprotein B
    • Dollery, S. J., Delboy, M. G. & Nicola, A. V. (2010). Low pH-induced conformational change in herpes simplex virus glycoprotein B. J Virol 84, 3759-3766.
    • (2010) J Virol , vol.84 , pp. 3759-3766
    • Dollery, S.J.1    Delboy, M.G.2    Nicola, A.V.3
  • 10
    • 0025313893 scopus 로고
    • Murine herpesvirus 68 is genetically related to the gammaherpesviruses Epstein-Barr virus and herpesvirus saimiri
    • Efstathiou, S., Ho, Y. M., Hall, S., Styles, C. J., Scott, S. D. & Gompels, U. A. (1990). Murine herpesvirus 68 is genetically related to the gammaherpesviruses Epstein-Barr virus and herpesvirus saimiri. J Gen Virol 71, 1365-1372.
    • (1990) J Gen Virol , vol.71 , pp. 1365-1372
    • Efstathiou, S.1    Ho, Y.M.2    Hall, S.3    Styles, C.J.4    Scott, S.D.5    Gompels, U.A.6
  • 12
    • 33744822158 scopus 로고    scopus 로고
    • Murine gammaherpesvirus-68 glycoprotein H-glycoprotein L complex is a major target for neutralizing monoclonal antibodies
    • Gill, M. B., Gillet, L., Colaco, S., May, J. S., de Lima, B. D. & Stevenson, P. G. (2006). Murine gammaherpesvirus-68 glycoprotein H-glycoprotein L complex is a major target for neutralizing monoclonal antibodies. J Gen Virol 87, 1465-1475.
    • (2006) J Gen Virol , vol.87 , pp. 1465-1475
    • Gill, M.B.1    Gillet, L.2    Colaco, S.3    May, J.S.4    de Lima, B.D.5    Stevenson, P.G.6
  • 14
    • 36348992611 scopus 로고    scopus 로고
    • Evidence for a multiprotein gamma-2 herpesvirus entry complex
    • Gillet, L. & Stevenson, P. G. (2007b). Evidence for a multiprotein gamma-2 herpesvirus entry complex. J Virol 81, 13082-13091.
    • (2007) J Virol , vol.81 , pp. 13082-13091
    • Gillet, L.1    Stevenson, P.G.2
  • 15
    • 33751394229 scopus 로고    scopus 로고
    • Murine gammaherpesvirus-68 glycoprotein B presents a difficult neutralization target to monoclonal antibodies derived from infected mice
    • Gillet, L., Gill, M. B., Colaco, S., Smith, C. M. & Stevenson, P. G. (2006). Murine gammaherpesvirus-68 glycoprotein B presents a difficult neutralization target to monoclonal antibodies derived from infected mice. J Gen Virol 87, 3515-3527.
    • (2006) J Gen Virol , vol.87 , pp. 3515-3527
    • Gillet, L.1    Gill, M.B.2    Colaco, S.3    Smith, C.M.4    Stevenson, P.G.5
  • 16
    • 37149016706 scopus 로고    scopus 로고
    • Post-exposure vaccination improves gammaherpesvirus neutralization
    • Gillet, L., May, J. S. & Stevenson, P. G. (2007a). Post-exposure vaccination improves gammaherpesvirus neutralization. PLoS ONE 2, e899.
    • (2007) PLoS ONE , vol.2
    • Gillet, L.1    May, J.S.2    Stevenson, P.G.3
  • 17
    • 36348942977 scopus 로고    scopus 로고
    • Glycosaminoglycan interactions in murine gammaherpesvirus-68 infection
    • Gillet, L., Adler, H. & Stevenson, P. G. (2007b). Glycosaminoglycan interactions in murine gammaherpesvirus-68 infection. PLoS ONE 2, e347.
