메뉴 건너뛰기




Volumn 2013, Issue , 2013, Pages

Multiantibody strategies for HIV

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; MICROBICIDE; MONOCLONAL ANTIBODY; ANTIVIRUS AGENT; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; NEUTRALIZING ANTIBODY; VIRUS ANTIGEN;

EID: 84879290712     PISSN: 17402522     EISSN: 17402530     Source Type: Journal    
DOI: 10.1155/2013/632893     Document Type: Review
Times cited : (8)

References (141)
  • 1
    • 44049108744 scopus 로고    scopus 로고
    • Toward an AIDS vaccine
    • 2-s2.0-44049108744 10.1126/science.1152622
    • Walker B. D., Burton D. R., Toward an AIDS vaccine. Science 2008 320 5877 760 764 2-s2.0-44049108744 10.1126/science.1152622
    • (2008) Science , vol.320 , Issue.5877 , pp. 760-764
    • Walker, B.D.1    Burton, D.R.2
  • 4
    • 53349160053 scopus 로고    scopus 로고
    • Challenges in the development of an HIV-1 vaccine
    • Barouch D. H., Challenges in the development of an HIV-1 vaccine. Nature 2008 455 613 619
    • (2008) Nature , vol.455 , pp. 613-619
    • Barouch, D.H.1
  • 5
  • 6
    • 0032503029 scopus 로고    scopus 로고
    • Viral strategies of immune evasion
    • 2-s2.0-0032503029 10.1126/science.280.5361.248
    • Ploegh H. L., Viral strategies of immune evasion. Science 1998 280 5361 248 253 2-s2.0-0032503029 10.1126/science.280.5361.248
    • (1998) Science , vol.280 , Issue.5361 , pp. 248-253
    • Ploegh, H.L.1
  • 8
    • 0036449295 scopus 로고    scopus 로고
    • Viral immune evasion: A masterpiece of evolution
    • 2-s2.0-0036449295 10.1007/s00251-002-0493-1
    • Vossen M. T. M., Westerhout E. M., Söderberg-Nauclér C., Wiertz E. J. H. J., Viral immune evasion: a masterpiece of evolution. Immunogenetics 2002 54 8 527 542 2-s2.0-0036449295 10.1007/s00251-002-0493-1
    • (2002) Immunogenetics , vol.54 , Issue.8 , pp. 527-542
    • Vossen, M.T.M.1    Westerhout, E.M.2    Söderberg-Nauclér, C.3    Wiertz, E.J.H.J.4
  • 9
    • 0033934327 scopus 로고    scopus 로고
    • Hepatitis C virus: Evasion of the interferon-induced antiviral response
    • 2-s2.0-0033934327
    • Taylor D. R., Hepatitis C virus: evasion of the interferon-induced antiviral response. Journal of Molecular Medicine 2000 78 4 182 190 2-s2.0-0033934327
    • (2000) Journal of Molecular Medicine , vol.78 , Issue.4 , pp. 182-190
    • Taylor, D.R.1
  • 11
    • 0032055774 scopus 로고    scopus 로고
    • Nef interacts with the subunit of clathrin adaptor complexes and reveals a cryptic sorting signal in MHC i molecules
    • 2-s2.0-0032055774 10.1016/S1074-7613(00)80553-1
    • Le Gall S., Erdtmann L., Benichou S., Berlioz-Torrent C., Liu L., Benarous R., Heard J. M., Schwartz O., Nef interacts with the subunit of clathrin adaptor complexes and reveals a cryptic sorting signal in MHC I molecules. Immunity 1998 8 4 483 495 2-s2.0-0032055774 10.1016/S1074-7613(00) 80553-1
    • (1998) Immunity , vol.8 , Issue.4 , pp. 483-495
    • Le Gall, S.1    Erdtmann, L.2    Benichou, S.3    Berlioz-Torrent, C.4    Liu, L.5    Benarous, R.6    Heard, J.M.7    Schwartz, O.8
  • 12
    • 0036146227 scopus 로고    scopus 로고
    • Nef-mediated resistance of human immunodeficiency virus type 1 to antiviral cytotoxic T lymphocytes
    • 2-s2.0-0036146227 10.1128/JVI.76.4.1626-1631.2002
    • Yang O. O., Nguyen P. T., Kalams S. A., Dorfman T., Göttlinger H. G., Stewart S., Chen I. S. Y., Threlkeld S., Walker B. D., Nef-mediated resistance of human immunodeficiency virus type 1 to antiviral cytotoxic T lymphocytes. Journal of Virology 2002 76 4 1626 1631 2-s2.0-0036146227 10.1128/JVI.76.4.1626-1631.2002
    • (2002) Journal of Virology , vol.76 , Issue.4 , pp. 1626-1631
    • Yang, O.O.1    Nguyen, P.T.2    Kalams, S.A.3    Dorfman, T.4    Göttlinger, H.G.5    Stewart, S.6    Chen, I.S.Y.7    Threlkeld, S.8    Walker, B.D.9
  • 13
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • 2-s2.0-0032546844 10.1126/science.280.5371.1884
    • Wyatt R., Sodroski J., The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 1998 280 5371 1884 1888 2-s2.0-0032546844 10.1126/science.280.5371.1884
    • (1998) Science , vol.280 , Issue.5371 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 15
    • 0035162494 scopus 로고    scopus 로고
    • Evolutionary and immunological implications of contemporary HIV-1 variation
    • 2-s2.0-0035162494 10.1093/bmb/58.1.19
    • Korber B., Gaschen B., Yusim K., Thakallapally R., Kesmir C., Detours V., Evolutionary and immunological implications of contemporary HIV-1 variation. British Medical Bulletin 2001 58 19 42 2-s2.0-0035162494 10.1093/bmb/58.1.19
    • (2001) British Medical Bulletin , vol.58 , pp. 19-42
    • Korber, B.1    Gaschen, B.2    Yusim, K.3    Thakallapally, R.4    Kesmir, C.5    Detours, V.6
  • 16
    • 78649820026 scopus 로고    scopus 로고
    • How innate immune mechanisms contribute to antibody-enhanced viral infections
    • 2-s2.0-78649820026 10.1128/CVI.00316-10
    • Ubol S., Halstead S. B., How innate immune mechanisms contribute to antibody-enhanced viral infections. Clinical and Vaccine Immunology 2010 17 12 1829 1835 2-s2.0-78649820026 10.1128/CVI.00316-10
    • (2010) Clinical and Vaccine Immunology , vol.17 , Issue.12 , pp. 1829-1835
    • Ubol, S.1    Halstead, S.B.2
  • 17
    • 70450162452 scopus 로고    scopus 로고
    • Identification and characterization of broadly neutralizing human monoclonal antibodies directed against the E2 envelope glycoprotein of hepatitis C virus
    • 2-s2.0-70450162452 10.1128/JVI.01138-09
    • Broering T. J., Garrity K. A., Boatright N. K., Sloan S. E., Sandor F., Thomas W. D., Szabo G., Finberg R. W., Ambrosino D. M., Babcock G. J., Identification and characterization of broadly neutralizing human monoclonal antibodies directed against the E2 envelope glycoprotein of hepatitis C virus. Journal of Virology 2009 83 23 12473 12482 2-s2.0-70450162452 10.1128/JVI.01138-09
    • (2009) Journal of Virology , vol.83 , Issue.23 , pp. 12473-12482
    • Broering, T.J.1    Garrity, K.A.2    Boatright, N.K.3    Sloan, S.E.4    Sandor, F.5    Thomas, W.D.6    Szabo, G.7    Finberg, R.W.8    Ambrosino, D.M.9    Babcock, G.J.10
  • 19
    • 37849016609 scopus 로고    scopus 로고
    • Identification of a broadly cross-reacting and neutralizing human monoclonal antibody directed against the hepatitis C virus E2 protein
    • 2-s2.0-37849016609 10.1128/JVI.01986-07
