메뉴 건너뛰기




Volumn 174, Issue 4, 2018, Pages 938-952.e13

Systematic Analysis of Monoclonal Antibodies against Ebola Virus GP Defines Features that Contribute to Protection

(48)  Saphire, Erica Ollmann a   Schendel, Sharon L a   Fusco, Marnie L a   Gangavarapu, Karthik a   Gunn, Bronwyn M b   Wec, Anna Z c   Halfmann, Peter J d   Brannan, Jennifer M e   Herbert, Andrew S e   Qiu, Xiangguo f   Wagh, Kshitij g   He, Shihua f   Giorgi, Elena E g   Theiler, James g   Pommert, Kathleen B J a   Krause, Tyler B c   Turner, Hannah L a   Murin, Charles D a   Pallesen, Jesper a   Davidson, Edgar h   more..


Author keywords

antibody; consortium; ebola virus; epitope; glycoprotein; neutralization; protection

Indexed keywords

MONOCLONAL ANTIBODY; VIRUS GLYCOPROTEIN; EPITOPE; MEMBRANE PROTEIN;

EID: 85050869127     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2018.07.033     Document Type: Article
Times cited : (163)

References (85)
  • 2
    • 10344255635 scopus 로고    scopus 로고
    • CD107a as a functional marker for the identification of natural killer cell activity
    • Alter, G., Malenfant, J.M., Altfeld, M., CD107a as a functional marker for the identification of natural killer cell activity. J. Immunol. Methods 294 (2004), 15–22.
    • (2004) J. Immunol. Methods , vol.294 , pp. 15-22
    • Alter, G.1    Malenfant, J.M.2    Altfeld, M.3
  • 3
    • 84922806645 scopus 로고    scopus 로고
    • Molecular characterization of the monoclonal antibodies composing ZMAb: a protective cocktail against Ebola virus
    • Audet, J., Wong, G., Wang, H., Lu, G., Gao, G.F., Kobinger, G., Qiu, X., Molecular characterization of the monoclonal antibodies composing ZMAb: a protective cocktail against Ebola virus. Sci. Rep., 4, 2014, 6881.
    • (2014) Sci. Rep. , vol.4 , pp. 6881
    • Audet, J.1    Wong, G.2    Wang, H.3    Lu, G.4    Gao, G.F.5    Kobinger, G.6    Qiu, X.7
  • 6
    • 0031688699 scopus 로고    scopus 로고
    • A mouse model for evaluation of prophylaxis and therapy of Ebola hemorrhagic fever
    • Bray, M., Davis, K., Geisbert, T., Schmaljohn, C., Huggins, J., A mouse model for evaluation of prophylaxis and therapy of Ebola hemorrhagic fever. J. Infect. Dis. 178 (1998), 651–661.
    • (1998) J. Infect. Dis. , vol.178 , pp. 651-661
    • Bray, M.1    Davis, K.2    Geisbert, T.3    Schmaljohn, C.4    Huggins, J.5
  • 7
    • 0035478854 scopus 로고    scopus 로고
    • Random Forests
    • Breiman, L., Random Forests. Mach. Learn. 45 (2001), 5–32.
    • (2001) Mach. Learn. , vol.45 , pp. 5-32
    • Breiman, L.1
  • 8
    • 84862495640 scopus 로고    scopus 로고
    • Properties of mouse and human IgG receptors and their contribution to disease models
    • Bruhns, P., Properties of mouse and human IgG receptors and their contribution to disease models. Blood 119 (2012), 5640–5649.
    • (2012) Blood , vol.119 , pp. 5640-5649
    • Bruhns, P.1
  • 9
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran, K., Sullivan, N.J., Felbor, U., Whelan, S.P., Cunningham, J.M., Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308 (2005), 1643–1645.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 13
    • 84945217199 scopus 로고    scopus 로고
    • Mechanism of Binding to Ebola Virus Glycoprotein by the ZMapp, ZMAb, and MB-003 Cocktail Antibodies
    • Davidson, E., Bryan, C., Fong, R.H., Barnes, T., Pfaff, J.M., Mabila, M., Rucker, J.B., Doranz, B.J., Mechanism of Binding to Ebola Virus Glycoprotein by the ZMapp, ZMAb, and MB-003 Cocktail Antibodies. J. Virol. 89 (2015), 10982–10992.