    • (2007) PLoS ONE , vol.2
    • Gillet, L.1    Adler, H.2    Stevenson, P.G.3
  • 18
    • 33845723594 scopus 로고    scopus 로고
    • Glycoprotein L disruption reveals two functional forms of the murine gammaherpesvirus 68 glycoprotein H
    • Gillet, L., May, J. S., Colaco, S. & Stevenson, P. G. (2007c). Glycoprotein L disruption reveals two functional forms of the murine gammaherpesvirus 68 glycoprotein H. J Virol 81, 280-291.
    • (2007) J Virol , vol.81 , pp. 280-291
    • Gillet, L.1    May, J.S.2    Colaco, S.3    Stevenson, P.G.4
  • 19
    • 45949085102 scopus 로고    scopus 로고
    • Glycoprotein B switches conformation during murid herpesvirus 4 entry
    • Gillet, L., Colaco, S. & Stevenson, P. G. (2008a). Glycoprotein B switches conformation during murid herpesvirus 4 entry. J Gen Virol 89, 1352-1363.
    • (2008) J Gen Virol , vol.89 , pp. 1352-1363
    • Gillet, L.1    Colaco, S.2    Stevenson, P.G.3
  • 20
    • 50949098291 scopus 로고    scopus 로고
    • The murid herpesvirus-4 gL regulates an entry-associated conformation change in gH
    • Gillet, L., Colaco, S. & Stevenson, P. G. (2008b). The murid herpesvirus-4 gL regulates an entry-associated conformation change in gH. PLoS ONE 3, e2811.
    • (2008) PLoS ONE , vol.3
    • Gillet, L.1    Colaco, S.2    Stevenson, P.G.3
  • 21
    • 63449095086 scopus 로고    scopus 로고
    • In vivo importance of heparan sulfate-binding glycoproteins for murid herpesvirus-4 infection
    • Gillet, L., May, J. S. & Stevenson, P. G. (2009a). In vivo importance of heparan sulfate-binding glycoproteins for murid herpesvirus-4 infection. J Gen Virol 90, 602-613.
    • (2009) J Gen Virol , vol.90 , pp. 602-613
    • Gillet, L.1    May, J.S.2    Stevenson, P.G.3
  • 23
    • 33646129465 scopus 로고    scopus 로고
    • Mixed infection with multiple strains of murine cytomegalovirus occurs following simultaneous or sequential infection of immunocompetent mice
    • Gorman, S., Harvey, N. L., Moro, D., Lloyd, M. L., Voigt, V., Smith, L. M., Lawson, M. A. & Shellam, G. R. (2006). Mixed infection with multiple strains of murine cytomegalovirus occurs following simultaneous or sequential infection of immunocompetent mice. J Gen Virol 87, 1123-1132.
    • (2006) J Gen Virol , vol.87 , pp. 1123-1132
    • Gorman, S.1    Harvey, N.L.2    Moro, D.3    Lloyd, M.L.4    Voigt, V.5    Smith, L.M.6    Lawson, M.A.7    Shellam, G.R.8
  • 24
    • 0028948946 scopus 로고
    • Complementarity, specificity and the nature of epitopes and paratopes in multivalent interactions
    • Greenspan, N. S. & Cooper, L. J. (1995). Complementarity, specificity and the nature of epitopes and paratopes in multivalent interactions. Immunol Today 16, 226-230.
    • (1995) Immunol Today , vol.16 , pp. 226-230
    • Greenspan, N.S.1    Cooper, L.J.2
  • 25
    • 67449093075 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops
    • Hannah, B. P., Cairns, T. M., Bender, F. C., Whitbeck, J. C., Lou, H., Eisenberg, R. J. & Cohen, G. H. (2009). Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops. J Virol 83, 6825-6836.
    • (2009) J Virol , vol.83 , pp. 6825-6836
    • Hannah, B.P.1    Cairns, T.M.2    Bender, F.C.3    Whitbeck, J.C.4    Lou, H.5    Eisenberg, R.J.6    Cohen, G.H.7
  • 27
    • 0023941343 scopus 로고
    • Monoclonal antibodies define a domain on herpes simplex virus glycoprotein B involved in virus penetration
    • Highlander, S. L., Cai, W. H., Person, S., Levine, M. & Glorioso, J. C. (1988). Monoclonal antibodies define a domain on herpes simplex virus glycoprotein B involved in virus penetration. J Virol 62, 1881-1888.