    • Perotti M., Mancini N., Diotti R. A., Tarr A. W., Ball J. K., Owsianka A., Adair R., Patel A. H., Clementi M., Burioni R., Identification of a broadly cross-reacting and neutralizing human monoclonal antibody directed against the hepatitis C virus E2 protein. Journal of Virology 2008 82 2 1047 1052 2-s2.0-37849016609 10.1128/JVI.01986-07
    • (2008) Journal of Virology , vol.82 , Issue.2 , pp. 1047-1052
    • Perotti, M.1    Mancini, N.2    Diotti, R.A.3    Tarr, A.W.4    Ball, J.K.5    Owsianka, A.6    Adair, R.7    Patel, A.H.8    Clementi, M.9    Burioni, R.10
  • 21
    • 82155199162 scopus 로고    scopus 로고
    • Affinity maturation to improve human monoclonal antibody neutralization potency and breadth against hepatitis C virus
    • Wang Y., Keck Z. Y., Saha A., Affinity maturation to improve human monoclonal antibody neutralization potency and breadth against hepatitis C virus. Journal of Biological Chemistry 2011 286 44218 44233
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 44218-44233
    • Wang, Y.1    Keck, Z.Y.2    Saha, A.3
  • 22
    • 79960485199 scopus 로고    scopus 로고
    • Neutralizing monoclonal antibodies against hepatitis C virus E2 protein bind discontinuous epitopes and inhibit infection at a postattachment step
    • Sabo M. C., Luca V. C., Prentoe J., Neutralizing monoclonal antibodies against hepatitis C virus E2 protein bind discontinuous epitopes and inhibit infection at a postattachment step. Journal of Virology 2011 85 7005 7019
    • (2011) Journal of Virology , vol.85 , pp. 7005-7019
    • Sabo, M.C.1    Luca, V.C.2    Prentoe, J.3
  • 26
    • 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
    • e1002653
    • Keck Z. Y., Xia J., Wang Y., Human monoclonal antibodies to a novel cluster of conformational epitopes on HCV E2 with resistance to neutralization escape in a genotype 2a isolate. PLOS Pathogens 2012 8 e1002653
    • (2012) PLOS Pathogens , vol.8
    • Keck, Z.Y.1    Xia, J.2    Wang, Y.3
  • 27
    • 17944375718 scopus 로고    scopus 로고
    • Nonneutralizing human antibody fragments against hepatitis C virus E2 glycoprotein modulate neutralization of binding activity of human recombinant Fabs
    • 2-s2.0-17944375718 10.1006/viro.2001.1014
    • Burioni R., Bugli F., Mancini N., Rosa D., Di Campli C., Moroncini G., Manzin A., Abrignani S., Varaldo P. E., Clementi M., Fadda G., Nonneutralizing human antibody fragments against hepatitis C virus E2 glycoprotein modulate neutralization of binding activity of human recombinant Fabs. Virology 2001 288 1 29 35 2-s2.0-17944375718 10.1006/viro.2001.1014
    • (2001) Virology , vol.288 , Issue.1 , pp. 29-35
    • Burioni, R.1    Bugli, F.2    Mancini, N.3    Rosa, D.4    Di Campli, C.5    Moroncini, G.6    Manzin, A.7    Abrignani, S.8    Varaldo, P.E.9    Clementi, M.10    Fadda, G.11
  • 29
    • 0036827644 scopus 로고    scopus 로고
    • Diverging effects of human recombinant anti-hepatitis C virus (HCV) antibody fragments derived from a single patient on the infectivity of a vesicular stomatitis virus/HCV pseudotype
    • 2-s2.0-0036827644 10.1128/JVI.76.22.11775-11779.2002
    • Burioni R., Matsuura Y., Mancini N., Tani H., Miyamura T., Varaldo P. E., Clementi M., Diverging effects of human recombinant anti-hepatitis C virus (HCV) antibody fragments derived from a single patient on the infectivity of a vesicular stomatitis virus/HCV pseudotype. Journal of Virology 2002 76 22 11775 11779 2-s2.0-0036827644 10.1128/JVI.76.22.11775-11779.2002
    • (2002) Journal of Virology , vol.76 , Issue.22 , pp. 11775-11779
    • Burioni, R.1    Matsuura, Y.2    Mancini, N.3    Tani, H.4    Miyamura, T.5    Varaldo, P.E.6    Clementi, M.7
  • 31
    • 4544331326 scopus 로고    scopus 로고
    • Cross-reactive pseudovirus-neutralizing anti-envelope antibodies coexist with antibodies devoid of such activity in persistent hepatitis C virus infection
    • 2-s2.0-4544331326 10.1016/j.virol.2004.06.042
    • Burioni R., Mancini N., Carletti S., Perotti M., Grieco A., Canducci F., Varaldo P. E., Clementi M., Cross-reactive pseudovirus-neutralizing anti-envelope antibodies coexist with antibodies devoid of such activity in persistent hepatitis C virus infection. Virology 2004 327 2 242 248 2-s2.0-4544331326 10.1016/j.virol.2004.06.042
    • (2004) Virology , vol.327 , Issue.2 , pp. 242-248
    • Burioni, R.1    Mancini, N.2    Carletti, S.3    Perotti, M.4    Grieco, A.5    Canducci, F.6    Varaldo, P.E.7    Clementi, M.8
  • 33
    • 82155191729 scopus 로고    scopus 로고
    • Hepatitis C virus evasion mechanisms from neutralizing antibodies
    • Di Lorenzo C., Angus A. G., Patel A. H., Hepatitis C virus evasion mechanisms from neutralizing antibodies. Viruses 2011 3 2280 2300
    • (2011) Viruses , vol.3 , pp. 2280-2300
    • Di Lorenzo, C.1    Angus, A.G.2    Patel, A.H.3
  • 34
    • 79961108533 scopus 로고    scopus 로고
    • Neutralizing activities of caprine antibodies towards conserved regions of the HCV envelope glycoprotein E2
    • El Abd Y. S., Tabll A. A., El Din N. G., Neutralizing activities of caprine antibodies towards conserved regions of the HCV envelope glycoprotein E2. Virology Journal 2011 8, article 391
    • (2011) Virology Journal , vol.8391
    • El Abd, Y.S.1    Tabll, A.A.2    El Din, N.G.3
  • 35
    • 84865477865 scopus 로고    scopus 로고
    • Anti-hepatitis C virus E2 (HCV/E2) glycoprotein monoclonal antibodies and neutralization interference
    • Sautto G., Mancini N., Diotti R. A., Solforosi L., Clementi M., Burioni R., Anti-hepatitis C virus E2 (HCV/E2) glycoprotein monoclonal antibodies and neutralization interference. Antiviral Research 2012 96 82 89
    • (2012) Antiviral Research , vol.96 , pp. 82-89
    • Sautto, G.1    Mancini, N.2    Diotti, R.A.3    Solforosi, L.4    Clementi, M.5    Burioni, R.6
  • 36
    • 79960835805 scopus 로고    scopus 로고
    • Immunity to dengue virus: A tale of original antigenic sin and tropical cytokine storms
    • 2-s2.0-79960835805 10.1038/nri3014
    • Rothman A. L., Immunity to dengue virus: a tale of original antigenic sin and tropical cytokine storms. Nature Reviews Immunology 2011 11 8 532 543 2-s2.0-79960835805 10.1038/nri3014
    • (2011) Nature Reviews Immunology , vol.11 , Issue.8 , pp. 532-543
    • Rothman, A.L.1
  • 37
    • 4644285658 scopus 로고    scopus 로고
    • Avoiding deceptive imprinting of the immune response to HIV-1 infection in vaccine development
    • 2-s2.0-4644285658 10.1080/08830180490432802
    • Muller S., Avoiding deceptive imprinting of the immune response to HIV-1 infection in vaccine development. International Reviews of Immunology 2004 23 5-6 423 436 2-s2.0-4644285658 10.1080/08830180490432802