    • (2015) J. Virol. , vol.89 , pp. 10982-10992
    • Davidson, E.1    Bryan, C.2    Fong, R.H.3    Barnes, T.4    Pfaff, J.M.5    Mabila, M.6    Rucker, J.B.7    Doranz, B.J.8
  • 15
    • 63149192804 scopus 로고    scopus 로고
    • The primed ebolavirus glycoprotein (19-kilodalton GP1,2): sequence and residues critical for host cell binding
    • Dube, D., Brecher, M.B., Delos, S.E., Rose, S.C., Park, E.W., Schornberg, K.L., Kuhn, J.H., White, J.M., The primed ebolavirus glycoprotein (19-kilodalton GP1,2): sequence and residues critical for host cell binding. J. Virol. 83 (2009), 2883–2891.
    • (2009) J. Virol. , vol.83 , pp. 2883-2891
    • Dube, D.1    Brecher, M.B.2    Delos, S.E.3    Rose, S.C.4    Park, E.W.5    Schornberg, K.L.6    Kuhn, J.H.7    White, J.M.8
  • 23
    • 84899756347 scopus 로고    scopus 로고
    • A novel human anti-interleukin-1β neutralizing monoclonal antibody showing in vivo efficacy
    • Goh, A.X.H., Bertin-Maghit, S., Ping Yeo, S., Ho, A.W.S., Derks, H., Mortellaro, A., Wang, C.-I., A novel human anti-interleukin-1β neutralizing monoclonal antibody showing in vivo efficacy. MAbs 6 (2014), 765–773.
    • (2014) MAbs , vol.6 , pp. 765-773
    • Goh, A.X.H.1    Bertin-Maghit, S.2    Ping Yeo, S.3    Ho, A.W.S.4    Derks, H.5    Mortellaro, A.6    Wang, C.-I.7
  • 33
    • 84963838685 scopus 로고    scopus 로고
    • Chimeric Filoviruses for Identification and Characterization of Monoclonal Antibodies
    • Ilinykh, P.A., Shen, X., Flyak, A.I., Kuzmina, N., Ksiazek, T.G., Crowe, J.E. Jr., Bukreyev, A., Chimeric Filoviruses for Identification and Characterization of Monoclonal Antibodies. J. Virol. 90 (2016), 3890–3901.
    • (2016) J. Virol. , vol.90 , pp. 3890-3901
    • Ilinykh, P.A.1    Shen, X.2    Flyak, A.I.3    Kuzmina, N.4    Ksiazek, T.G.5    Crowe, J.E.6    Bukreyev, A.7
  • 35
    • 84992724541 scopus 로고    scopus 로고
    • Human antibody repertoire after VSV-Ebola vaccination identifies novel targets and virus-neutralizing IgM antibodies
    • Khurana, S., Fuentes, S., Coyle, E.M., Ravichandran, S., Davey, R.T. Jr., Beigel, J.H., Human antibody repertoire after VSV-Ebola vaccination identifies novel targets and virus-neutralizing IgM antibodies. Nat. Med. 22 (2016), 1439–1447.
    • (2016) Nat. Med. , vol.22 , pp. 1439-1447
    • Khurana, S.1    Fuentes, S.2    Coyle, E.M.3    Ravichandran, S.4    Davey, R.T.5    Beigel, J.H.6
  • 36
    • 84869465815 scopus 로고    scopus 로고
    • Two synthetic antibodies that recognize and neutralize distinct proteolytic forms of the ebola virus envelope glycoprotein
    • Koellhoffer, J.F., Chen, G., Sandesara, R.G., Bale, S., Saphire, E.O., Chandran, K., Sidhu, S.S., Lai, J.R., Two synthetic antibodies that recognize and neutralize distinct proteolytic forms of the ebola virus envelope glycoprotein. ChemBioChem 13 (2012), 2549–2557.