    • (1988) J Virol , vol.62 , pp. 1881-1888
    • Highlander, S.L.1    Cai, W.H.2    Person, S.3    Levine, M.4    Glorioso, J.C.5
  • 28
    • 34547110512 scopus 로고    scopus 로고
    • Epstein-Barr virus entry
    • Hutt-Fletcher, L. M. (2007). Epstein-Barr virus entry. J Virol 81, 7825-7832.
    • (2007) J Virol , vol.81 , pp. 7825-7832
    • Hutt-Fletcher, L.M.1
  • 29
    • 0024422587 scopus 로고
    • Reinfections and site-specific immunity in herpes simplex virus infections
    • Klein, R. J. (1989). Reinfections and site-specific immunity in herpes simplex virus infections. Vaccine 7, 380-381.
    • (1989) Vaccine , vol.7 , pp. 380-381
    • Klein, R.J.1
  • 30
    • 33746870392 scopus 로고    scopus 로고
    • Variation and infectivity neutralization in influenza
    • Knossow, M. & Skehel, J. J. (2006). Variation and infectivity neutralization in influenza. Immunology 119, 1-7.
    • (2006) Immunology , vol.119 , pp. 1-7
    • Knossow, M.1    Skehel, J.J.2
  • 31
    • 0032174579 scopus 로고    scopus 로고
    • Lipids, lipid domains and lipid-protein interactions in endocytic membrane traffic
    • Kobayashi, T., Gu, F. & Gruenberg, J. (1998). Lipids, lipid domains and lipid-protein interactions in endocytic membrane traffic. Semin Cell Dev Biol 9, 517-526.
    • (1998) Semin Cell Dev Biol , vol.9 , pp. 517-526
    • Kobayashi, T.1    Gu, F.2    Gruenberg, J.3
  • 32
    • 8744255609 scopus 로고    scopus 로고
    • Characterization of murine gammaherpesvirus 68 glycoprotein B
    • Lopes, F. B., Colaco, S., May, J. S. & Stevenson, P. G. (2004). Characterization of murine gammaherpesvirus 68 glycoprotein B. J Virol 78, 13370-13375.
    • (2004) J Virol , vol.78 , pp. 13370-13375
    • Lopes, F.B.1    Colaco, S.2    May, J.S.3    Stevenson, P.G.4
  • 33
    • 0013797229 scopus 로고
    • Immunochemical quantitation of antigens by single radial immunodiffusion
    • Mancini, G., Carbonara, A. O. & Heremans, J. F. (1965). Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry 2, 235-254.
    • (1965) Immunochemistry , vol.2 , pp. 235-254
    • Mancini, G.1    Carbonara, A.O.2    Heremans, J.F.3
  • 34
    • 77956849504 scopus 로고    scopus 로고
    • Vaccination with murid herpesvirus-4 glycoprotein B reduces viral lytic replication but does not induce detectable virion neutralization
    • May, J. S. & Stevenson, P. G. (2010). Vaccination with murid herpesvirus-4 glycoprotein B reduces viral lytic replication but does not induce detectable virion neutralization. J Gen Virol 91, 2542-2552.
    • (2010) J Gen Virol , vol.91 , pp. 2542-2552
    • May, J.S.1    Stevenson, P.G.2
  • 35
    • 1642421746 scopus 로고    scopus 로고
    • Forced lytic replication impairs host colonization by a latency-deficient mutant of murine gammaherpesvirus-68
    • May, J. S., Coleman, H. M., Smillie, B., Efstathiou, S. & Stevenson, P. G. (2004). Forced lytic replication impairs host colonization by a latency-deficient mutant of murine gammaherpesvirus-68. J Gen Virol 85, 137-146.