    • (2004) International Reviews of Immunology , vol.23 , Issue.5-6 , pp. 423-436
    • Muller, S.1
  • 38
    • 79953035293 scopus 로고    scopus 로고
    • Immune response to dengue virus and prospects for a vaccine
    • Murphy B. R., Whitehead S. S., Immune response to dengue virus and prospects for a vaccine. Annual Review of Immunology 2011 29 587 619
    • (2011) Annual Review of Immunology , vol.29 , pp. 587-619
    • Murphy, B.R.1    Whitehead, S.S.2
  • 39
    • 84868211668 scopus 로고    scopus 로고
    • Protective efficacy of the recombinant, live-attenuated CYD tetravalent dengue vaccine in Thai schoolchildren: A randomised, controlled phase 2b trial
    • Sabchareon A., Wallace D., Sirivichayakul C., Protective efficacy of the recombinant, live-attenuated CYD tetravalent dengue vaccine in Thai schoolchildren: a randomised, controlled phase 2b trial. Lancet 2012 380 9853 1559 1567
    • (2012) Lancet , vol.380 , Issue.9853 , pp. 1559-1567
    • Sabchareon, A.1    Wallace, D.2    Sirivichayakul, C.3
  • 40
    • 82955194795 scopus 로고    scopus 로고
    • A human monoclonal antibody with neutralizing activity against highly divergent influenza subtypes
    • e28001
    • Clementi N., De Marco D., Mancini N., A human monoclonal antibody with neutralizing activity against highly divergent influenza subtypes. PLoS ONE 2011 6 e28001
    • (2011) PLoS ONE , vol.6
    • Clementi, N.1    De Marco, D.2    Mancini, N.3
  • 42
    • 0036441307 scopus 로고    scopus 로고
    • Mechanism of neutralization of influenza virus infectivity by antibodies
    • 2-s2.0-0036441307 10.1006/viro.2002.1625
    • Knossow M., Gaudier M., Douglas A., Barrère B., Bizebard T., Barbey C., Gigant B., Skehel J. J., Mechanism of neutralization of influenza virus infectivity by antibodies. Virology 2002 302 2 294 298 2-s2.0-0036441307 10.1006/viro.2002.1625
    • (2002) Virology , vol.302 , Issue.2 , pp. 294-298
    • Knossow, M.1    Gaudier, M.2    Douglas, A.3    Barrère, B.4    Bizebard, T.5    Barbey, C.6    Gigant, B.7    Skehel, J.J.8
  • 43
    • 84859364851 scopus 로고    scopus 로고
    • A non-VH1-69 heterosubtypic neutralizing human monoclonal antibody protects mice against H1N1 and H5N1 viruses
    • e34415
    • De Marco D., Clementi N., Mancini N., A non-VH1-69 heterosubtypic neutralizing human monoclonal antibody protects mice against H1N1 and H5N1 viruses. PLoS ONE 2012 7 e34415
    • (2012) PLoS ONE , vol.7
    • De Marco, D.1    Clementi, N.2    Mancini, N.3
  • 44
    • 77049088439 scopus 로고    scopus 로고
    • Monoclonal antibodies isolated from human B cells neutralize a broad range of H1 subtype influenza A viruses including swine-origin Influenza virus (S-OIV)
    • 2-s2.0-77049088439 10.1016/j.virol.2009.12.014
    • Burioni R., Canducci F., Mancini N., Clementi N., Sassi M., De Marco D., Diotti R. A., Saita D., Sampaolo M., Sautto G., Pianezze M., Clementi M., Monoclonal antibodies isolated from human B cells neutralize a broad range of H1 subtype influenza A viruses including swine-origin Influenza virus (S-OIV). Virology 2010 399 1 144 152 2-s2.0-77049088439 10.1016/j.virol.2009.12.014
    • (2010) Virology , vol.399 , Issue.1 , pp. 144-152
    • Burioni, R.1    Canducci, F.2    Mancini, N.3    Clementi, N.4    Sassi, M.5    De Marco, D.6    Diotti, R.A.7    Saita, D.8    Sampaolo, M.9    Sautto, G.10    Pianezze, M.11    Clementi, M.12
  • 45
    • 84863558273 scopus 로고    scopus 로고
    • High titer and avidity of nonneutralizing antibodies against influenza vaccine antigen are associated with severe influenza
    • To K. K., Zhang A. J., Hung I. F., High titer and avidity of nonneutralizing antibodies against influenza vaccine antigen are associated with severe influenza. Clinical and Vaccine Immunology 2012 19 1012 1018
    • (2012) Clinical and Vaccine Immunology , vol.19 , pp. 1012-1018
    • To, K.K.1    Zhang, A.J.2    Hung, I.F.3
  • 46
    • 79251550432 scopus 로고    scopus 로고
    • Identification of novel conserved functional motifs across most Influenza A viral strains
    • 2-s2.0-79251550432 10.1186/1743-422X-8-44
    • Elhefnawi M., Alaidi O., Mohamed N., Kamar M., El-Azab I., Zada S., Siam R., Identification of novel conserved functional motifs across most Influenza A viral strains. Virology Journal 2011 8, article 44 2-s2.0-79251550432 10.1186/1743-422X-8-44
    • (2011) Virology Journal , vol.844
    • Elhefnawi, M.1    Alaidi, O.2    Mohamed, N.3    Kamar, M.4    El-Azab, I.5    Zada, S.6    Siam, R.7
  • 47
    • 84864530741 scopus 로고    scopus 로고
    • A phage display vector optimized for the generation of human antibody combinatorial libraries and the molecular cloning of monoclonal antibody fragments
    • Solforosi L., Mancini N., Canducci F., A phage display vector optimized for the generation of human antibody combinatorial libraries and the molecular cloning of monoclonal antibody fragments. New Microbiologica 2012 35 289 294
    • (2012) New Microbiologica , vol.35 , pp. 289-294
    • Solforosi, L.1    Mancini, N.2    Canducci, F.3
  • 48
    • 66649100756 scopus 로고    scopus 로고
    • Differential neutralization efficiency of hemagglutinin epitopes, antibody interference, and the design of influenza vaccines
    • 2-s2.0-66649100756 10.1073/pnas.0903427106
    • Ndifon W., Wingreen N. S., Levin S. A., Differential neutralization efficiency of hemagglutinin epitopes, antibody interference, and the design of influenza vaccines. Proceedings of the National Academy of Sciences of the United States of America 2009 106 21 8701 8706 2-s2.0-66649100756 10.1073/pnas.0903427106
    • (2009) Proceedings of the National Academy of Sciences of the United States of America , vol.106 , Issue.21 , pp. 8701-8706
    • Ndifon, W.1    Wingreen, N.S.2    Levin, S.A.3
  • 49
    • 33645235641 scopus 로고    scopus 로고
    • A recombinant baculovirus-expressed S glycoprotein vaccine elicits high titers of SARS-associated coronavirus (SARS-CoV) neutralizing antibodies in mice
    • 2-s2.0-33645235641 10.1016/j.vaccine.2006.01.059
    • Zhou Z., Post P., Chubet R., Holtz K., McPherson C., Petric M., Cox M., A recombinant baculovirus-expressed S glycoprotein vaccine elicits high titers of SARS-associated coronavirus (SARS-CoV) neutralizing antibodies in mice. Vaccine 2006 24 17 3624 3631 2-s2.0-33645235641 10.1016/j.vaccine.2006.01.059
    • (2006) Vaccine , vol.24 , Issue.17 , pp. 3624-3631