    • (2012) ChemBioChem , vol.13 , pp. 2549-2557
    • Koellhoffer, J.F.1    Chen, G.2    Sandesara, R.G.3    Bale, S.4    Saphire, E.O.5    Chandran, K.6    Sidhu, S.S.7    Lai, J.R.8
  • 37
    • 84924060844 scopus 로고    scopus 로고
    • Advances in the development of influenza virus vaccines
    • Krammer, F., Palese, P., Advances in the development of influenza virus vaccines. Nat. Rev. Drug Discov. 14 (2015), 167–182.
    • (2015) Nat. Rev. Drug Discov. , vol.14 , pp. 167-182
    • Krammer, F.1    Palese, P.2
  • 38
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor
    • Lee, J.E., Fusco, M.L., Hessell, A.J., Oswald, W.B., Burton, D.R., Saphire, E.O., Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 454 (2008), 177–182.
    • (2008) Nature , vol.454 , pp. 177-182
    • Lee, J.E.1    Fusco, M.L.2    Hessell, A.J.3    Oswald, W.B.4    Burton, D.R.5    Saphire, E.O.6
  • 40
    • 84942096625 scopus 로고    scopus 로고
    • Conformational Masking and Receptor-Dependent Unmasking of Highly Conserved Env Epitopes Recognized by Non-Neutralizing Antibodies That Mediate Potent ADCC against HIV-1
    • Lewis, G.K., Finzi, A., DeVico, A.L., Pazgier, M., Conformational Masking and Receptor-Dependent Unmasking of Highly Conserved Env Epitopes Recognized by Non-Neutralizing Antibodies That Mediate Potent ADCC against HIV-1. Viruses 7 (2015), 5115–5132.
    • (2015) Viruses , vol.7 , pp. 5115-5132
    • Lewis, G.K.1    Finzi, A.2    DeVico, A.L.3    Pazgier, M.4
  • 42
    • 84990237697 scopus 로고    scopus 로고
    • An Ebola Virus-Like Particle-Based Reporter System Enables Evaluation of Antiviral Drugs In Vivo under Non-Biosafety Level 4 Conditions
    • Li, D., Chen, T., Hu, Y., Zhou, Y., Liu, Q., Zhou, D., Jin, X., Huang, Z., An Ebola Virus-Like Particle-Based Reporter System Enables Evaluation of Antiviral Drugs In Vivo under Non-Biosafety Level 4 Conditions. J. Virol. 90 (2016), 8720–8728.
    • (2016) J. Virol. , vol.90 , pp. 8720-8728
    • Li, D.1    Chen, T.2    Hu, Y.3    Zhou, Y.4    Liu, Q.5    Zhou, D.6    Jin, X.7    Huang, Z.8
  • 43
    • 84875998684 scopus 로고    scopus 로고
    • Impact of immune complex size and glycosylation on IgG binding to human FcγRs
    • Lux, A., Yu, X., Scanlan, C.N., Nimmerjahn, F., Impact of immune complex size and glycosylation on IgG binding to human FcγRs. J. Immunol. 190 (2013), 4315–4323.
    • (2013) J. Immunol. , vol.190 , pp. 4315-4323
    • Lux, A.1    Yu, X.2    Scanlan, C.N.3    Nimmerjahn, F.4
  • 48
    • 85030704263 scopus 로고    scopus 로고
    • Non-neutralizing Antibodies Targeting the V1V2 Domain of HIV Exhibit Strong Antibody-Dependent Cell-mediated Cytotoxic Activity
    • Mayr, L.M., Decoville, T., Schmidt, S., Laumond, G., Klingler, J., Ducloy, C., Bahram, S., Zolla-Pazner, S., Moog, C., Non-neutralizing Antibodies Targeting the V1V2 Domain of HIV Exhibit Strong Antibody-Dependent Cell-mediated Cytotoxic Activity. Sci. Rep., 7, 2017, 12655.