    • (2004) J Gen Virol , vol.85 , pp. 137-146
    • May, J.S.1    Coleman, H.M.2    Smillie, B.3    Efstathiou, S.4    Stevenson, P.G.5
  • 36
    • 14744272167 scopus 로고    scopus 로고
    • Glycoprotein M is an essential lytic replication protein of the murine gammaherpesvirus 68
    • May, J. S., Colaco, S. & Stevenson, P. G. (2005). Glycoprotein M is an essential lytic replication protein of the murine gammaherpesvirus 68. J Virol 79, 3459-3467.
    • (2005) J Virol , vol.79 , pp. 3459-3467
    • May, J.S.1    Colaco, S.2    Stevenson, P.G.3
  • 37
    • 47749084293 scopus 로고    scopus 로고
    • An essential role for the proximal but not the distal cytoplasmic tail of glycoprotein M in murid herpesvirus 4 infection
    • May, J. S., Smith, C. M., Gill, M. B. & Stevenson, P. G. (2008). An essential role for the proximal but not the distal cytoplasmic tail of glycoprotein M in murid herpesvirus 4 infection. PLoS ONE 3, e2131.
    • (2008) PLoS ONE , vol.3
    • May, J.S.1    Smith, C.M.2    Gill, M.B.3    Stevenson, P.G.4
  • 38
    • 0027448559 scopus 로고
    • Glycoprotein B of human cytomegalovirus promotes virion penetration into cells, transmission of infection from cell to cell, and fusion of infected cells
    • Navarro, D., Paz, P., Tugizov, S., Topp, K., La Vail, J. & Pereira, L. (1993). Glycoprotein B of human cytomegalovirus promotes virion penetration into cells, transmission of infection from cell to cell, and fusion of infected cells. Virology 197, 143-158.
    • (1993) Virology , vol.197 , pp. 143-158
    • Navarro, D.1    Paz, P.2    Tugizov, S.3    Topp, K.4    la Vail, J.5    Pereira, L.6
  • 39
    • 0027398669 scopus 로고
    • Fine specificity of the human immune response to the major neutralization epitopes expressed on cytomegalovirus gp58/116 (gB), as determined with human monoclonal antibodies
    • Ohlin, M., Sundqvist, V. A., Mach, M., Wahren, B. & Borrebaeck, C. A. (1993). Fine specificity of the human immune response to the major neutralization epitopes expressed on cytomegalovirus gp58/116 (gB), as determined with human monoclonal antibodies. J Virol 67, 703-710.
    • (1993) J Virol , vol.67 , pp. 703-710
    • Ohlin, M.1    Sundqvist, V.A.2    Mach, M.3    Wahren, B.4    Borrebaeck, C.A.5
  • 40
    • 30644467785 scopus 로고    scopus 로고
    • The aminoterminal residue of glycoprotein B is critical for neutralization of bovine herpesvirus 1
    • Okazaki, K., Fujii, S., Takada, A. & Kida, H. (2006). The aminoterminal residue of glycoprotein B is critical for neutralization of bovine herpesvirus 1. Virus Res 115, 105-111.
    • (2006) Virus Res , vol.115 , pp. 105-111
    • Okazaki, K.1    Fujii, S.2    Takada, A.3    Kida, H.4
  • 41
    • 33745974537 scopus 로고    scopus 로고
    • Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
    • Roche, S., Bressanelli, S., Rey, F. A. & Gaudin, Y. (2006). Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science 313, 187-191.
    • (2006) Science , vol.313 , pp. 187-191
    • Roche, S.1    Bressanelli, S.2    Rey, F.A.3    Gaudin, Y.4
  • 42
    • 33846959065 scopus 로고    scopus 로고
    • Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G
    • Roche, S., Rey, F. A., Gaudin, Y. & Bressanelli, S. (2007). Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G. Science 315, 843-848.