    • Zhou, Z.1    Post, P.2    Chubet, R.3    Holtz, K.4    McPherson, C.5    Petric, M.6    Cox, M.7
  • 50
    • 28544437130 scopus 로고    scopus 로고
    • Immunopathogenesis of coronavirus infections: Implications for SARS
    • 2-s2.0-28544437130 10.1038/nri1732
    • Perlman S., Dandekar A. A., Immunopathogenesis of coronavirus infections: implications for SARS. Nature Reviews Immunology 2005 5 12 917 927 2-s2.0-28544437130 10.1038/nri1732
    • (2005) Nature Reviews Immunology , vol.5 , Issue.12 , pp. 917-927
    • Perlman, S.1    Dandekar, A.A.2
  • 51
    • 70449697853 scopus 로고    scopus 로고
    • Antibody-mediated synergy and interference in the neutralization of SARS-CoV at an epitope cluster on the spike protein
    • 2-s2.0-70449697853 10.1016/j.bbrc.2009.10.115
    • Zhong L., Haynes L., Struble E. B., Tamin A., Virata-Theimer M. L., Zhang P., Antibody-mediated synergy and interference in the neutralization of SARS-CoV at an epitope cluster on the spike protein. Biochemical and Biophysical Research Communications 2009 390 3 1056 1060 2-s2.0-70449697853 10.1016/j.bbrc.2009.10.115
    • (2009) Biochemical and Biophysical Research Communications , vol.390 , Issue.3 , pp. 1056-1060
    • Zhong, L.1    Haynes, L.2    Struble, E.B.3    Tamin, A.4    Virata-Theimer, M.L.5    Zhang, P.6
  • 53
    • 84855678360 scopus 로고    scopus 로고
    • Neutralizing human monoclonal antibodies to severe acute respiratory syndrome coronavirus: Target, mechanism of action, and therapeutic potential
    • Coughlin M. M., Prabhakar B. S., Neutralizing human monoclonal antibodies to severe acute respiratory syndrome coronavirus: target, mechanism of action, and therapeutic potential. Reviews in Medical Virology 2012 22 2 17
    • (2012) Reviews in Medical Virology , vol.22 , pp. 2-17
    • Coughlin, M.M.1    Prabhakar, B.S.2
  • 56
    • 60849133898 scopus 로고    scopus 로고
    • Dynamic features of the selective pressure on the human immunodeficiency virus type 1 (HIV-1) gp120 CD4-binding site in a group of long term non progressor (LTNP) subjects
    • 2-s2.0-60849133898 10.1186/1742-4690-6-4
    • Canducci F., Marinozzi M. C., Sampaolo M., Berrè S., Bagnarelli P., Degano M., Gallotta G., Mazzi B., Lemey P., Burioni R., Clementi M., Dynamic features of the selective pressure on the human immunodeficiency virus type 1 (HIV-1) gp120 CD4-binding site in a group of long term non progressor (LTNP) subjects. Retrovirology 2009 6, article 4 2-s2.0-60849133898 10.1186/1742-4690-6-4
    • (2009) Retrovirology , vol.64
    • Canducci, F.1    Marinozzi, M.C.2    Sampaolo, M.3    Berrè, S.4    Bagnarelli, P.5    Degano, M.6    Gallotta, G.7    Mazzi, B.8    Lemey, P.9    Burioni, R.10    Clementi, M.11
  • 57
    • 0035202616 scopus 로고    scopus 로고
    • Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies
    • 2-s2.0-0035202616 10.1128/JVI.75.24.12198-12208.2001
    • Zwick M. B., Wang M., Poignard P., Stiegler G., Katinger H., Burton D. R., Parren P. W. H. I., Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies. Journal of Virology 2001 75 24 12198 12208 2-s2.0-0035202616 10.1128/JVI.75.24.12198- 12208.2001
    • (2001) Journal of Virology , vol.75 , Issue.24 , pp. 12198-12208
    • Zwick, M.B.1    Wang, M.2    Poignard, P.3    Stiegler, G.4    Katinger, H.5    Burton, D.R.6    Parren, P.W.H.I.7
  • 58
    • 0028001866 scopus 로고
    • Combination effect on HIV infection in vitro of soluble CD4 and HIV-neutralizing antibodies
    • 2-s2.0-0028001866
    • Hansen J. E. S., Sorensen A. M., Olofsson S., Osinaga E., Roseto A., Combination effect on HIV infection in vitro of soluble CD4 and HIV-neutralizing antibodies. Archives of Virology 1994 134 1-2 179 184 2-s2.0-0028001866
    • (1994) Archives of Virology , vol.134 , Issue.1-2 , pp. 179-184
    • Hansen, J.E.S.1    Sorensen, A.M.2    Olofsson, S.3    Osinaga, E.4    Roseto, A.5
  • 59
    • 0034856156 scopus 로고    scopus 로고
    • Additive effects characterize the interaction of antibodies involved in neutralization of the primary dualtropic human immunodeficiency virus type 1 isolate 89.6
    • 2-s2.0-0034856156 10.1128/JVI.75.19.9177-9186.2001
    • Verrier F., Nádas A., Gorny M. K., Zolla-Pazner S., Additive effects characterize the interaction of antibodies involved in neutralization of the primary dualtropic human immunodeficiency virus type 1 isolate 89.6. Journal of Virology 2001 75 19 9177 9186 2-s2.0-0034856156 10.1128/JVI.75.19. 9177-9186.2001
    • (2001) Journal of Virology , vol.75 , Issue.19 , pp. 9177-9186
    • Verrier, F.1    Nádas, A.2    Gorny, M.K.3    Zolla-Pazner, S.4
  • 60
    • 65449174955 scopus 로고    scopus 로고
    • Oligomer-specific conformations of the Human Immunodeficiency Virus (HIV-1) gp41 envelope glycoprotein ectodomain recognized by human monoclonal antibodies
    • 2-s2.0-65449174955 10.1089/aid.2008.0213
    • Yuan W., Li X., Kasterka M., Gorny M. K., Zolla-Pazner S., Sodroski J., Oligomer-specific conformations of the Human Immunodeficiency Virus (HIV-1) gp41 envelope glycoprotein ectodomain recognized by human monoclonal antibodies. AIDS Research and Human Retroviruses 2009 25 3 319 328 2-s2.0-65449174955 10.1089/aid.2008.0213
    • (2009) AIDS Research and Human Retroviruses , vol.25 , Issue.3 , pp. 319-328
    • Yuan, W.1    Li, X.2    Kasterka, M.3    Gorny, M.K.4    Zolla-Pazner, S.5    Sodroski, J.6
  • 61
    • 78651388412 scopus 로고    scopus 로고
    • Nonneutralizing HIV-1 gp41 envelope cluster II human monoclonal antibodies show polyreactivity for binding to phospholipids and protein autoantigens
    • 2-s2.0-78651388412 10.1128/JVI.01680-10
    • Dennison S. M., Anasti K., Scearce R. M., Sutherland L., Parks R., Xia S. M., Liao H. X., Gorny M. K., Zolla-Pazner S., Haynes B. F., Alam S. M., Nonneutralizing HIV-1 gp41 envelope cluster II human monoclonal antibodies show polyreactivity for binding to phospholipids and protein autoantigens. Journal of Virology 2011 85 3 1340 1347 2-s2.0-78651388412 10.1128/JVI.01680-10
    • (2011) Journal of Virology , vol.85 , Issue.3 , pp. 1340-1347
    • Dennison, S.M.1    Anasti, K.2    Scearce, R.M.3    Sutherland, L.4    Parks, R.5    Xia, S.M.6    Liao, H.X.7    Gorny, M.K.8    Zolla-Pazner, S.9    Haynes, B.F.10    Alam, S.M.11
  • 62
    • 0034046091 scopus 로고    scopus 로고
    • Recognition by human monoclonal antibodies of free and complexed peptides representing the prefusogenic and fusogenic forms of human immunodeficiency virus type 1 gp41