    • (2017) Sci. Rep. , vol.7 , pp. 12655
    • Mayr, L.M.1    Decoville, T.2    Schmidt, S.3    Laumond, G.4    Klingler, J.5    Ducloy, C.6    Bahram, S.7    Zolla-Pazner, S.8    Moog, C.9
  • 50
    • 84872010391 scopus 로고    scopus 로고
    • Antigenic subversion: a novel mechanism of host immune evasion by Ebola virus
    • Mohan, G.S., Li, W., Ye, L., Compans, R.W., Yang, C., Antigenic subversion: a novel mechanism of host immune evasion by Ebola virus. PLoS Pathog., 8, 2012, e1003065.
    • (2012) PLoS Pathog. , vol.8 , pp. e1003065
    • Mohan, G.S.1    Li, W.2    Ye, L.3    Compans, R.W.4    Yang, C.5
  • 54
    • 0032128276 scopus 로고    scopus 로고
    • Natural killer cells from human immunodeficiency virus (HIV)-infected individuals are an important source of CC-chemokines and suppress HIV-1 entry and replication in vitro
    • Oliva, A., Kinter, A.L., Vaccarezza, M., Rubbert, A., Catanzaro, A., Moir, S., Monaco, J., Ehler, L., Mizell, S., Jackson, R., et al. Natural killer cells from human immunodeficiency virus (HIV)-infected individuals are an important source of CC-chemokines and suppress HIV-1 entry and replication in vitro. J. Clin. Invest. 102 (1998), 223–231.
    • (1998) J. Clin. Invest. , vol.102 , pp. 223-231
    • Oliva, A.1    Kinter, A.L.2    Vaccarezza, M.3    Rubbert, A.4    Catanzaro, A.5    Moir, S.6    Monaco, J.7    Ehler, L.8    Mizell, S.9    Jackson, R.10
  • 60
    • 0034663585 scopus 로고    scopus 로고
    • Recombinant RNA replicons derived from attenuated Venezuelan equine encephalitis virus protect guinea pigs and mice from Ebola hemorrhagic fever virus
    • Pushko, P., Bray, M., Ludwig, G.V., Parker, M., Schmaljohn, A., Sanchez, A., Jahrling, P.B., Smith, J.F., Recombinant RNA replicons derived from attenuated Venezuelan equine encephalitis virus protect guinea pigs and mice from Ebola hemorrhagic fever virus. Vaccine 19 (2000), 142–153.
    • (2000) Vaccine , vol.19 , pp. 142-153
    • Pushko, P.1    Bray, M.2    Ludwig, G.V.3    Parker, M.4    Schmaljohn, A.5    Sanchez, A.6    Jahrling, P.B.7    Smith, J.F.8
  • 61
    • 80054837546 scopus 로고    scopus 로고
    • Characterization of Zaire ebolavirus glycoprotein-specific monoclonal antibodies
    • Qiu, X., Alimonti, J.B., Melito, P.L., Fernando, L., Ströher, U., Jones, S.M., Characterization of Zaire ebolavirus glycoprotein-specific monoclonal antibodies. Clin. Immunol. 141 (2011), 218–227.
    • (2011) Clin. Immunol. , vol.141 , pp. 218-227
    • Qiu, X.1    Alimonti, J.B.2    Melito, P.L.3    Fernando, L.4    Ströher, U.5    Jones, S.M.6
  • 65
    • 0029976177 scopus 로고    scopus 로고
    • The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing
    • Sanchez, A., Trappier, S.G., Mahy, B.W., Peters, C.J., Nichol, S.T., The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing. Proc. Natl. Acad. Sci. USA 93 (1996), 3602–3607.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3602-3607
    • Sanchez, A.1    Trappier, S.G.2    Mahy, B.W.3    Peters, C.J.4    Nichol, S.T.5
  • 66
    • 0031878483 scopus 로고    scopus 로고
    • Biochemical analysis of the secreted and virion glycoproteins of Ebola virus
    • Sanchez, A., Yang, Z.Y., Xu, L., Nabel, G.J., Crews, T., Peters, C.J., Biochemical analysis of the secreted and virion glycoproteins of Ebola virus. J. Virol. 72 (1998), 6442–6447.