    • (2007) Science , vol.315 , pp. 843-848
    • Roche, S.1    Rey, F.A.2    Gaudin, Y.3    Bressanelli, S.4
  • 43
    • 44749085794 scopus 로고    scopus 로고
    • Structures of vesicular stomatitis virus glycoprotein: Membrane fusion revisited
    • Roche, S., Albertini, A. A., Lepault, J., Bressanelli, S. & Gaudin, Y. (2008). Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited. Cell Mol Life Sci 65, 1716-1728.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1716-1728
    • Roche, S.1    Albertini, A.A.2    Lepault, J.3    Bressanelli, S.4    Gaudin, Y.5
  • 44
    • 37149016707 scopus 로고    scopus 로고
    • IgG fc receptors provide an alternative infection route for murine gamma-herpesvirus-68
    • Rosa, G. T., Gillet, L., Smith, C. M., de Lima, B. D. & Stevenson, P. G. (2007). IgG fc receptors provide an alternative infection route for murine gamma-herpesvirus-68. PLoS ONE 2, e560.
    • (2007) PLoS ONE , vol.2
    • Rosa, G.T.1    Gillet, L.2    Smith, C.M.3    de Lima, B.D.4    Stevenson, P.G.5
  • 45
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A. & Zhang, Y. (2010). I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5, 725-738.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 46
    • 42349086399 scopus 로고    scopus 로고
    • Murine gammaherpesvirus-68 inhibits antigen presentation by dendritic cells
    • Smith, C. M., Gill, M. B., May, J. S. & Stevenson, P. G. (2007). Murine gammaherpesvirus-68 inhibits antigen presentation by dendritic cells. PLoS ONE 2, e1048.
    • (2007) PLoS ONE , vol.2
    • Smith, C.M.1    Gill, M.B.2    May, J.S.3    Stevenson, P.G.4
  • 47
    • 0141632878 scopus 로고    scopus 로고
    • Herpesvirus entry: An update
    • Spear, P. G. & Longnecker, R. (2003). Herpesvirus entry: an update. J Virol 77, 10179-10185.
    • (2003) J Virol , vol.77 , pp. 10179-10185
    • Spear, P.G.1    Longnecker, R.2
  • 48
    • 0032802172 scopus 로고    scopus 로고
    • Antigenic domain 1 of human cytomegalovirus glycoprotein B induces a multitude of different antibodies which, when combined, results in incomplete virus neutralization
    • Speckner, A., Glykofrydes, D., Ohlin, M. & Mach, M. (1999). Antigenic domain 1 of human cytomegalovirus glycoprotein B induces a multitude of different antibodies which, when combined, results in incomplete virus neutralization. J Gen Virol 80, 2183-2191.
    • (1999) J Gen Virol , vol.80 , pp. 2183-2191
    • Speckner, A.1    Glykofrydes, D.2    Ohlin, M.3    Mach, M.4
  • 49
    • 78649413011 scopus 로고    scopus 로고
    • Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1
    • Stampfer, S. D., Lou, H., Cohen, G. H., Eisenberg, R. J. & Heldwein, E. E. (2010). Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1. J Virol 84, 12924-12933.
    • (2010) J Virol , vol.84 , pp. 12924-12933
    • Stampfer, S.D.1    Lou, H.2    Cohen, G.H.3    Eisenberg, R.J.4    Heldwein, E.E.5
  • 51
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. (2008). I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9, 40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 52
    • 33745098337 scopus 로고    scopus 로고
    • Protective 'immunity' by pre-existent neutralizing antibody titers and preactivated T cells but not by so-called 'immunological memory'
    • Zinkernagel, R. M. & Hengartner, H. (2006). Protective 'immunity' by pre-existent neutralizing antibody titers and preactivated T cells but not by so-called 'immunological memory'. Immunol Rev 211, 310-319.
    • (2006) Immunol Rev , vol.211 , pp. 310-319
    • Zinkernagel, R.M.1    Hengartner, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.