    • 2-s2.0-0034046091 10.1128/JVI.74.13.6186-6192.2000
    • Gorny M. K., Zolla-Pazner S., Recognition by human monoclonal antibodies of free and complexed peptides representing the prefusogenic and fusogenic forms of human immunodeficiency virus type 1 gp41. Journal of Virology 2000 74 13 6186 6192 2-s2.0-0034046091 10.1128/JVI.74.13.6186-6192.2000
    • (2000) Journal of Virology , vol.74 , Issue.13 , pp. 6186-6192
    • Gorny, M.K.1    Zolla-Pazner, S.2
  • 64
    • 84865483379 scopus 로고    scopus 로고
    • Natalizumab-associated progressive multifocal leukoencephalopathy
    • Mancini N., Clementi M., Burioni R., Natalizumab-associated progressive multifocal leukoencephalopathy. New England Journal of Medicine 2012 367 871 872
    • (2012) New England Journal of Medicine , vol.367 , pp. 871-872
    • Mancini, N.1    Clementi, M.2    Burioni, R.3
  • 67
    • 17644379940 scopus 로고    scopus 로고
    • Antigen-specific memory B cell development
    • 2-s2.0-17644379940 10.1146/annurev.immunol.23.021704.115732
    • McHeyzer-Williams L. J., McHeyzer-Williams M. G., Antigen-specific memory B cell development. Annual Review of Immunology 2005 23 487 513 2-s2.0-17644379940 10.1146/annurev.immunol.23.021704.115732
    • (2005) Annual Review of Immunology , vol.23 , pp. 487-513
    • McHeyzer-Williams, L.J.1    McHeyzer-Williams, M.G.2
  • 68
    • 0026060620 scopus 로고
    • Intraclonal generation of antibody mutants in germinal centres
    • 2-s2.0-0026060620 10.1038/354389a0
    • Jacob J., Kelsoe G., Rajewsky K., Weiss U., Intraclonal generation of antibody mutants in germinal centres. Nature 1991 354 6352 389 392 2-s2.0-0026060620 10.1038/354389a0
    • (1991) Nature , vol.354 , Issue.6352 , pp. 389-392
    • Jacob, J.1    Kelsoe, G.2    Rajewsky, K.3    Weiss, U.4
  • 69
    • 0013935657 scopus 로고
    • Original antigenic sin in ferrets: The response to sequential infections with influenza viruses
    • 2-s2.0-0013935657
    • Webster R. G., Original antigenic sin in ferrets: the response to sequential infections with influenza viruses. Journal of Immunology 1966 97 2 177 183 2-s2.0-0013935657
    • (1966) Journal of Immunology , vol.97 , Issue.2 , pp. 177-183
    • Webster, R.G.1
  • 70
    • 0001147595 scopus 로고
    • Epidemiologic and immunologic significance of age distribution of antibody to antigenic variants of influenza virus
    • 2-s2.0-0001147595
    • Davenport F. M., Hennessy A. V., Francis T. Jr., Epidemiologic and immunologic significance of age distribution of antibody to antigenic variants of influenza virus. The Journal of Experimental Medicine 1953 98 6 641 656 2-s2.0-0001147595
    • (1953) The Journal of Experimental Medicine , vol.98 , Issue.6 , pp. 641-656
    • Davenport, F.M.1    Hennessy, A.V.2    Francis Jr., T.3
  • 72
    • 84960989501 scopus 로고
    • Influenza: The new acquaintance
    • Francis T. Jr., Influenza: the new acquaintance. Annals of Internal Medicine 1953 39 2 203 221
    • (1953) Annals of Internal Medicine , vol.39 , Issue.2 , pp. 203-221
    • Francis Jr., T.1
  • 74
    • 0036186079 scopus 로고    scopus 로고
    • Antibody convergence along a common idiotypic axis in immunodeficiency virus and hepatitis C virus infections
    • 2-s2.0-0036186079 10.1002/jmv.2105
    • Grant M. D., Antibody convergence along a common idiotypic axis in immunodeficiency virus and hepatitis C virus infections. Journal of Medical Virology 2002 66 1 13 21 2-s2.0-0036186079 10.1002/jmv.2105
    • (2002) Journal of Medical Virology , vol.66 , Issue.1 , pp. 13-21
    • Grant, M.D.1
  • 75
    • 22544457161 scopus 로고    scopus 로고
    • Dengue virus (DV) enhancing antibody activity in preillness plasma does not predict subsequent disease severity or viremia in secondary DV infection
    • 2-s2.0-22544457161 10.1086/431520
    • Laoprasopwattana K., Libraty D. H., Endy T. P., Nisalak A., Chunsuttiwat S., Vaughn D. W., Reed G., Ennis F. A., Rothman A. L., Green S., Dengue virus (DV) enhancing antibody activity in preillness plasma does not predict subsequent disease severity or viremia in secondary DV infection. Journal of Infectious Diseases 2005 192 3 510 519 2-s2.0-22544457161 10.1086/431520
    • (2005) Journal of Infectious Diseases , vol.192 , Issue.3 , pp. 510-519
    • Laoprasopwattana, K.1    Libraty, D.H.2    Endy, T.P.3    Nisalak, A.4    Chunsuttiwat, S.5    Vaughn, D.W.6    Reed, G.7    Ennis, F.A.8    Rothman, A.L.9    Green, S.10
  • 76
    • 1642415963 scopus 로고    scopus 로고
    • Relationship of preexisting dengue virus (DV) neutralizing antibody levels to viremia and severity of disease in a prospective cohort study of DV infection in Thailand
    • 2-s2.0-1642415963 10.1086/382280
    • Endy T. P., Nisalak A., Chunsuttitwat S., Vaughn D. W., Green S., Ennis F. A., Rothman A. L., Libraty D. H., Relationship of preexisting dengue virus (DV) neutralizing antibody levels to viremia and severity of disease in a prospective cohort study of DV infection in Thailand. Journal of Infectious Diseases 2004 189 6 990 1000 2-s2.0-1642415963 10.1086/382280
    • (2004) Journal of Infectious Diseases , vol.189 , Issue.6 , pp. 990-1000
    • Endy, T.P.1    Nisalak, A.2    Chunsuttitwat, S.3    Vaughn, D.W.4    Green, S.5    Ennis, F.A.6    Rothman, A.L.7    Libraty, D.H.8
  • 78
    • 84876797103 scopus 로고    scopus 로고
    • Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus
    • Liao H. X., Lynch R., Zhou T., Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. Nature 2013 496 469 476
    • (2013) Nature , vol.496 , pp. 469-476
    • Liao, H.X.1    Lynch, R.2    Zhou, T.3
  • 79
    • 79958863431 scopus 로고    scopus 로고
    • Selection of human anti-HIV broadly neutralizing antibodies occurs within the context of frozen 1F7-idiotypic repertoire
    • 2-s2.0-79958863431 10.1097/QAD.0b013e328347f9fa
    • Parsons M. S., Rouleau D., Routy J. P., Leblanc R., Grant M. D., Bernard N. F., Selection of human anti-HIV broadly neutralizing antibodies occurs within the context of frozen 1F7-idiotypic repertoire. AIDS 2011 25 10 1259 1264 2-s2.0-79958863431 10.1097/QAD.0b013e328347f9fa
    • (2011) AIDS , vol.25 , Issue.10 , pp. 1259-1264
    • Parsons, M.S.1    Rouleau, D.2    Routy, J.P.3    Leblanc, R.4    Grant, M.D.5    Bernard, N.F.6
  • 80
    • 43949157657 scopus 로고
    • Deceptive imprinting in the immune response against HIV-1
    • 2-s2.0-0028097587 10.1016/0167-5699(94)90192-9