    • (1998) J. Virol. , vol.72 , pp. 6442-6447
    • Sanchez, A.1    Yang, Z.Y.2    Xu, L.3    Nabel, G.J.4    Crews, T.5    Peters, C.J.6
  • 67
    • 84940771125 scopus 로고    scopus 로고
    • Human Non-neutralizing HIV-1 Envelope Monoclonal Antibodies Limit the Number of Founder Viruses during SHIV Mucosal Infection in Rhesus Macaques
    • Santra, S., Tomaras, G.D., Warrier, R., Nicely, N.I., Liao, H.-X., Pollara, J., Liu, P., Alam, S.M., Zhang, R., Cocklin, S.L., et al. Human Non-neutralizing HIV-1 Envelope Monoclonal Antibodies Limit the Number of Founder Viruses during SHIV Mucosal Infection in Rhesus Macaques. PLoS Pathog., 11, 2015, e1005042.
    • (2015) PLoS Pathog. , vol.11 , pp. e1005042
    • Santra, S.1    Tomaras, G.D.2    Warrier, R.3    Nicely, N.I.4    Liao, H.-X.5    Pollara, J.6    Liu, P.7    Alam, S.M.8    Zhang, R.9    Cocklin, S.L.10
  • 69
    • 84888990148 scopus 로고    scopus 로고
    • Protective antiviral antibodies that lack neutralizing activity: precedents and evolution of concepts
    • Schmaljohn, A.L., Protective antiviral antibodies that lack neutralizing activity: precedents and evolution of concepts. Curr. HIV Res. 11 (2013), 345–353.
    • (2013) Curr. HIV Res. , vol.11 , pp. 345-353
    • Schmaljohn, A.L.1
  • 70
    • 84990820131 scopus 로고    scopus 로고
    • Cell-targeting antibodies in immunity to Ebola
    • Schmaljohn, A., Lewis, G.K., Cell-targeting antibodies in immunity to Ebola. Pathog. Dis., 74, 2016, ftw021.
    • (2016) Pathog. Dis. , vol.74 , pp. ftw021
    • Schmaljohn, A.1    Lewis, G.K.2
  • 71
    • 33645788357 scopus 로고    scopus 로고
    • Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein
    • Schornberg, K., Matsuyama, S., Kabsch, K., Delos, S., Bouton, A., White, J., Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein. J. Virol. 80 (2006), 4174–4178.
    • (2006) J. Virol. , vol.80 , pp. 4174-4178
    • Schornberg, K.1    Matsuyama, S.2    Kabsch, K.3    Delos, S.4    Bouton, A.5    White, J.6
  • 73
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • Shields, R.L., Lai, J., Keck, R., O'Connell, L.Y., Hong, K., Meng, Y.G., Weikert, S.H.A., Presta, L.G., Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 277 (2002), 26733–26740.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Meng, Y.G.6    Weikert, S.H.A.7    Presta, L.G.8
  • 74
    • 63849240274 scopus 로고    scopus 로고
    • Rapid generation of fully human monoclonal antibodies specific to a vaccinating antigen
    • Smith, K., Garman, L., Wrammert, J., Zheng, N.-Y., Capra, J.D., Ahmed, R., Wilson, P.C., Rapid generation of fully human monoclonal antibodies specific to a vaccinating antigen. Nat. Protoc. 4 (2009), 372–384.