    • Kohler H., Muller S., Nara P. L., Deceptive imprinting in the immune response against HIV-1. Immunology Today 1994 15 10 475 478 2-s2.0-0028097587 10.1016/0167-5699(94)90192-9
    • (1994) Immunology Today , vol.15 , Issue.10 , pp. 475-478
    • Kohler, H.1    Muller, S.2    Nara, P.L.3
  • 81
    • 0032211011 scopus 로고    scopus 로고
    • Deceptive imprinting: A cosmopolitan strategy for complicating vaccination
    • 2-s2.0-0032211011 10.1016/S0264-410X(98)00168-6
    • Nara P. L., Garrity R., Deceptive imprinting: a cosmopolitan strategy for complicating vaccination. Vaccine 1998 16 19 1780 1787 2-s2.0-0032211011 10.1016/S0264-410X(98)00168-6
    • (1998) Vaccine , vol.16 , Issue.19 , pp. 1780-1787
    • Nara, P.L.1    Garrity, R.2
  • 82
    • 0027205321 scopus 로고
    • A strategy for prophylactic vaccination against HIV
    • 2-s2.0-0027205321
    • Salk J., Bretscher P. A., Salk P. L., Clerici M., Shearer G. M., A strategy for prophylactic vaccination against HIV. Science 1993 260 5112 1270 1272 2-s2.0-0027205321
    • (1993) Science , vol.260 , Issue.5112 , pp. 1270-1272
    • Salk, J.1    Bretscher, P.A.2    Salk, P.L.3    Clerici, M.4    Shearer, G.M.5
  • 83
    • 0026776364 scopus 로고
    • Human monoclonal and polyclonal anti-human immunodeficiency virus-1 antibodies share a common clonotypic specificity
    • 2-s2.0-0026776364 10.1002/eji.1830220713
    • Wang H., Muller S., Zolla-Pazner S., Kohler H., Human monoclonal and polyclonal anti-human immunodeficiency virus-1 antibodies share a common clonotypic specificity. European Journal of Immunology 1992 22 7 1749 1755 2-s2.0-0026776364 10.1002/eji.1830220713
    • (1992) European Journal of Immunology , vol.22 , Issue.7 , pp. 1749-1755
    • Wang, H.1    Muller, S.2    Zolla-Pazner, S.3    Kohler, H.4
  • 84
    • 84869190870 scopus 로고    scopus 로고
    • Broad-range neutralizing anti-influenza A human monoclonal antibodies: New perspectives in therapy and prophylaxis
    • Clementi N., Criscuolo E., Castelli M., Clementi M., Broad-range neutralizing anti-influenza A human monoclonal antibodies: new perspectives in therapy and prophylaxis. New Microbiologica 2012 35 4 399 406
    • (2012) New Microbiologica , vol.35 , Issue.4 , pp. 399-406
    • Clementi, N.1    Criscuolo, E.2    Castelli, M.3    Clementi, M.4
  • 87
    • 80051670323 scopus 로고    scopus 로고
    • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins
    • Corti D., Voss J., Gamblin S. J., A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins. Science 2011 333 6044 850 856
    • (2011) Science , vol.333 , Issue.6044 , pp. 850-856
    • Corti, D.1    Voss, J.2    Gamblin, S.J.3
  • 88
    • 0035701421 scopus 로고    scopus 로고
    • A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1
    • 2-s2.0-0035701421 10.1089/08892220152741450
    • Stiegler G., Kunert R., Purtscher M., Wolbank S., Voglauer R., Steindl F., Katinger H., A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1. AIDS Research and Human Retroviruses 2001 17 18 1757 1765 2-s2.0-0035701421 10.1089/08892220152741450
    • (2001) AIDS Research and Human Retroviruses , vol.17 , Issue.18 , pp. 1757-1765
    • Stiegler, G.1    Kunert, R.2    Purtscher, M.3    Wolbank, S.4    Voglauer, R.5    Steindl, F.6    Katinger, H.7
  • 89
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker L. M., Phogat S. K., Chan-Hui P. Y., Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 2010 326 285 289
    • (2010) Science , vol.326 , pp. 285-289
    • Walker, L.M.1    Phogat, S.K.2    Chan-Hui, P.Y.3
  • 90
    • 69149083668 scopus 로고    scopus 로고
    • Neutralizing antibodies generated during natural HIV-1 infection: Good news for an HIV-1 vaccine?
    • 2-s2.0-66449106428 10.1038/nm.1949
    • Stamatatos L., Morris L., Burton D. R., Mascola J. R., Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine? Nature Medicine 2009 15 866 870 2-s2.0-66449106428 10.1038/nm.1949
    • (2009) Nature Medicine , vol.15 , pp. 866-870
    • Stamatatos, L.1    Morris, L.2    Burton, D.R.3    Mascola, J.R.4
  • 91
  • 92
    • 0027985431 scopus 로고
    • Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody
    • Burton D. R., Pyati J., Koduri R., Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 1994 266 1024 1027
    • (1994) Science , vol.266 , pp. 1024-1027
    • Burton, D.R.1    Pyati, J.2    Koduri, R.3
  • 93
    • 65749107719 scopus 로고    scopus 로고
    • HIV-1 and influenza antibodies: Seeing antigens in new ways
    • 2-s2.0-65749107719 10.1038/ni.1746
    • Kwong P. D., Wilson I. A., HIV-1 and influenza antibodies: seeing antigens in new ways. Nature Immunology 2009 10 6 573 578 2-s2.0-65749107719 10.1038/ni.1746
    • (2009) Nature Immunology , vol.10 , Issue.6 , pp. 573-578
    • Kwong, P.D.1    Wilson, I.A.2
  • 95
    • 0032947286 scopus 로고    scopus 로고
    • Protection of macaques against pathogenic simian/humanimmunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies
    • Mascola J. R., Lewis M. G., Stiegler G., Protection of macaques against pathogenic simian/humanimmunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies. Journal of Virology 1999 73 4009 4018
    • (1999) Journal of Virology , vol.73 , pp. 4009-4018
    • Mascola, J.R.1    Lewis, M.G.2    Stiegler, G.3
  • 97
    • 84870562234 scopus 로고    scopus 로고
    • HIV therapy by a combination of broadly neutralizing antibodies in humanized mice
    • Klein F., Halper-Stromberg A., Horwitz J. A., HIV therapy by a combination of broadly neutralizing antibodies in humanized mice. Nature 2012 492 7427 118 122
    • (2012) Nature , vol.492 , Issue.7427 , pp. 118-122
    • Klein, F.1    Halper-Stromberg, A.2    Horwitz, J.A.3
  • 98
    • 84863269120 scopus 로고    scopus 로고
    • HIV-1 neutralization coverage is improved by combining monoclonal antibodies that target independent epitopes
    • Doria-Rose N. A., Louder M. K., Yang Z., HIV-1 neutralization coverage is improved by combining monoclonal antibodies that target independent epitopes. Journal of Virology 2012 86 6 3393 3397
    • (2012) Journal of Virology , vol.86 , Issue.6 , pp. 3393-3397
    • Doria-Rose, N.A.1    Louder, M.K.2    Yang, Z.3
  • 101
    • 0033119374 scopus 로고    scopus 로고
    • Neutralizing antibodies have limited effects on the control of established HIV-1 infection in vivo
    • 2-s2.0-0033119374 10.1016/S1074-7613(00)80043-6
    • Poignard P., Sabbe R., Picchio G. R., Wang M., Gulizia R. J., Katinger H., Parren P. W. H. I., Mosier D. E., Burton D. R., Neutralizing antibodies have limited effects on the control of established HIV-1 infection in vivo. Immunity 1999 10 4 431 438 2-s2.0-0033119374 10.1016/S1074-7613(00)80043-6
    • (1999) Immunity , vol.10 , Issue.4 , pp. 431-438
    • Poignard, P.1    Sabbe, R.2    Picchio, G.R.3    Wang, M.4    Gulizia, R.J.5    Katinger, H.6    Parren, P.W.H.I.7    Mosier, D.E.8    Burton, D.R.9
  • 104
    • 77953760056 scopus 로고    scopus 로고
    • Antibody-mediated modulation of immune responses
    • Nimmerjahn F., Ravetch J. V., Antibody-mediated modulation of immune responses. Immunological Reviews 2010 236 265 275
    • (2010) Immunological Reviews , vol.236 , pp. 265-275
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 106
    • 84865295305 scopus 로고    scopus 로고
    • Topical gel formulation of broadly neutralizing anti-HIV-1 monoclonal antibody VRC01 confers protection against HIV-1 vaginal challenge in a humanized mouse model
    • Veselinovic M., Neff C. P., Mulder L. R., Akkina R., Topical gel formulation of broadly neutralizing anti-HIV-1 monoclonal antibody VRC01 confers protection against HIV-1 vaginal challenge in a humanized mouse model. Virology 2012 432 2 505 510
    • (2012) Virology , vol.432 , Issue.2 , pp. 505-510
    • Veselinovic, M.1    Neff, C.P.2    Mulder, L.R.3    Akkina, R.4
  • 107
    • 84875314771 scopus 로고    scopus 로고
    • A prospective randomized double blind placebo-controlled phase 1 pharmacokinetic and safety study of a vaginal microbicide gel containing three potent broadly neutralizing monoclonal antibodies (2F5, 2G12, 4E10) (MabGel)
    • Abstract LB1
    • Morris G., Chindove S., Woodhall S., A prospective randomized double blind placebo-controlled phase 1 pharmacokinetic and safety study of a vaginal microbicide gel containing three potent broadly neutralizing monoclonal antibodies (2F5, 2G12, 4E10) (MabGel). Microbicides 2010 Abstract LB1
    • (2010) Microbicides
    • Morris, G.1    Chindove, S.2    Woodhall, S.3
  • 108
    • 74249104684 scopus 로고    scopus 로고
    • Targeting trojan horse leukocytes for hiv prevention
    • 2-s2.0-74249104684 10.1097/QAD.0b013e32833424c8
    • Anderson D. J., Politch J. A., Nadolski A. M., Blaskewicz C. D., Pudney J., Mayer K. H., Targeting trojan horse leukocytes for hiv prevention. AIDS 2010 24 2 163 187 2-s2.0-74249104684 10.1097/QAD.0b013e32833424c8
    • (2010) AIDS , vol.24 , Issue.2 , pp. 163-187
    • Anderson, D.J.1    Politch, J.A.2    Nadolski, A.M.3    Blaskewicz, C.D.4    Pudney, J.5    Mayer, K.H.6
  • 110
    • 84859044775 scopus 로고    scopus 로고
    • Transmembrane domain membrane proximal external region but not surface unit-directed broadly neutralizing HIV-1 antibodies can restrict dendritic cell-mediated HIV-1 trans-infection
    • Sagar M., Akiyama H., Etemad B., Ramirez N., Freitas I., Gummuluru S., Transmembrane domain membrane proximal external region but not surface unit-directed broadly neutralizing HIV-1 antibodies can restrict dendritic cell-mediated HIV-1 trans-infection. Journal of Infectious Diseases 2012 205 8 1248 1257
    • (2012) Journal of Infectious Diseases , vol.205 , Issue.8 , pp. 1248-1257
    • Sagar, M.1    Akiyama, H.2    Etemad, B.3    Ramirez, N.4    Freitas, I.5    Gummuluru, S.6
  • 114
    • 79952924019 scopus 로고    scopus 로고
    • Rozrolimupab, symphobodies against rhesus D, for the potential prevention of hemolytic disease of the newborn and the treatment of idiopathic thrombocytopenic purpura
    • 2-s2.0-79952924019
    • Stasi R., Rozrolimupab, symphobodies against rhesus D, for the potential prevention of hemolytic disease of the newborn and the treatment of idiopathic thrombocytopenic purpura. Current Opinion in Molecular Therapeutics 2010 12 6 734 740 2-s2.0-79952924019
    • (2010) Current Opinion in Molecular Therapeutics , vol.12 , Issue.6 , pp. 734-740
    • Stasi, R.1
  • 116
    • 1542572660 scopus 로고    scopus 로고
    • Pathogen-specific recombinant human polyclonal antibodies: Biodefence applications
    • 2-s2.0-1542572660 10.1517/14712598.4.3.387
    • Bregenholt S., Haurum J., Pathogen-specific recombinant human polyclonal antibodies: biodefence applications. Expert Opinion on Biological Therapy 2004 4 3 387 396 2-s2.0-1542572660 10.1517/14712598.4.3.387
    • (2004) Expert Opinion on Biological Therapy , vol.4 , Issue.3 , pp. 387-396
    • Bregenholt, S.1    Haurum, J.2
  • 117
    • 33744777491 scopus 로고    scopus 로고
    • Recombinant human polyclonal antibodies: A new class of therapeutic antibodies against viral infections
    • 2-s2.0-33744777491 10.2174/138161206777442173
    • Bregenholt S., Jensen A., Lantto J., Hyldig S., Haurum J. S., Recombinant human polyclonal antibodies: a new class of therapeutic antibodies against viral infections. Current Pharmaceutical Design 2006 12 16 2007 2015 2-s2.0-33744777491 10.2174/138161206777442173
    • (2006) Current Pharmaceutical Design , vol.12 , Issue.16 , pp. 2007-2015
    • Bregenholt, S.1    Jensen, A.2    Lantto, J.3    Hyldig, S.4    Haurum, J.S.5
  • 120
    • 33749044654 scopus 로고    scopus 로고
    • Development of recombinant human polyclonal antibodies for the treatment of complex human diseases
    • 2-s2.0-33749044654 10.1517/14712598.6.9.905
    • Tolstrup A. B., Frandsen T. P., Bregenholt S., Development of recombinant human polyclonal antibodies for the treatment of complex human diseases. Expert Opinion on Biological Therapy 2006 6 9 905 912 2-s2.0-33749044654 10.1517/14712598.6.9.905
    • (2006) Expert Opinion on Biological Therapy , vol.6 , Issue.9 , pp. 905-912
    • Tolstrup, A.B.1    Frandsen, T.P.2    Bregenholt, S.3
  • 122
    • 33847613926 scopus 로고    scopus 로고
    • Process economics of industrial monoclonal antibody manufacture
    • 2-s2.0-33847613926 10.1016/j.jchromb.2006.07.037
    • Farid S. S., Process economics of industrial monoclonal antibody manufacture. Journal of Chromatography B 2007 848 1 8 18 2-s2.0-33847613926 10.1016/j.jchromb.2006.07.037
    • (2007) Journal of Chromatography B , vol.848 , Issue.1 , pp. 8-18
    • Farid, S.S.1
  • 123
    • 4043140159 scopus 로고    scopus 로고
    • Detection of anti-type 3 muscarinic acetylcholine receptor autoantibodies in the sera of Sjögren's syndrome patients by use of a transfected cell line assay
    • 2-s2.0-4043140159 10.1002/art.20371