    • (2009) Nat. Protoc. , vol.4 , pp. 372-384
    • Smith, K.1    Garman, L.2    Wrammert, J.3    Zheng, N.-Y.4    Capra, J.D.5    Ahmed, R.6    Wilson, P.C.7
  • 75
    • 64749097604 scopus 로고    scopus 로고
    • Correlates of protective immunity for Ebola vaccines: implications for regulatory approval by the animal rule
    • Sullivan, N.J., Martin, J.E., Graham, B.S., Nabel, G.J., Correlates of protective immunity for Ebola vaccines: implications for regulatory approval by the animal rule. Nat. Rev. Microbiol. 7 (2009), 393–400.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 393-400
    • Sullivan, N.J.1    Martin, J.E.2    Graham, B.S.3    Nabel, G.J.4
  • 76
    • 0037229321 scopus 로고    scopus 로고
    • Identification of protective epitopes on ebola virus glycoprotein at the single amino acid level by using recombinant vesicular stomatitis viruses
    • Takada, A., Feldmann, H., Stroeher, U., Bray, M., Watanabe, S., Ito, H., McGregor, M., Kawaoka, Y., Identification of protective epitopes on ebola virus glycoprotein at the single amino acid level by using recombinant vesicular stomatitis viruses. J. Virol. 77 (2003), 1069–1074.
    • (2003) J. Virol. , vol.77 , pp. 1069-1074
    • Takada, A.1    Feldmann, H.2    Stroeher, U.3    Bray, M.4    Watanabe, S.5    Ito, H.6    McGregor, M.7    Kawaoka, Y.8
  • 77
    • 0029589329 scopus 로고
    • GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases
    • Volchkov, V.E., Becker, S., Volchkova, V.A., Ternovoj, V.A., Kotov, A.N., Netesov, S.V., Klenk, H.D., GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases. Virology 214 (1995), 421–430.
    • (1995) Virology , vol.214 , pp. 421-430
    • Volchkov, V.E.1    Becker, S.2    Volchkova, V.A.3    Ternovoj, V.A.4    Kotov, A.N.5    Netesov, S.V.6    Klenk, H.D.7
  • 82
    • 72849133481 scopus 로고    scopus 로고
    • A forward genetic strategy reveals destabilizing mutations in the Ebolavirus glycoprotein that alter its protease dependence during cell entry
    • Wong, A.C., Sandesara, R.G., Mulherkar, N., Whelan, S.P., Chandran, K., A forward genetic strategy reveals destabilizing mutations in the Ebolavirus glycoprotein that alter its protease dependence during cell entry. J. Virol. 84 (2010), 163–175.
    • (2010) J. Virol. , vol.84 , pp. 163-175
    • Wong, A.C.1    Sandesara, R.G.2    Mulherkar, N.3    Whelan, S.P.4    Chandran, K.5
  • 84
    • 85019650530 scopus 로고    scopus 로고
    • Immunization-Elicited Broadly Protective Antibody Reveals Ebolavirus Fusion Loop as a Site of Vulnerability
    • Zhao, X., Howell, K.A., He, S., Brannan, J.M., Wec, A.Z., Davidson, E., Turner, H.L., Chiang, C.-I., Lei, L., Fels, J.M., et al. Immunization-Elicited Broadly Protective Antibody Reveals Ebolavirus Fusion Loop as a Site of Vulnerability. Cell 169 (2017), 891–904.e15.
    • (2017) Cell , vol.169 , pp. 891-904.e15
    • Zhao, X.1    Howell, K.A.2    He, S.3    Brannan, J.M.4    Wec, A.Z.5    Davidson, E.6    Turner, H.L.7    Chiang, C.-I.8    Lei, L.9    Fels, J.M.10
  • 85
    • 16244401458 scopus 로고    scopus 로고
    • Regularization and variable selection via the elastic net
    • Zou, H., Hastie, T., Regularization and variable selection via the elastic net. J. R. Stat. Soc. Series B Stat. Methodol. 67 (2005), 301–320.
    • (2005) J. R. Stat. Soc. Series B Stat. Methodol. , vol.67 , pp. 301-320
    • Zou, H.1    Hastie, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.