    • Gao J., Cha S., Jonsson R., Opalko J., Peck A. B., Detection of anti-type 3 muscarinic acetylcholine receptor autoantibodies in the sera of Sjögren's syndrome patients by use of a transfected cell line assay. Arthritis and Rheumatism 2004 50 8 2615 2621 2-s2.0-4043140159 10.1002/art.20371
    • (2004) Arthritis and Rheumatism , vol.50 , Issue.8 , pp. 2615-2621
    • Gao, J.1    Cha, S.2    Jonsson, R.3    Opalko, J.4    Peck, A.B.5
  • 126
    • 77953980755 scopus 로고    scopus 로고
    • Production of pharmaceutical-grade recombinant aprotinin and a monoclonal antibody product using plant-based transient expression systems
    • Pogue G. P., Vojdani F., Palmer K. E., Production of pharmaceutical-grade recombinant aprotinin and a monoclonal antibody product using plant-based transient expression systems. Plant Biotechnology Journal 2010 8 5 638 654
    • (2010) Plant Biotechnology Journal , vol.8 , Issue.5 , pp. 638-654
    • Pogue, G.P.1    Vojdani, F.2    Palmer, K.E.3
  • 128
    • 78650656127 scopus 로고    scopus 로고
    • Fc-glycosylation influences Fc γ receptor binding and cell-mediated anti-HIV activity of monoclonal antibody 2G12
    • Forthal D. N., Gach J. S., Landucci G., Jez J., Strasser R., Kunert R., Steinkellner H., Fc-glycosylation influences Fc γ receptor binding and cell-mediated anti-HIV activity of monoclonal antibody 2G12. Journal of Immunology 2010 185 11 6876 6882
    • (2010) Journal of Immunology , vol.185 , Issue.11 , pp. 6876-6882
    • Forthal, D.N.1    Gach, J.S.2    Landucci, G.3    Jez, J.4    Strasser, R.5    Kunert, R.6    Steinkellner, H.7
  • 129
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • 2-s2.0-34247122497 10.1146/annurev.immunol.25.022106.141702
    • Arnold J. N., Wormald M. R., Sim R. B., Rudd P. M., Dwek R. A., The impact of glycosylation on the biological function and structure of human immunoglobulins. Annual Review of Immunology 2007 25 21 50 2-s2.0-34247122497 10.1146/annurev.immunol.25.022106.141702
    • (2007) Annual Review of Immunology , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 130
    • 84876531530 scopus 로고    scopus 로고
    • Prophylactic and therapeutic testing of Nicotiana-derived RSV-neutralizing human monoclonal antibodies in the cotton rat model
    • Zeitlin L., Bohorov O., Bohorova N., Prophylactic and therapeutic testing of Nicotiana-derived RSV-neutralizing human monoclonal antibodies in the cotton rat model. Monoclonal Antibodies 2013 5 2
    • (2013) Monoclonal Antibodies , vol.5 , Issue.2
    • Zeitlin, L.1    Bohorov, O.2    Bohorova, N.3
  • 131
    • 84877618448 scopus 로고    scopus 로고
    • Delineating antibody recognition in polyclonal sera from patterns of HIV-1 isolate neutralization
    • Georgiev I. S., Doria-Rose N. A., Zhou T., Delineating antibody recognition in polyclonal sera from patterns of HIV-1 isolate neutralization. Science 2013 340 6133 751 756
    • (2013) Science , vol.340 , Issue.6133 , pp. 751-756
    • Georgiev, I.S.1    Doria-Rose, N.A.2    Zhou, T.3
  • 132
    • 27744441119 scopus 로고    scopus 로고
    • Neutralization of HIV-1 primary isolate by ELDKWA-specific murine monoclonal antibodies
    • 2-s2.0-27744441119 10.1016/j.imbio.2005.05.025
    • Zhang G., Lu H., Lu Y., Jiang S., Chen Y. H., Neutralization of HIV-1 primary isolate by ELDKWA-specific murine monoclonal antibodies. Immunobiology 2005 210 9 639 645 2-s2.0-27744441119 10.1016/j.imbio.2005.05.025
    • (2005) Immunobiology , vol.210 , Issue.9 , pp. 639-645
    • Zhang, G.1    Lu, H.2    Lu, Y.3    Jiang, S.4    Chen, Y.H.5
  • 133
    • 0028235930 scopus 로고
    • Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS
    • 2-s2.0-0028235930
    • Muster T., Guinea R., Trkola A., Purtscher M., Klima A., Steindl F., Palese P., Katinger H., Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS. Journal of Virology 1994 68 6 4031 4034 2-s2.0-0028235930
    • (1994) Journal of Virology , vol.68 , Issue.6 , pp. 4031-4034
    • Muster, T.1    Guinea, R.2    Trkola, A.3    Purtscher, M.4    Klima, A.5    Steindl, F.6    Palese, P.7    Katinger, H.8
  • 134
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker L. M., Huber M., Doores K. J., Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 2011 477 7365 466 470
    • (2011) Nature , vol.477 , Issue.7365 , pp. 466-470
    • Walker, L.M.1    Huber, M.2    Doores, K.J.3
  • 135
    • 84866493348 scopus 로고    scopus 로고
    • Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
    • Huang J., Ofek G., Laub L., Broad and potent neutralization of HIV-1 by a gp41-specific human antibody. Nature 2012 491 7424 406 412
    • (2012) Nature , vol.491 , Issue.7424 , pp. 406-412
    • Huang, J.1    Ofek, G.2    Laub, L.3
  • 136
    • 84879115266 scopus 로고    scopus 로고
    • Cross-group neutralization of HIV-1 and evidence for conservation of the PG9/PG16 epitopes within divergent groups
    • Braibant M., Gong E. Y., Plantier J. C., Moreau T., Alessandri E., Simon F., Barin F., Cross-group neutralization of HIV-1 and evidence for conservation of the PG9/PG16 epitopes within divergent groups. AIDS 2013
    • (2013) AIDS
    • Braibant, M.1    Gong, E.Y.2    Plantier, J.C.3    Moreau, T.4    Alessandri, E.5    Simon, F.6    Barin, F.7
  • 137
    • 80052938385 scopus 로고    scopus 로고
    • Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors
    • Bonsignori M., Hwang K. K., Chen X., Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors. Journal of Virology 2011 19 9998 10009
    • (2011) Journal of Virology , Issue.19 , pp. 9998-10009
    • Bonsignori, M.1    Hwang, K.K.2    Chen, X.3
  • 139
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X., Yang Z. Y., Li Y., Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 2010 329 856 861
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1    Yang, Z.Y.2    Li, Y.3
  • 140
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid J. F., Mouquet M., Ueberheide B., Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 2011 333 6049 1633 1637
    • (2011) Science , vol.333 , Issue.6049 , pp. 1633-1637
    • Scheid, J.F.1    Mouquet, M.2    Ueberheide, B.3
  • 141
    • 82755184131 scopus 로고    scopus 로고
    • Increasing the potency and breadth of an HIV antibody by using structure-based rational design
    • Diskin R., Scheid J. F., Marcovecchio P. M., Increasing the potency and breadth of an HIV antibody by using structure-based rational design. Science 2011 334 6060 1289 1293
    • (2011) Science , vol.334 , Issue.6060 , pp. 1289-1293
    • Diskin, R.1    Scheid, J.F.2    Marcovecchio, P.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.